Skip to main content
NCBI home page
Journal of Food Science and Technology logoLink to Journal of Food Science and Technology
. 2020 Jan 4;57(8):2771–2785. doi: 10.1007/s13197-019-04222-6

Effect of wheat grain protein composition on end-use quality

Ambika Sharma 1,#, Sheenu Garg 1,#, Imran Sheikh 1, Pritesh Vyas 1,✉, H S Dhaliwal 1,✉
PMCID: PMC7316921  PMID: 32624587

Abstract

The quality of wheat products has been a new challenge next to wheat production which was achieved substantially during green revolution. The end-use quality of wheat is an essential factor for its commercial demand. The quality of wheat is largely based on the wheat storage proteins which extensively influences the dough properties. High molecular weight glutenin subunits (HMWGS), low molecular weight glutenin subunits (LMWGS) and gliadins significantly influence the end-use quality. Genomics and proteomics study of these gluten proteins of bread and durum wheat have explored new avenues for precise identification of the alleles and their role in end-use quality improvement. Secalin protein of Secale cereale encoded by Sec-1 loci and is associated with 1RS.1BL translocation has been known for deterioration of end-use quality. Chromosomal manipulations using various approaches have led to the development of new recombinant lines of wheat without secalin. Advanced techniques associated with assessment of end-use quality have integrated the knowledge of useful or deteriorating HMWGS/LMWGS alleles and their potential role in end-use quality. This review gives a comprehensive insight of different aspects of the end-use quality perspective for bread making in wheat along with some information on the immunological interference of gluten in celiac disease.

Keywords: Gluten, End-use quality, 1RS.1BL translocation, Secalin, Celiac disease

Introduction

Wheat significantly contributes to the nourishment of humans and has been grown in various environments around the world (Kiszonas and Morris 2018). The growing population has increased the need for wheat-based products as a result of which a focus on the end-use quality is very much essential. Wheat flour is used in various products such as bread, pasta, noodles and biscuits (Žilić et al. 2011). The two main types of wheat are: hexaploid wheat (Triticum aestivum L.), which comprises of about 95%, and tetraploid durum wheat (Triticum durum), which accounts for the rest 5% of total world wheat produce. These two types of wheat differ in their genetic constitution, grain composition and their end-use quality (Peña et al. 2002).

As per the guidance document of Food Safety and Standards of India 2015, in India Chapati, bread and biscuits are most popular products covering 80% of the total market. Around 2000 organized and 10,000,000 unorganized sectors in India produce 1.3 million tonnes and 1.7 million tonnes of bakery products, respectively. The market size of bakery was estimated worth US$ 7.6 billion in 2015 in India. According to Euromonitor International data the total retail sales of the world’s bread market was US$170 billion in 2006 which reached to US$220 billion in 2011. According to the global bakery product market- Growth, Trends and Forecast, 2017–2022 the total market size of the bakery products will reach US$ 530 billion by 2021 at a 4.5% CGAR during the forecast period.

In recent years, breeding through wide hybridization and selection of progenies with better end-use quality traits have been shifted from phenotyping to genetic approaches for selecting superior traits. In addition to the focus on higher yield, rust resistance and drought tolerance, end-use quality parameters also require attention and need to be analyzed because the wheat quality is primarily meant for the bread making quality. Consequently, most of the present studies are primarily focused at identifying useful dough properties which are suitable for improved end-use quality. Development of new wheat varieties with high quality requires deeper understanding of traits for better end-use quality (Kiszonas and Morris 2018).

Seed storage proteins are the major determinants influencing the end-use quality and manufacturing of various wheat based products (Kaur et al. 2016). Basically, the wheat storage protein, gluten is responsible for determining the different rheological properties of dough (Branković et al. 2018). A strong association between bread making and gluten content has been analyzed with the help of various bread baking tests. The separation of gluten protein into its various components has provided major clues for advanced research in molecular breeding and better selection of desired traits for improved gluten quality (Kiszonas and Morris 2018). Gliadins and glutenins components of gluten proteins are responsible for its dough rheological properties (Fleitas et al. 2018). The glutenin proteins are linked by disulfide bonds and are classified in two categories which are referred to as high molecular weight glutenin subunits (HMWGS) and low molecular weight glutenin subunits (LMWGS). The amount of HMWGS and LMWGS along with allelic pattern of gluten is highly corroborated with end-use quality (Sherman et al. 2018).

The end-use quality deterioration is one of the major aspects which need to be considered during improvement of wheat cultivars. Allelic patterns of HMWGS and LMWGS have different roles in gluten complex formation influencing the end-use quality. The absence of D genome in Triticum durum leads to its deprivation of some very significant alleles responsible for better bread making quality. However durum wheat is very useful for pasta making due to its grain hardess (Wrigley 2009). Various alien introgressions from novel sources providing biotic and abiotic resistance in wheat have adversely affected the wheat quality. The most common introgression is 1RS.1BL translocation in which short arm of wheat (1BS) chromosome is replaced by short arm of rye (1RS) chromosome. It is known for better root traits, enhanced agronomic performance and providing multiple disease resistance in wheat but on the other hand 1RS deteriorates bread making quality because of the rye storage protein secalin and the absence of Glu-B3/Gli-B1 on 1BS (Kiszonas and Morris 2018; Graybosch 2001).

Numerous attempts have been made to improve the end-use quality of wheat. In 1RS.1BL translocation, secalin was eliminated and introgression of Glu-B3/Gli-B1 loci from wheat (Lukaszewski 2000; Howell et al. 2014) was done. The quality of durum wheat has been improved by chromosomal manipulations through addition and substitution of 1D chromosome (Lukaszewski 2003). Important effects of HMWGS have been studied and utilized as essential parameters for better end-use quality. Although HMWGS significantly affects the bread making quality but LMWGS and gliadins also affect the gluten complex formation (Tanaka et al. 2000). Over-expression of the HMWGS allele Glu1-Bx7 subunit (Bx7OE) in wheat genotypes was strongly correlated with enhanced dough quality (Cho et al. 2017).

The end-use quality of wheat cultivars can be analyzed by different techniques. Farinograph, extensiograph, mixograph and micro-SDS sedimentation test (MST) have been used extensively in the cereal research laboratories to check the quality parameters such as the dough consistency, viscosity, hardiness, texture and thus are used in flour quality control (Hadnađev et al. 2013). The MST is one of the simplest and important techniques used to check the flour quality for bread making process. Protein content is a significant parameter in grain quality assessment and its relation with wet gluten affects the quality of common flour which is a pre-requisite for consumers. Celiac disease (CD) is one of the major drawbacks of the gluten based food products. The mechanism behind this disease is the hypersensitivity of the host body against the gluten which consequently damages the intestinal tissues. It also has a relationship with type I diabetes and autoimmune thyroid disease. Gluten free food products have been the only remedy till date for these kind of disorders (Nijhawan and Goyal 2015).

Classification of wheat storage proteins

The classification of the wheat storage proteins is based on their solubility as the gluten and the non-gluten proteins (Fig. 1).

Fig.1.

Fig.1

Open in a new tab

The classificiation and nomenclature of wheat storage proteins

Non-gluten proteins

The non-gluten proteins account for 20–25% of the total cereal grain protein and the majority of them are monomeric (Merlino et al. 2009). Molecular weights of these proteins are usually below 25 KDa, although a significant proportion has molecular weight between 60–70 KDa. The albumins and globulins have high content of K, W and M amino acids (Žilić et al. 2011). They significantly influence the texture and crumb grain properties of the bread (Caballero et al. 2007).

Gluten proteins

These are also called as prolamins as they have proportion of amino acids P and D as their structural components (Barak et al. 2015). The proteins are cross linked in wheat gluten and form networks through the rapid formation of protein matrix (Kiszonas and Morris 2018). Bread making quality is highly affected by the type and amount of gluten proteins (Fig. 2). Gluten significantly determines the elasticity of dough and the end-use properties of cereal based products (Barak et al. 2013). Gluten quality has been considered to be the most important quality parameter for wheat flakes, because gluten protein (water-insoluble protein complex) gives wheat dough a unique viscoelastic property (Guo et al. 2018). The viscoelastic property of wheat flakes is lost due to the elimination of gluten proteins. Gluten index i.e. ratio of glutenin and gliadins is a significant parameter for measuring bread making quality as more is the gluten index better is bread making quality. This seems to be contrasting for chapatti making as gluten index has negative influence on the chapatti score (Kumar et al. 2018).

