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. 2020 Sep 18;18(9):471. doi: 10.3390/md18090471

Table 3.

Recent studies on sea cucumber collagen.

Sea Cucumber Species Focus of Study Major Findings Reference
Stichopus japonicus Chemical composition and subunit structure of collagen Collagen was comprised of 2 distinct subunits (α1 and α2 and rich in glutamic acid compared to other fibrillar collagen [14]
Characterization and subunit composition of collagen Pepsin solubilized collagen resembled type I collagen and its amino acid composition was different from vertebrate collagen. [16]
Changes of collagen during cooking Crude collagen fibers were more susceptible to heat treatment compared to pepsin-solubilized collagen [115]
Identification of physicochemical properties and radical scavenging capacities of pepsin-solubilized collagen Extracted collagen maintained intact triple-stranded helices and high moisture retention and absorption capacities as well as exhibiting better radical scavenging ability compared to vitamins C and E. [95]
Wound-healing effects on human keratinocyte (HaCaT) cell line of pepsin-solubilized collagen Pepsin-solubilized collagen has the potential to use as an alternative mammalian collagen in the nutraceutical and pharmaceutical industries [96]
Effect of autolysis of intact collagen fibers related to the distributions of cathepsin L Lysosomal cathepsin L degrades the collagen fibers and speed and degree of autolysis is negatively correlated with the density of collagen. [116]
Structural characteristics of sea cucumber collagen fibers in the presence of endogenous cysteine proteinases Collagen fibrils disaggregated into collagen fibrils by cysteine proteinases and the structural disorder of the native collagen fibers increased due to cysteine protease. [102]
Structural and biochemical changes of collagen related to autolysis Collagen fibers and microfibrils gradually degraded with the autolysis and structural damage was less in monomeric collagen compared to other structural elements [103]
Structural and thermal properties of sea cucumber collagen Distance between adjacent molecular chains in collagen molecules was decreased and CO2, NH3, H2O, CH4, NO2 and HCN gases released during the heat treatment [117]
Enzymatic hydrolysis of collagen to determine the structural changes of collagen fibrils Collagen fibers were partially degraded into collagen fibrils by enzymatic (trypsin) treatments [118]
Investigate the effect of collagenase type I on the structural features of collagen fibers Collagenase was responsible for partial depolymerization of collagen fibers into fibrils, uncoiled the fibrils, degrade monomeric collagen [119]
Parastichopus californicus Purification and characterization of pepsin-solubilized collagen from skin and connective tissue Collagen extracted from skin and connective tissue contains type I collagen with three α1 chain. Amino acid composition is different from the mammalian type I collagen [120]
Bohadschia spp. Analysis of isolated pepsin-solubilized collagen Type I collagen was identified with three α1 chain [121]
Stichopus vastus Isolation and characterization of pepsin-solubilized collagen Purified collagen belongs to type I collagen contains three α1 chain with triple helical structure [99]
Molecular mass distribution, amino acid composition and radical-scavenging activity of collagen hydrolysates prepared from isolated collagen β and α1 chains of the collagen were hydrolyzed by trypsin and molecular mass distribution ranged from 5 to 25 kDa. Hydrolysates contains high glycine, alanine, glutamate, proline and hydroxyproline residues and showed significant radical scavenging activity [122]
Physicochemical and biochemical properties of pepsin solubilized collagen Glycine was the predominant amino acid present in purified collagen that possessed high moisture absorption and retention capacity [122]
Identification of Angiotensin I converting enzyme (ACE) inhibitory and radical scavenging activities from collagen hydrolysates Novel bioactive peptides generated by optimized trypsin hydrolysis have the potential to use as ACE inhibitors and radical scavenging agents. [100]
Holothuria parva Purification and characterization of pepsin-solubilized collagen Isolated collagen constituted three α1 chain and was rich in glycine, proline, alanine and hydroxyproline [98]
Stichopus monotuberculatus Isolation and characterization of pepsin-solubilized collagen Isolated collagen was classified as type I collagen consisted of three α1 chain [101]
Holothuria scabra Determination of nano-collagen quality and extraction of acid solubilized collagen Extracted acid solubilized collagen had significant effect on physicochemical characteristics of nano-collagen particles [123]
Australostichopus mollis Biochemical composition of isolated collagen Type I collagen was present with α1 and α2 chains, α chain dimers, β chains, and γ components. Most abundant amino acids were glycine, alanine, threonine, serine, and proline. [124]
Holothuria leucospilota In vitro activity of anti-tyrosinase and anti-elastase activity of isolated collagen Isolated collagen exhibited weak anti-tyrosine activity and moderate anti-elastase activity [125]
Acaudina leucoprocta Extraction methods to remove heavy metals from the isolated collagen Pepsi- solubilized collagen showed two isoforms and amount of heavy metals present in the collagen were below the contaminant limit [126]
Acaudina molpadioides Preparation and characterization of antioxidative peptides from collagen hydrolysates Collagen peptides which showed highest antioxidant activity were rich in hydrophobic acid residues. [127]
Stichopus vastus and Holothuria atra Comparison of partial characteristics of two different sea cucumbers No significant difference in amino acid composition, yield, or whiteness [128]
Apostichopus japonicus Type of constituent collagen using proteomics and bioinformatic strategies Heterogenicity of the sea cucumber collagen fibrils was revealed for the first time that provides novel insight into the composition of sea cucumber collagen [104]
Analysis of the effect of epigallocatechin gallate (EGCG) on preserving molecular structure of collagen fibers during heating EGCG protects the structure of crude collagen fibers in a dosage dependent manner and effects hydrogen bonds on the collagen which promotes protein aggregation [105]
Holothuria cinerascens Potential application of collagen in moisturizing cosmetics Collagen showed better moisture retention and moisture absorption capacity. Abundant hydrophilic groups in collagen increases their ability for cosmetic formulations [83]