Fig. 2.

Fig. 2

Open in a new tab

Factors affecting rheology and bread-making characteristics of wheat

Glutens are characteristically separated into two components: the gliadins and the glutenin. Gliadins act as softening agents for glutenins which increases the viscosity of the gluten complex and reduces the increased levels of elasticity of glutenins (Guo et al. 2018). Monomeric gliadins, which impart viscous flow and ductility to the dough and the polymeric glutenins determine the viscoelasticity of the dough and play pivotal role in determining the end-use quality (Payne 1987). The functional and rheological properties of dough relies on the ratio of glutenin/gliadin, ratio of high/low glutenin polypeptide, gliadin binding strength to glutenins, size and structure of glutenin polypeptides (Barak et al. 2015).

Gliadins

Gliadins are heterogeneous polypeptide mixtures and comprise of approximately 50% of the total gluten (Pattison 2013). They are classified into four classes: α, β, γ and ω in which α and β gliadins has been grouped together as one class, due to similarity in their structure, i.e. the α-type gliadins (Barak et al. 2015). Hydrated gliadins play important part in determination of viscosity and ductility of the dough (Pattison 2013).

Glutenins

Glutenins are polymers that consist of protein subunits, linked by disulfide bonds between the chains, i.e. HMWGS and LMWGS (Pattison 2013). The LMWGS are the main constituents of the storage protein and comprise 60% of the wheat seed storage protein (Table 1). It has been mentioned that LMWGS are the significant fraction of the large gluten network which impart elasticity and ductility to the dough. LMWGS are further classified into: LMW-m, LMW-s and LMW-i, following the first amino acid residue of their mature proteins, M, S and I respectively. Because of their importance for the quality of wheat flour and the difficulty of distinguishing their alleles with PAGE, allele specific molecular markers have been used to determine various LMWGS alleles (Si et al. 2013).

Table 1.

Properties of glutenin and gliadins proteins

Sr.No Group Total fraction of protein content (%) Structure Molecular weight (KDa)
1 HMWGS 10–20 Polymeric 65–90
2 LMWGS 70–80 Polymeric 30–45
3 α-gliadins 70–80 Monomeric 30–45
4 β-gliadins 70–80 Monomeric 30–45
5 γ-gliadins 70–80 Monomeric 30–45
6 ω-gliadins 10–20 Monomeric 40–75
Open in a new tab

Role of HMWGS and LMWGS alleles in end-use quality

The HMWGS and LMWGS are significant components of the wheat gluten network for determining the end-use quality. HMWGS, encoded by the Glu-1 loci present on the long arms of 1A, 1B and 1D chromosomes are referred to as Glu-A1, Glu-B1 and Glu-D1 (Lombardo et al. 2017). The genes coding for LMWGS are present on the short arm of 1A, 1B, and 1D chromosome encoded by Glu-3 referred to as Glu-A3, Glu-B3 and Glu-D3 loci which are closely linked to the Gli-1 locus encoding gliadins (Macharia et al. 2014). Allelic variation of HMWGS and LMWGS strongly influences the end-use quality (Payne 1987).

High molecular weight glutenin subunit (HMWGS)

The HMWGS are a group of storage proteins which are deposited in the endosperm of wheat during grain filling. The HMWGS forms both inter and intramolecular disulphide bonds with other HMWGS and LMWGS. These loci are highly polymorphic in nature and these allelic variations have been responsible for different combinations of HMWGS in various wheat varieties (Rasheed et al. 2012). Various alleles encoding HMWGS and their effect on end-use quality of wheat have been reported (Payne 1987). The combinations of different HMWGS alleles determine end-use quality based on the Glu-1 score rating system (Table 2) used in different studies (Rasheed et al. 2012). The highest frequency of occurrence of HMWGS Glu-A1(2*), Glu-B1(7 + 8), (7 + 9), (17 + 18), (20) and Glu-D1(5 + 10), (2 + 12) are present in many of the wheat genotypes worldwide. Better bread is attributed to superior high molecular weight subunits such as Glu-A1(1)/(2*), Glu-B1(7 + 8)/(7 + 9)/ (17 + 18) and Glu-D1(5 + 10) and the poor bread making cultivars generally have inferior high molecular subunits like Glu-A1(null), Glu-B1(6 + 8)/(13 + 16)/(20)/(22) and Glu-D1(2 + 12) (Gálová et al. 2002; Bakshi and Bhagwat 2016; Filip 2018). Glu-A1(1)/(2*) is associated with improved dough quality than to Glu-A1(null) allele. Glu-B1(7 + 8), (7 + 9) and (17 + 18) positively affect the end-use quality and have high Glu-1 scores (Table 2).

Table 2.

Glu-1 scores of different combinations of HMWGS (Glu-A1, Glu-B1 and Glu-D1)

S. No Glu-A1 Glu-B1 Glu-D1 Glu-1 score Reference
1 1 7 5 + 10 8 Nakamura (2000)
2 1 7 2 + 12 6
3 1 7 + 8 5 + 10 10
4 1 7 + 8 2 + 12 8
5 1 7 + 8 3 + 12 8
6 2 ∗  7 2 + 12 6
7 2 ∗  7 5 + 10 8
8 2 ∗  7 + 8 2 + 12 8
9 2 ∗  7 + 9 2 + 12 7
10 2 ∗  6 + 8 2 + 12 6
11 2 ∗  13 + 16 2 + 12 8
12 Null 7 2 + 12 4
13 Null 7 4 + 12 3
14 Null 7 5 + 10 6
15 Null 7 + 8 2 + 12 6
16 Null 7 + 8 3 + 12 6
17 Null 7 + 8 4 + 12 5
18 Null 7 + 8 5 + 10 8
19 Null 7 + 9 2 + 12 5
20 Null 7 + 9 3 + 12 5
21 Null 6 + 8 2 + 12 4
22 Null 13 + 16 2 + 12 6
23 Null 17 + 18 2 + 12 6
24 2* 7 + 8 5 + 10 10 Gálová et al. (2002)
25 2* 17 + 18 5 + 10 10
26 2* 7 + 9 5 + 10 9
27 2* 7 5 + 10 8
28 Null 7 + 8 2 + 12 6
29 Null 13 + 16 2 + 12 4
30 1 7 + 8 5 + 10 10 Gianibelli et al. (2002)
31 1 7 + 8 2 + 12 8
32 Null 7 + 8 5 + 10 8
33 – – 5 + 10 8 Osman et al. (2012)
34 1 17 + 18 – 6
35 1 7 + 8 – 6
36 1 7 + 9 – 6
37 2* 17 + 18 – 6
38 2* 7 + 9 – 6
39 – 7 2 + 12 4
40 – 6 + 8 4 + 12 4
41 0 7 + 9 5 + 10 7 Chňapek et al. (2015)
42 0 7 + 8 5 + 10 8
43 0 7 + 8 2 + 12 6
44 0 7 + 9 2 + 12 5
45 0 6 + 8 5 + 10 6
46 1 7 + 9 5 + 10 9
47 1 7 + 9 2 + 12 7
48 1 7 + 9 3 + 12 7
49 1 20 5 + 10 8
50 1 14 + 15 5 + 10 8
51 2* 7 + 8 5 + 10 10
52 2* 7 + 9 5 + 10 9
53 2* 17 + 18 5 + 10 10 Bakshi and Bhagwat (2016)
54 2* 7 + 9 5 + 10 9
55 2* 7 + 8 2 + 12 8
56 2* 17 + 18 2 + 12 8
57 2* 7 + 9 2 + 12 7
58 2* 20 2 + 12 6
59 1 17 + 18 5 + 10 10
60 1 7 + 9 5 + 10 9
61 1 7 5 + 10 8
62 1 20 5 + 10 8
63 1 17 + 18 2 + 12 8
64 1 20 2 + 12 6
65 Null 17 + 18 2 + 12 6
66 Null 7 + 9 2 + 12 5
67 Null 20 2 + 12 4
68 Null 13 + 19 2 + 12 –
69 – 7 + 9 5 + 10 9 Filip (2018)
70 – 22 5 + 10 8
71 – 20 2 + 12 4
Open in a new tab

HMWGS Glu-D1 (5 + 10) have positive influence on the gluten strength than the HMWGS Glu-D1(2 + 12) which deteriorate the end-use quality (Barak et al. 2013). Glu-B1(7 + 8) showed high Glu-1 score along with HMWGS Glu-D1(5 + 10) while Glu-1 score got decreased with HMWGS Glu-D1(2 + 12) (Table 2). It is considered that Glu-D1(4 + 12) pair has the lowest influence on the sedimentation volume (Giraldo et al. 2010). Previous reports suggest that the contribution of Glu-A1 to gluten quality is affected by Glu-B1 and Glu-D1. Glu-1Ay subunit although is inactive in most of the bread wheat cultivars (Yu et al. 2019) but in Australian wheat cultivars Glu-1Ay is found to have significant effect in improving end-use quality (Roy et al. 2018). Introgression of 1E-encoded storage protein from Agropyron elongatum also enhanced the bread making property of Chinese Spring (Garg et al. 2009). Glu-B1(17 + 18) had stronger influence on bread making quality as compared to Glu-B1(20). Glu-B1(6 + 8) also has negative impact on end-use quality but it is still better than Glu-B1(20) (Tanaka et al. 2000).

Low molecular weight glutenin subunit (LMWGS)

The LMWGS are essential in determining the gluten networking as they comprise of 1/3rd of the seed protein and more than half of the total glutenins (Garg et al. 2007). Although LMWGS also have pronounced effect on dough properties but they are less studied due to the complexity in their banding pattern because of overlapping with gliadins on SDS-PAGE. There are only few reports indicating the association of LMWGS with the end-use quality (Sharma et al. 2012). LMWGS have significant effect in deciding the dough properties in durum wheat. Glu-A3 and Glu-B3 with Glu-D1(5 + 10) allele are known for its positive effects on end-use quality. At Glu-A3 locus, the Glu-A3b and Glu-A3d enhance bread making quality whereas Glu-A3e contributes to a poor dough property. The Glu-B3b and Glu-B3g alleles at the Glu-B3 locus, highly contribute to the gluten complex and strongly affect the bread making quality. In case of Glu-D3 locus, Glu-D3b and Glu-D3a increase the dough strength (Ito et al. 2015). The LMWGS at the Glu-B3 locus lead to significant variance in the MST value of wheat, Glu-B3b, Glu-B3g and Glu-B3h increased the MST value and Glu-B3a, Glu-B3c and Glu-B3j reduced it (Si et al. 2013). Glu-B3 and Glu-D3 exerted significant effect on gluten strength measured by mixograph study (Sharma et al. 2012). The major bottleneck is the lack of information on LMWGS allele score which limits their utilization in various breeding programmes. However, with the development of molecular markers it is now possible to have undisputed classification of LMWGS alleles (Zhang et al. 2011).

Proteomics and genomics of gluten protein

Wheat quality is mainly defined by grain hardness and protein content. Molecular structure of the proteins determines the gluten networking, which is regulated by the mutual ionic interactions, and plays significant role during the bread making process (Gianibelli et al. 2001). The whole wheat protein profiling is shown in proteomics study with the 2D resolution followed by the separation of the individual components for identification. According to this study there are at least 1300 polypeptides and over 300 of which have been BLAST against the established protein database information recognized through N-terminal amino acid sequencing (Skylas et al. 2000).

HMWGS contain higher proportions of P, G and D with small fraction of K amino acids, comprises of two domains i.e. a central repetitive domain and two non-repetitive terminal domains mostly consisting of C amino acid residues (Shewry et al. 1992). The x-type repetitive domains of HMWGS represesnt a tripeptide motif GQQ and the central domains of y-type HMWGS exihibit second P residue in the GYYPTSPQQ repeat motif which is replaced by a L amino acid. β-turn conformation has been adopted by both the domains and has repetetive amino acid sequences (Tatham et al. 1990). The non-repetitive sequence of N-terminal region has 81 to 140 residues with 3–5 cysteine residues (Shewry et al. 1992). On the basis of the first 16 amino acids residues, minor variations such as E at 6th position in Dx-type and R in Dy-type subunits can be distinguished. The C residue is present at the position 10 in all HMWGS but in By7 subunit it is present at positions 12 and 14 (Anderson et al. 1991). The non-repetitive domain of C-terminus consists of 42 residues having one residue of cysteine (Gianibelli et al. 2001). Recently the advances of molecular biology for sequencing and cloning of several glutenin subunits enhance the understanding of these proteins.

Although the LMWGS are significant for end-use quality of wheat, a comprehensive information on the genes and encoded polypeptides is still lacking. Based on the first amino acid present at N-terminal region, 7 main types of LMWGS were identified in a study by Lew et al. (1992). According to the observation LMW-s are more in number than LMW-m beginning with SHIPGL and the later has METSHIPGL, METSRIPGL or METSCIPGL at its N-terminal (Lew et al. 1992). Abundance of β-turns in the repetitive domains at N-terminal region leads to spiral conformation whereas in non-repetitive domains α-helix leads to compact conformation. At the C-terminal domain of LMWGS there are seven cysteine residues including an unpaired one for intermolecular bonding (Thomson et al. 1992).

Electrophoresis of grain storage proteins is done to evaluate and distinguish many HMWGS alleles so far but it has also resulted in incorrect elucidation of allelic differences due to overlapping mobility of the subunits on gel (Gianibelli et al. 2001). The molecular markers are highly useful for gene identification and introgression of new genotypes with the help of marker assisted selection (MAS). The PCR based molecular markers have been developed based on the available HMWGS sequences which lead to the genotyping at early stages of plant growth (Lei et al. 2006). Recently, specific molecular markers were designed for HMWGS Glu-B1 locus and were applied in the durum and bread wheat cultivars which conclude that the integrated protein profiling and molecular data is required for HMWGS characterization to avoid allele misidentification in wheat genotypes. HMWGS Bx20 + By20 alleles are commonly found in durum wheat and several PCR based markers study has revealed allelic variation for them suggesting the possibility of sharing of different haplotypes by the genes (Janni et al. 2017). The molecular studies done by Zhang et al. (2011) has led to the characterization of almost all the LMWGS and thus integrating the protein profiling and molecular data.

Role of gluten in durum based products

Durum wheat (Triticum turgidum L. var. durum) has been grown on around 17 million hectares worldwide. Mediterranean basin is the largest durum producing area with highest consumers of durum wheat products. Canada, Italy, Turkey, USA, Morocco and Kazakhstan are the top durum wheat producing countries (Nazco et al. 2012). Mediterranean durum landraces have been known for their broad genetic variability, superior adaptation to semi-arid climates and resistance to disease, pests and abiotic stresses compared with bread wheat (Cakmak et al. 2010; Nazco et al. 2012; Boehm et al. 2017). Amongst the Mediterranean ecosystem, Morocco is well known for production of durum wheat which is grown over an area ranging from 1 to 1.2 million hectares annually (Zarkti et al. 2012). In Europe durum wheat is mainly used for pasta production whereas couscous and bread-making are the more important uses in northern Africa. Earlier most of the research has been done on the evaluation of pasta quality but recently bread, couscous and burghul making quality parameters of durum have also been considered. The improvement of durum wheat quality with the help of genetic approaches is becoming a main concern in Morocco to fulfill the consumers’ needs for durum bread and couscous (Amri et al. 2000). Durum wheat is the main choice for the production of pasta and couscous due to its high protein content and gluten characteristics. Durum wheat has a very hard kernel which is a major constraint in bread making quality (Morris et al. 2015). In durum wheat the capacity of semolina to form dough suitable for pasta production principally depends on the rheological properties of its gluten (Lerner et al. 2006). Protein content and sedimentation test are the parameters widely used to assess the quality of durum wheat. Durum wheat is considered unsuitable for the majority of commercial bread-baking operations and other end-use food products as compared to hexaploid bread wheat. Although both the wheats share the A and B genomes, the absence of the D genome in durum greatly affects its milling performance and end-use quality. Even the commonly used dough tests like the alveograph, extensograph, and farinograph often found durum gluten to be too inelastic and weak. The difference in bread making quality of durum wheat is associated with the allelic composition of HMWGS and LMWGS on Glu-B1 and Glu-B3 loci, respectively. HMWGS (7 + 8) and HMWGS (6 + 8) exhibit better dough properties than HMWGS (20) at Glu-B1 locus (Boehm et al. 2017). HMWGS (20) is highly distributed in durum wheat but its presence is associated with poor end use quality. 1Bx20 has a detrimental effect on dough strength as compared with subunit 1Bx7. These subunits are highly similar in their sequence and structure, the only major difference is the substitution of two cysteine residues in the N-terminal domain of subunit 1Bx20 by tyrosines. This substitution is responsible for the detrimental effect on dough strength by affecting the pattern of disulphide cross-links in the glutenin polymers (Shewry et al. 2003). Previous studies reported that the presence of LMW-1 (associated with γ-gliadin 42) and the absence of LMW-2 (associated with γ-gliadin 45) in durum wheat genotypes are associated with weak gluten, whereas the absence of LMW-1 and the presence of LMW-2 are associated with moderate to strong gluten. Bread making quality of soft durum wheat is highly dependent on the combination of favourable alleles for gluten strength. Flours produced from soft kernel durum wheat behave similarly to hexaploid bread wheat flours in terms of gluten strength and dough mixing characteristics (Boehm et al. 2017).

Durum wheat lacking D genome is the hardest of all wheats and has 9% to 18% protein. The D genome largely influences the dough rheology and thus affecting the end-use quality of wheat. Semolina durum is preferably utilized for making pasta due to its grain hardness (Wrigley 2009). In durum, LMWGS are the sulfur-rich subunits (Delcour et al. 2012) whose levels in a durum wheat cultivars are important for end-use products. LMW-m and-s type subunits are associated with good quality dough whereas poor quality has been found associated with α-and γ-gliadin content (D’Ovidio and Masci 2004). The protein plays a significant role in determining pasta properties as it forms a network during different downstream processing methods of pasta. Pasta drying is a sensitive procedure linked with quality deterioration which may lead to the loss of desirable qualities i.e. elasticity and rigidity (Delcour and Hoseney 2010). The degree of protein polymerization plays a significant role in determining pasta cooking quality (Delcour et al. 2012).

Effect of secalin on end-use quality

Triticale (X Triticosecale Wittmack) is an amphiploid having wheat (Triticum aestivum L.) and rye (Secale cereale L.) genomes (Mergoum et al. 2009). The ploidy level of triticale ranges from hexaploid (2n = 42 = AABBRR) to octaploid (2n = 56 = AABBDDRR) (Ayalew et al. 2018). Octaploid triticales (2n = 56 = AABBDDRR), derived from hexaploid wheat and rye, were the first to be developed in the early twentieth century but they did not spread as commercial cultivars. So in the early 1950s, the bulk of research has been focused on the development and improvement of hexaploid triticales due to their better adaptation and genomic stability than the octaploid triticale (Ammar et al. 2004).

The most successful and cultivated substituted triticale line with the 1RS.1BL translocation, known for their agronomic performance and abiotic stress tolerance has been extensively used in wheat breeding programs. However 1RS is associated with adverse effects on end-use quality of wheat because of the presence of Sec-1 locus on 1RS that encodes for secalin (Gellrich et al. 2003) and the loss of Glu-B3/Gli-B1 on 1BS. These two substitutions brought various changes in the protein composition which further led to sticky dough and reduced gluten strength which prevents their use in commercial bread preparation. The secalin proteins are monomeric in nature and they are highly soluble in water which leads to the formation of sticky dough (Graybosch 2001).

Attempts to overcome the end-use quality deterioration

Protein quality and quantity are important parameters in the variation of the end-use quality of wheat. Glu-B1(7 + 9)/(7 + 8)/(17 + 18) alleles along with Glu-D1(5 + 10) are considered to be the most favorable for bread making (Bakshi and Bhagwat 2016). Over-expression of the HMWGS allele Glu1-Bx7 subunit (Bx7OE) is strongly associated with improved gluten strength and bread making quality (Cho et al. 2017). Southern blotting of Glu1-Bx7 revealed two copies of the gene and hence over-expression of Glu1-Bx7 allele (Lukow et al. 1992) which can be visualized on SDS-PAGE (Fig. 3).Wheat genotypes with both the over-expressed Bx7 subunit and the Glu-D1 (5 + 10) have been considered to be more suitable for better dough properties (Cho et al. 2017).

Fig. 3.

Fig. 3

Open in a new tab

HMWGS pattern for different genotypes along with standards (WL711, Chinese Spring, PBW343 (Lr24 + GPC B1)); Lane 1: WL711; 2: Chinese Spring; 3: W1635 (arrow indicates the over-expressed Glu1-Bx7); 4: HahnWR; 5: HS240; 6: UP2338; 7: PBW343 (Lr24 + GPC B1); 8: Chinese Spring; 9: DBW17; 10: PBW621 + Yr10; 11: PBW550 + Yr5; 12: MACS2496; 12: MACS6222; 14:MACS6478

Durum wheat cultivars have poor bread making quality due to the lack of D genome and silenced Glu-A1 locus because of the presence of stop codon within the locus (Garg et al. 2007). Improvement in the protein content of durum cultivars has been done by introgressing genes from homeologous group 1 chromosomes via interspecific hybridization and chromosomal manipulations (Lukaszewski 2003). Durum wheat improvement was also done by transferring useful alleles required for improved gluten quality from 1D chromosome (Garg et al. 2007).

In 1RS.1BL translocation various efforts had been done to alleviate the quality deterioration in wheat through induced homeologous recombination or by centric mismatch fusion (Lukaszewski 2000). Recombinants with different degree of rye introgression at proximal (T lines) and distal ends (1B+ lines) in wheat were developed through backcross breeding in bread wheat cultivar Pavon 76 background. A desired set of alleles (without Sec-1 and with Glu-B3/Gli-B1) was obtained in one of the recombinants (Lukaszewski 2000) which is being used to enhance the bread making quality of wheat with marker assisted selection (MAS). In previous studies the 1RS arm (1RSWW) was developed by the elimination of Sec-1 loci of rye and introgression of Glu-B3/Gli-B1 loci from wheat (Howell et al. 2014). The HMWGS Glu-B1(7 + 9) and (7 + 8) with Glu-D1(5 + 10) compensated the quality deterioration because of secalin and improved the bread making quality (Fig. 4) (Sharma et al. 2018).

Fig. 4.

Fig. 4

Open in a new tab

Comparative study of bread quality in different wheat genotypes including 1RS.1BL translocation lines (UP2338, HS240, PBW550 + Yr5, DBW17, MACS6222, MACS2496, Pavon 1RS.1BL), 1RS.1BS recombinants lines (MA1 Pavon, 1RS44:38 and 1B + 38) and without translocation (HD2967, PBW621 + Yr10, MACS 6478 and Pavon76) using white bread as the standard (image

taken from Sharma et al. 2018)

Dough quality parameters analysis

Quality parameters of wheat such as whole grain, flour, dough and bread are analyzed by different qualitative and quantitative techniques. These parameters are utilized to measure the functionality and quality of the end-use (Peña et al. 2002). End-use quality characteristics such as grain protein content, gluten index, MST value, water absorption, dough development, loaf volume, baking score etc. have been used to decipher the gene-environment interactions affecting the quality characteristics (Rozbicki et al. 2015).

Protein content

Protein content is a significant parameter to determine the wheat grain quality. Protein content of 10–13% is considered good for chapatti making (Austin and Ram 1971). Higher protein content will improve the bread making quality as it will have more gluten protein (Kumar et al. 2018). The viscoelasticity of the dough is ensured by the quantity and quality of the wheat storage proteins for bread production (Mutlu et al. 2011). A number of techniques are used to determine the protein content, including Kjeldahl method, Dumas method, calorimetric/spectrophotometric evaluations and near-infrared reflectance spectroscopy (NIRS). Previously, the Kjeldahl method was used frequently but at present Dumas method is used because it is faster and less complicated than the Kjeldahl method (Freund and Kim 2006). NIRS is one of the best techniques utilized to predict the protein content of wheat grain. NIR spectra include test weight, color, total gluten content, soluble gliadin content, soluble and insoluble glutenin content and flour particle size etc. (Dowell et al. 2006).

Micro SDS-sedimentation test (MST)

MST is an important technique for distinguishing wheat varieties on the basis of qualitative and quantitative determination of gluten. The resulting sediment is associated with the swelling of glutenins, which is closely related to the bread making quality (Mutlu et al. 2011). MST values and gluten index indicate the variations in gluten strength as higher gluten content leads to higher sedimentation volume (Guo et al. 2018). The MST value is also correlated positively with the ratio of extension (R) to extensibility (E) of gluten which influences the dough quality. During the bread making process, the dough should have high extensibility in response to gas pressure and also have high strength to withstand the collapse of gas cells to have large bread volume (Dhaka and Khatkar 2015). Being an important parameter for analysis of bread making the micro SDS sedimentation test has very little significance in chapatti making as higher MST values result in poor chapatti making quality (Kumar et al. 2018).

Farinograph

The farinograph measures water absorption capacity, dough stability, resistance, development time and the dough softening (Frakolaki et al. 2018). Farinograph also determines the quality score for gluten strength (Dowell et al. 2006). The principle of farinograph operation relies on the resistance of the dough to the kneader shaft. The moment of resistance of the kneader shaft changes progressively as the components are mixed due to which the flour particles are hydrated and the dough formation takes place. The graphical record of the moment (dough consistency) during kneading with the farinograph device is called farinogram. The water absorption, which is strongly dependent on the gluten quality, indicates dough yield and the dough development time allows conclusions about the swelling rate. The drop in consistency (degree of softening) indicates whether the flour is strong or weak. The farinogram curves are characteristic of the gluten properties of the flour (Freund and Kim 2006).

Extensiograph

The extensiograph measures gluten characteristics such as resistance and extensibility (Yegin et al. 2018). Brabend extensiograph is an instrument used to perform a test in which two main parameters are measured—the maximum elongation resistance and the extensibility. Extensiograph plays a significant role in determining various properties as different food products have different properties as in the case of pasta and bread where the dough strength and ductility is variable (Bangur et al. 1997).

Mixograph

The Mixograph predicts the dough mixing properties of wheat varieties. Mixograph is used to determine water uptake, mixing time and mixing tolerance of dough and also used to optimize the effect of various additives used in baking (Dowell et al. 2006). The peak dough resistance (PDR) shows correlation between loaf volumes of different flour samples. The PDR also correlates significantly with the Glu-1 quality scores thus it can be used in baking test for evaluating the baking potential of flour rather than the other 'gel-protein' based methods. Mixograph correlates loaf volume, Glu-1 quality scores, protein content, MST values and re-absorption. Mixing properties are influenced by protein content in moderate flour while in case of strong or weak flours the mixing property remains unaffected (Khatkar et al. 1996).

Consistograph

Consistograph is used to determine the water absorption capacity. The water absorption of the dough is related to the moisture and recipe of bread making. The flour intake plays an important role in the making of all kinds of baked food products (Mutlu et al. 2011). Consistograph study of dietary fiber-reinforced dough and control dough (devoid of added fiber) showed that the water absorption was increased by the addition of fibers. This result is consistent with different types of fibers and hydrocolloids, although they were usually obtained with a farinograph or a blender. This result was expected due to the presence of (OH−) groups in the fiber making way for H-bonds leading to more aqueous interactions. Increase in the fiber addition from 2 to 5% enhances the water absorption capacity (Gómez et al. 2003). The principle bottleneck among bran's biochemical constituents is fiber which by absorbing water reduces the gluten quality for whole wheat bread making (Khalid et al. 2017). The decrease in consistency (degree of softening) indicates whether the flour is strong or weak (Freund and Kim 2006).

Fermentograph

The bread making process comprises of three phases: mixing, fermenting and baking. In the fermentation step, the CO2 produced by the yeast during mixing, increases the volume of the dough. The fermentograph displays the nature of the dough during the expansion of gas cells leading to the deformation of dough. As the dough membrane rip apart it limits the rise of dough during fermentation (Hrušková et al. 2006).

Celiac disease

Gluten is a water insoluble protein present in the endosperm portion of wheat, barley and rye. Gluten-related disorder describes a condition related to digestion of gluten-containing food products (Pietzak 2012). Adverse effects caused by wheat ingestion have been defined into three categories in a recent International Consensus (1) the autoimmune reaction known as celiac disease (CD) (2) allergic reactions (3) non-celiac gluten sensitivity (NCGS) (Nijhawan and Goyal 2015). CD is a systemic immunological disorder which affects the small intestine and is initiated by a reaction to storage proteins, glutens found in cereal grains, in genetically susceptible individuals (Plenge 2010). The body’s immune system starts out breaking intestinal tissue after having gluten based products (Fig. 5) causing nutrition deficiencies such as anemia and osteoporosis (Pietzak 2012).

Fig. 5.

Fig. 5

Open in a new tab

Outline of the mechanism of celiac disease

Genetic background has an important role in the predisposition to the celiac disease. CD is caused by uncontrolled T-cell responses to GLU peptides and inflammation is induced by α-gliadins (Vader et al. 2002). α-gliadin of wheat is classified by GliA2, GliB2 and GliD2 loci present on the short arm of chromosome 6 of wheat (Kaur et al. 2016). 90% of CD patients show an expressed HLA-DQ2 haplotype (DQA1 0501/DQB1 0201) whereas the rest 5% have HLA-DQ8 haplotype expression (DQA1 0301/DQB1 0302). It is during the early childhood days when the children possessing HLA haplotype DR3-DQ2 homozygote are prone for celiac disease (Liu et al. 2014). The gliadins get deamidated by the TTG (tissue transglutaminase) followed by the change of charge on the gliadins fragment thus facilitating their binding with HLA-DQ2 and HLA-DQ8. The T-cell recognizes the gliadins peptides and produce proinflammatory cytokines (interferon γ) (Lebwohl et al. 2013). GLU specific HLA-haplotypes (DQ2/DQ8) restricted T-cells are present at the lesion site inside the gut (Fig. 5). Presence of negatively charged amino acids facilitates the binding of peptides to the above mentioned HLA haplotypes very efficiently GLU-derived peptides have low affinity ligands for HLA-DQ2/DQ8 because it has a small number of negatively charged amino acids. The epitope sequences present on T-cell stimulatory gluten peptides (e.g. Glia-α20, Glia-γ30, Glt-156, Glt-17, Glu-21 and Glu-5) have been discussed previously by Vader et al. (2002). Type I diabetes mellitus and autoimmune thyroid disease generally occurs with CD (Ludvigsson et al. 2006). Wheat germ agglutinin (WGA), a lectin, is also associated with autoimmune disorders. This WGA binds with a sialic acid (N-Glycoylneuraminic acid) present on the glycocalyx of the human cell and allows for cell entry provoking the immune system for response and thus perturbing the immune tolerance (Vojdani 2015).

Gluten free cereals (rice, amaranth, buckwheat, corn, millet, quinoa, sorghum, teff and oats) have been suggested as an alternative diet for the patients suffering from celiac disease. For gluten free bakery products certain additives are used which includes egg white protein, soy whey (Zannini et al. 2012; Masure et al. 2016), enzymes (crosslinking agents) such as transglutaminase, tyrosinase (Khoury et al. 2018), hydrocolloids (for increasing viscosity of the batter for improved loaf volume) such as methyl cellulose and carboxymethyl cellulose (Zannini et al. 2012; Masure et al. 2016). Avoiding the grains (wheat, rye and barley) having gluten is primarily important to eliminate the allergic reaction (Nijhawan and Goyal 2015). Understanding the reasons of celiac disease and gluten intolerance is the major goal of many researches in the world. Along with focus on human diagnosis and treatment, identification of about 20 proteins fragment in wheat that cause celiac disease have been done. But no one has been able to identify all of them or breed a variety of wheat, which is safe to eat for celiac patients. Endosperm specific silencing of wheat DEMETER gene led to the development of wheat genotypes safe for celiac disease patients without much affecting the bread making attributes (Rustgi et al. 2015). Variations in α-gliadin gene sequences especially at T-cell stimulatory epitopes glia-α9, glia-α20, glia-α2 and glia-α have been found in various wheat genotypes. A lower percentage of T-cell stimulatory epitopes in wheat genotypes namely C591, C273 and K78 is an initial step for the development of a wheat variety which will be less harmful for CD patients (Kaur et al. 2017).

Conclusion

Dough quality for improved bread making is a pre-requisite and is affected by various factors associated with gluten and gliadins. The HMWGS such as Glu-B1 (7 + 8/7 + 9/17 + 18) and GluD1 (5 + 10) significantly increases the dough strength and provide high micro SDS sedimentation value. The combination of Glu-B1(7 + 8)/(7 + 9) and Glu-D1(5 + 10) even overcomes the negative effect of secalin on end-use quality. Protein content and its quality influence the visco-elasticity of dough and contribute to the improved end-use quality. The rheological and functional properties of gluten are largely affected by gliadins/glutenin ratio. Gliadins enhance the viscosity of the gluten protein complex while LMWGS increases the elasticity of the dough. LMWGS alleles Glu-A3, Glu-B3 along with HMWGS Glu-D1 contribute to dough properties and improved end-use quality. The dough quality measurement by various techniques provides information regarding dough softening, dough stability, dough mixing properties, dough extensibility, gluten strength and dough fermentation properties. Further studies are required for analysis of end-use quality and the factors responsible for its improvement. Although studies have been done in the past on HMWGS alleles and their role in end-use quality but LMWGS and their impact on bread making quality is yet to be explored completely.

Acknowledgements

The authors acknowledge Department of Biotechnology, Government of India (BT/PR10886/AGII/106/934/2014) for providing financial support. The authors also acknowledge Akal College of Agriculture, Eternal University for arranging required infrastructure and research amenities.

Conflict of interest The authors declare no conflict of interest for this work.

Footnotes

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Ambika Sharma and Sheenu Garg have contributed equally to this work.

Contributor Information

Pritesh Vyas, Email: pritesh2010@gmail.com.

H. S. Dhaliwal, Email: hsdhaliwal07@gmail.com

References

  1. Ammar K, Mergoum M, Rajaram S (2004) The history and evolution of triticale. Triticale improvement and production (No.CIS-4898.CIMMYT)
  2. Amri A, Boujnah M, Nsarellah N, Taghouti M, Nachit MM. Genetic and agronomic approaches to improve durum wheat quality in Morocco. In: Nachit MM, Fonzo N, Araus JL, editors. Durum wheat improvement in the Mediterranean region: new challenges. Zaragoza: CIHEAM-IAMZ; 2000. pp. 543–547. [Google Scholar]
  3. Anderson OD, Cassidy B, Steffen J, Dvorak J, Greene FC. Structure of the high- and low-molecular-weight gene families of the homeologous group 1 chromosomes of the hexaploid bread wheat cultivar Cheyenne. In: Bushuk W, Tkachuk R, editors. Gluten proteins. St. Paul: AACC; 1991. pp. 512–519. [Google Scholar]
  4. Austin A, Ram A. Studies on chapati making quality of wheat. New Delhi: Rajendra Printers; 1971. pp. 1–108. [Google Scholar]
  5. Ayalew H, Kumssa TT, Butler TJ, Ma XF. Triticale improvement for forage and cover crop uses in the Southern Great Plains of the United States. Front Plant Sci. 2018;9:1130. doi: 10.3389/fpls.2018.01130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bakshi S, Bhagwat SG. High molecular weight glutenin subunit variation among Indian wheat varieties. J Agric Sci. 2016;6(11):349–355. [Google Scholar]
  7. Bangur R, Batey IL, McKenzie E, MacRitchie F. Dependence of extensiograph parameters on wheat protein composition measured by SE-HPLC. J Cereal Sci. 1997;25(3):237–241. [Google Scholar]
  8. Barak S, Mudgil D, Khatkar BS. Relationship of gliadin and glutenin proteins with dough rheology, flour pasting and bread making performance of wheat varieties. LWT-Food Sci Technol. 2013;51(1):211–217. [Google Scholar]
  9. Barak S, Mudgil D, Khatkar BS. Biochemical and functional properties of wheat gliadins: a review. Food Sci Nutr. 2015;55(3):357–368. doi: 10.1080/10408398.2012.654863. [DOI] [PubMed] [Google Scholar]
  10. Boehm JD, Ibba MI, Kiszonas AM, Morris CF. End-use quality of CIMMYT-derived soft-kernel durum wheat germplasm: II. Dough strength and pan bread quality. Crop Sci. 2017;57(3):1485–94. [Google Scholar]
  11. Branković G, Dodig D, Pajić V, Kandić V, Knežević D, Đurić N, Živanović T. Genetic parameters of Triticum aestivum and Triticum durum for technological quality properties in Serbia. Zemdirbyste-Agriculture. 2018;105(1):39–48. [Google Scholar]
  12. Caballero PA, Gómez M, Rosell CM. Bread quality and dough rheology of enzyme-supplemented wheat flour. Eur Food Res Technol. 2007;224(5):525–534. [Google Scholar]
  13. Cakmak I, Pfeiffer WH, McClafferty B. Biofortification of durum wheat with zinc and iron. Cereal Chem. 2010;87(1):10–20. [Google Scholar]
  14. Chňapek M, Peroutková R, Vivodík M, Gálová Z. Identification of technologically important genes and their products in the collection of bread wheat genotypes. J Microbiol Biotechnol Food Sci. 2015;4((Special issue 02)):26–29. [Google Scholar]
  15. Cho SW, Roy SK, Chun JB, Cho K, Park CS. Overexpression of the Bx7 high molecular weight glutenin subunit on the Glu-B1 locus in a Korean wheat landraces. Plant Biotechnol Rep. 2017;11:97–105. [Google Scholar]
  16. D’Ovidio R, Masci S. The low-molecular-weight glutenin subunits of wheat gluten. J Cereal Sci. 2004;39:321–339. [Google Scholar]
  17. Delcour JA, Hoseney RC. Principles of cereal science and technology. St. Paul: AACC Internatioanl; 2010. [Google Scholar]
  18. Delcour JA, Joye IJ, Pareyt B, Wilderjans E, Brijs K, Lagrain B. Wheat gluten functionality as a quality determinant in cereal-based food products. Ann Rev Food Sci Technol. 2012;3:469–492. doi: 10.1146/annurev-food-022811-101303. [DOI] [PubMed] [Google Scholar]
  19. Dhaka V, Khatkar BS. Effects of gliadin/glutenin and HMW-GS/LMW-GS ratio on dough rheological properties and bread making potential of wheat varieties. J Food Qual. 2015;38(2):71–82. [Google Scholar]
  20. Dowell FE, Maghirang EB, Xie F, Lookhart GL, Pierce RO, Seabourn BW, Bean SR, Wilson JD, Chung OK. Predicting wheat quality characteristics and functionality using near-infrared spectroscopy. Cereal Chem. 2006;83(5):529–536. [Google Scholar]
  21. Filip E. Composition of high molecular weight glutenin subunits in polish common wheat cultivars (Triticum aestivum L.) J Food Quality. 2018 doi: 10.1155/2018/2473420. [DOI] [Google Scholar]
  22. Fleitas MC, Schierenbeck M, Gerard GS, Dietz JI, Golik SI, Campos PE, Simón MR. How leaf rust disease and its control with fungicides affect dough properties, gluten quality and loaf volume under different N rates in wheat. J Cereal Sci. 2018;80:119–127. [Google Scholar]
  23. Frakolaki G, Giannou V, Topakas E, Tzia C. Chemical characterization and breadmaking potential of spelt versus wheat flour. J Cer Sci. 2018;79:50–56. [Google Scholar]
  24. Freund W, Kim MY (2006) Determining the baking quality of wheat and rye flour. pdfs.semanticscholar.org
  25. Gálová Z, Michalik I, Knoblochova H, Gregova E. Variation in HMW glutenin subunits of different species of wheat. Rostlinna Vyroba. 2002;48(2):15–19. [Google Scholar]
  26. Garg M, Dhaliwal HS, Chhuneja P, Kumar D, Dou QW, Elamein HMM, Tanaka H, Tsujimoto H. Negative effect of chromosome 1A on dough strength shown by modification of 1D addition in durum wheat (Triticum durum) Theor Appl Genet. 2007;114:1141–1150. doi: 10.1007/s00122-007-0506-4. [DOI] [PubMed] [Google Scholar]
  27. Garg M, Tanaka H, Ishikawa N, Takata K, Yanaka M, Tsujimoto H. Agropyron elongatum HMW-glutenins have a potential to improve wheat end-product quality through targeted chromosome introgression. J Cereal Sci. 2009;50:358–363. [Google Scholar]
  28. Gellrich C, Schieberle P, Wieser H. Biochemical characterization and quantification of the storage protein (secalin) types in rye flour. Cereal Chem. 2003;80:102–109. [Google Scholar]
  29. Gianibelli MC, Larroque OR, MacRitchie F, Wrigley CW. Biochemical, genetic, and molecular characterization of wheat glutenin and its component subunits. Cereal Chem. 2001;78(6):635–646. [Google Scholar]
  30. Gianibelli MC, Echaide M, Larroque OR, Carrillo JM, Dubcovsky J. Biochemical and molecular characterisation of Glu-1 loci in Argentinean wheat cultivars. Euphytica. 2002;128(1):61–73. [Google Scholar]
  31. Giraldo P, Rodriguez-Quijano M, Simon C, Vázquez JF, Carrillo JM. Allelic variation in HMW glutenins in Spanish wheat landraces and their relationship with bread quality. Span J Agric Res. 2010;8(4):1012–1023. [Google Scholar]
  32. Gómez M, Ronda F, Blanco CA, Caballero PA, Apesteguía A. Effect of dietary fibre on dough rheology and bread quality. Eur Food Res Technol. 2003;216(1):51–56. [Google Scholar]
  33. Graybosch RA. Mini review: uneasy unions: quality effects of rye chromatin transfers to wheat. J Cereal Sci. 2001;33(1):3–16. [Google Scholar]
  34. Guo X, Sun X, Zhang Y, Wang R, Yan X. Interactions between soy protein hydrolyzates and wheat proteins in noodle making dough. Food Chem. 2018;245:500–507. doi: 10.1016/j.foodchem.2017.10.126. [DOI] [PubMed] [Google Scholar]
  35. Hadnađev M, DapčevićHadnadev T, Šimurina O, Filipčev B. Empirical and fundamental rheological properties of wheat flour dough as affected by different climatic conditions. J Agric Sci Technol. 2013;15:1381–1391. [Google Scholar]
  36. Howell T, Hale I, Jankuloski L, Bonafede M, Gilbert M, Dubcovsky J. Mapping a region within the 1RS.1BL translocation in common wheat affecting grain yield and canopy water status. Theoret Appl Genet. 2014;127(12):2695–2709. doi: 10.1007/s00122-014-2408-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Hrušková M, Švec I, Jirsa O. Correlation between milling and baking parameters of wheat varieties. J Food Eng. 2006;77(3):439–444. [Google Scholar]
  38. Ito M, Maruyama-Funatsuki W, Ikeda TM, Nishio Z, Nagasawa K, Tabiki T. Dough properties and bread-making quality-related characteristics of Yumechikara near-isogenic wheat lines carrying different Glu-B3 alleles. Breed Sci. 2015;65(3):241–248. doi: 10.1270/jsbbs.65.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Janni M, Cadonici S, Pignone D, Marmiroli N. Survey and new insights in the application of PCR-based molecular markers for identification of HMW-GS at the Glu-B1 locus in durum and bread wheat. Plant Breed. 2017;136(4):467–473. [Google Scholar]
  40. Kaur A, Shevkani K, Katyal M, Singh N, Ahlawat AK, Singh AM. Physicochemical and rheological properties of starch and flour from different durum wheat varieties and their relationships with noodle quality. J Food Sci Technol. 2016;4:2127–2138. doi: 10.1007/s13197-016-2202-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Kaur A, Bains NS, Sood A, Yadav B, Sharma P, Kaur S, Garg M, Midha V, Chhuneja P. Molecular characterization of α-gliadin gene sequences in Indian wheat cultivars vis-à-vis celiac disease eliciting epitopes. J Plant Biochem Biotechnol. 2017;26(1):106–112. [Google Scholar]
  42. Khalid KH, Ohm JB, Simsek S. Whole wheat bread: effect of bran fractions on dough and end-product quality. J Cereal Sci. 2017;78:48–56. [Google Scholar]
  43. Khatkar BS, Bell AE, Schofield JD. A comparative study of the inter-relationships between mixograph parameters and bread-making qualities of wheat flours and glutens. J Sci Food Agri. 1996;72(1):71–85. [Google Scholar]
  44. Khoury DE, Ducharme BS, Joye IJ. A review on the gluten-free diet: technological and nutritional challenges. Nutrients. 2018;10(10):1410. doi: 10.3390/nu10101410. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Kiszonas AM, Morris CF. Wheat breeding for quality: a historical review. Cereal Chem. 2018;95(1):17–34. [Google Scholar]
  46. Kumar S, Sohu VS, Gupta SK, Singh RP, Bains NS. Understanding the chapatti making attributes of Indian wheats. I: The physico-chemical basis. J Appl Nat Sci. 2018;10(2):572–592. [Google Scholar]
  47. Lebwohl B, Blaser MJ, Ludvigsson JF, Green PH, Rundle A, Sonnenberg A, Genta RM. Decreased risk of celiac disease in patients with Helicobacter pylori colonization. Am J Epidemiol. 2013;178(12):1721–1730. doi: 10.1093/aje/kwt234. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Lei ZS, Gale KR, He ZH, Gianibelli C, Larroque O, Xia XC, Butow BJ, Ma W. Y-type gene specific markers for enhanced discrimination of high-molecular weight glutenin alleles at the Glu-B1 locus in hexaploid wheat. J Cereal Sci. 2006;43(1):94–101. [Google Scholar]
  49. Lerner SE, Seghezzo ML, Molfese ER, Ponzio NR, Cogliatti M, Rogers WJ. N-and S-fertiliser effects on grain composition, industrial quality and end-use in durum wheat. J Cereal Sci. 2006;44(1):2–11. [Google Scholar]
  50. Lew EJL, Kuzmicky DD, Kasarda DD. Characterization of low molecular weight glutenin subunits by reversed-phase high performance liquid chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and N-terminal amino acid sequencing. Cereal Chem. 1992;69:508–515. [Google Scholar]
  51. Liu E, Lee HS, Aronsson CA, Hagopian WA, Koletzko S, Rewers MJ, Eisenbarth GS, Bingley PJ, Bonifacio E, Simell V, Agardh D. Risk of pediatric celiac disease according to HLA haplotype and country. New Engl J Med. 2014;371(1):42–49. doi: 10.1056/NEJMoa1313977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Lombardo LA, Nisi MM, Salines N, Ghione CE, Helguera M. Identification of novel high molecular weight glutenin subunit mutants in bread wheat (Triticum aestivum L.) Cytogenet Cell Genet. 2017;51(4):305–314. [Google Scholar]
  53. Ludvigsson JF, Ludvigsson J, Ekbom A, Montgomery SM. Celiac disease and risk of subsequent type 1 diabetes: a general population cohort study of children and adolescents. Diabetes Care. 2006;29:2483–2488. doi: 10.2337/dc06-0794. [DOI] [PubMed] [Google Scholar]
  54. Lukaszewski AJ. Manipulation of the 1RS.1BL translocation in wheat by induced homeologous recombination. Crop Sci. 2000;40(1):216–225. [Google Scholar]
  55. Lukaszewski AJ. Registration of six germplasms of durum wheat with introgressions of the Glu-D1 locus. Crop Sci. 2003;43(3):1138. [Google Scholar]
  56. Lukow OM, Forsyth SA, Payne PI. Over-production of HMW [High Molecular Weight] glutenin subunits coded on chromosome 1B in common wheat-Triticum aestivum. J Genet Breed. 1992;46:187–192. [Google Scholar]
  57. Macharia GK, Peña RJ, Simsek S, Anderson JA. Variation at glutenin subunit loci, single kernel characterization and evaluation of grain protein in East African bread wheat varieties. Euphytica. 2014;197(3):409–421. [Google Scholar]
  58. Masure HG, Fierens E, Delcour JA. Current and forward looking experimental approaches in gluten-free bread making research. J Cereal Sci. 2016;67:92–111. [Google Scholar]
  59. Mergoum M, Singh PK, Pena RJ, Lozano-del Río AJ, Cooper KV, Salmon DF, Macpherson HG. Triticale: a “new” crop with old challenges. In: Carena M, editor. Cereals. Berlin: Springer; 2009. pp. 267–287. [Google Scholar]
  60. Merlino M, Leroy P, Chambon C, Branlard G. Mapping and proteomic analysis of albumin and globulin proteins in hexaploid wheat kernels (Triticum aestivum L.) Theor Appl Genet. 2009;18:1321–1337. doi: 10.1007/s00122-009-0983-8. [DOI] [PubMed] [Google Scholar]
  61. Morris CF, Casper J, Kiszonas AM, Fuerst EP, Murray J, Simeone MC, Lafiandra D. Soft kernel durum wheat—a new bakery ingredient? Cereal Foods World. 2015;60:76–83. doi: 10.1094/CFW-60-2-0076. [DOI] [Google Scholar]
  62. Mutlu AC, Boyaci IH, Genis HE, Ozturk R, Basaran-Akgul N, Sanal T, Evlice AK. Prediction of wheat quality parameters using near-infrared spectroscopy and artificial neural networks. Eur Food Res Technol. 2011;233(2):267–274. [Google Scholar]
  63. Nakamura H. Allelic variation at high-molecular-weight glutenin subunit Loci, Glu-A1, Glu-B1 and Glu-D1, in Japanese and Chinese hexaploid wheats. Euphytica. 2000;112(2):187. [Google Scholar]
  64. Nazco R, Villegas D, Ammar K, Pena RJ, Moragues M, Royo C. Can Mediterranean durum wheat landraces contribute to improved grain quality attributes in modern cultivars? Euphytica. 2012;185(1):1–7. [Google Scholar]
  65. Nijhawan S, Goyal G. Celiac disease review. J Gastrointest Dig Syst. 2015;5(6):350. [Google Scholar]
  66. Osman AM, Struik PC, van Bueren ETL. Perspectives to breed for improved baking quality wheat varieties adapted to organic growing conditions. J Sci Food Agric. 2012;92(2):207–215. doi: 10.1002/jsfa.4710. [DOI] [PubMed] [Google Scholar]
  67. Pattison AL (2013) Genetic improvement of grain quality for bread making in triticale. https://ses.library.usyd.edu.au.
  68. Payne PI. Genetics of wheat storage proteins and the effect of allelic variation on bread-making quality. Annu Rev Plant Physiol. 1987;38(1):141–153. [Google Scholar]
  69. Peña RJ, Trethowan R, Pfeiffer WH, Ginkel MV. Quality (end-use) improvement in wheat: compositional, genetic, and environmental factors. J Crop Prod. 2002;5(1–2):1–37. [Google Scholar]
  70. Pietzak M. Celiac disease, wheat allergy, and gluten sensitivity: when gluten free is not a fad. J Parenter Enter Nutr. 2012;36(99):1_suppl–75S. doi: 10.1177/0148607111426276. [DOI] [PubMed] [Google Scholar]
  71. Plenge RM. Unlocking the pathogenesis of celiac disease. Nature Genet. 2010;42(4):281. doi: 10.1038/ng0410-281. [DOI] [PubMed] [Google Scholar]
  72. Rasheed A, Mahmood T, Kazi AG, Ghafoor A, Mujeeb-Kazi A. Allelic variation and composition of HMW-GS in advanced lines derived from D-genome synthetic hexaploid/bread wheat (Triticum aestivum L.) J Crop Sci. 2012;15(1):1–7. [Google Scholar]
  73. Roy N, Islam S, Ma J, Lu M, Torok K, Tomoskozi S, Bekes F, Lafiandra D, Appels R, Ma W. Expressed Ay HMW glutenin subunit in Australian wheat cultivars indicates a positive effect on wheat quality. J Cereal Sci. 2018;79:494–500. [Google Scholar]
  74. Rozbicki J, Ceglińska A, Gozdowski D, Jakubczak M, Cacak-Pietrzak G, Mądry W, Golba J, Piechociński M, Sobczyński G, Studnicki M, Drzazga T. Influence of the cultivar, environment and management on the grain yield and bread-making quality in winter wheat. J Cereal Sci. 2015;61:126–132. [Google Scholar]
  75. Rustgi S, Wettstein DV, Ankrah N, Brew-Appiah RAT, Wen N, Mitchell SM, Gemini R, Rei-senauer P. Celiac-safe wheat genotypes: A dietary solution to the gluten-induced disorders. Ann Wheat Newslett. 2015;61:99–103. [Google Scholar]
  76. Sharma S, Ram S, Gupta R. Relationship of high and low molecular weight glutenins with chemical and rheological properties of wheat flour. J Wheat Res. 2012;4(1):74–78. [Google Scholar]
  77. Sharma A, Sheikh I, Kumar R, Kumar K, Vyas P, Dhaliwal HS. Evaluation of end-use quality and root traits in wheat cultivars associated with 1RS.1BL translocation. Euphytica. 2018;214(4):62. [Google Scholar]
  78. Sherman JD, Varella AC, Lanning SP, Martin JM, Heo HY, Nash D, Talbert LE. Effect of a gene for high dough strength on whole wheat baking parameters of hard white spring wheat. Cereal Chem. 2018;95(3):411–417. [Google Scholar]
  79. Shewry PR, Halford NG, Tatham AS. The high molecular weight subunits of wheat glutenin. J Cereal Sci. 1992;15:105–120. [Google Scholar]
  80. Shewry P, Gilbert S, Savage A, Tatham A, Wan YF, Belton P, Wellner N, D'ovidio R, Bekes F, Halford N. Sequence and properties of HMW subunit 1Bx20 from pasta wheat (Triticum durum) which is associated with poor end use properties. Theor Appl Genet. 2003;106(4):744–750. doi: 10.1007/s00122-002-1135-6. [DOI] [PubMed] [Google Scholar]
  81. Si H, Zhao M, He F, Ma C. Effect of Glu-B3 allelic variation on sodium dodecyl sulfate sedimentation volume in common wheat (Triticum aestivum L.) Sci World J. 2013;9:99. doi: 10.1155/2013/848549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Skylas DJ, Mackintosh JA, Cordwell SJ, Walsh BJ, Harry J, Blumenthal C, Copeland L, Wrigley CW, Rathmell WG. Proteome approach to the characterisation of protein composition in the developing and mature wheat-grain endosperm. J Cereal Sci. 2000;52:169–188. [Google Scholar]
  83. Tanaka K, Yamauchi H, Nishio Z, Kuwabara T. Effect of high molecular weight glutenin subunits on bread-making quality using near-isogenic lines. Breed Sci. 2000;50(4):303–308. [Google Scholar]
  84. Tatham AS, Drake AF, Shewry PR. Conformational studies of synthetic peptides corresponding to the repetitive region of the high molecular weight (HMW) glutenin subunits of wheat. J Cereal Sci. 1990;11:189–200. [Google Scholar]
  85. Thomson NH, Miles MJ, Tatham AS, Shewry PR. Molecular images of cereal proteins by STM. Ultramicroscopy. 1992;4244:1118–1122. doi: 10.1016/0304-3991(92)90425-j. [DOI] [PubMed] [Google Scholar]
  86. Vader W, Kooy Y, van Veelen P, de Ru A, Harris D, Benckhuijsen W, Koning F. The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides. Gastroenterology. 2002;122(7):1729–1737. doi: 10.1053/gast.2002.33606. [DOI] [PubMed] [Google Scholar]
  87. Vojdani A. Lectins, Agglutinins, and their roles in autoimmune reactivities. Altern Ther. 2015;21:42–47. [PubMed] [Google Scholar]
  88. Wrigley CW. Wheat: a unique grain for the world. Romania. 2009;7:2–9. [Google Scholar]
  89. Yegin S, Altinel B, Tuluk K. A novel extremophilic xylanase produced on wheat bran from Aureobasidium pullulans NRRL Y-2311-1: effects on dough rheology and bread quality. Food Hydrocoll. 2018;81:389–397. [Google Scholar]
  90. Yu Z, Peng Y, Islam MS, She M, Lu M, Lafiandra D, Roy N, Juhasz A, Yan G, Ma W. Molecular characterization and phylogenetic analysis of active y-type high molecular weight glutenin subunit genes at Glu-A1 locus in wheat. J Cereal Sci. 2019 doi: 10.1016/j.jcs.2019.01.003. [DOI] [Google Scholar]
  91. Zannini E, Jones JM, Renzetti S, Arendt EK. Functional replacements for gluten. Ann Rev Food Sci Technol. 2012;3:227–245. doi: 10.1146/annurev-food-022811-101203. [DOI] [PubMed] [Google Scholar]
  92. Zarkti H, Ouabbou H, Udupa SM, Gaboun F, Hilali A. Agro-morphological variability in durum wheat landraces of Morocco. Aus J Crop Sci. 2012;7:1172. [Google Scholar]
  93. Zhang X, Liu D, Yang W, Liu K, Sun J, Guo X, Li Y, Wang D, Ling H, Zhang A. Development of a new marker system for identifying the complex members of the low-molecular-weight glutenin subunit gene family in bread wheat (Triticum aestivum L.) Theor Appl Genet. 2011;122(8):1503–16. doi: 10.1007/s00122-011-1550-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Žilić S, Barać M, Pešić M, Hadži-Tašković-Šukalović V, Dodiga D, Mladenović-Drinić S, Janković M. Genetic variability of albumin-globulin content, and lipoxygenase, peroxidase activities among bread and durum wheat genotypes. Genetika. 2011;43(3):503–516. [Google Scholar]

Articles from Journal of Food Science and Technology are provided here courtesy of Springer

RESOURCES