Bacillus amyloliquefaciens |
Two extracellular keratinolytic proteases produced by S13 were purified. These two enzymes were with 47 and 28 kDa, respectively |
Hamiche et al., 2019 |
Bacillus cereus |
A strain KB043 was shown to be able to produce keratinase |
Swetlana and Jain, 2010 |
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This strain producing keratinase was screened from the halophilic environment |
Arokiyaraj et al., 2019 |
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A strain was able to degrade feathers by producing keratinase |
Jeevana Lakshmi et al., 2013 |
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A strain Wu2 was able to produce keratinolytic enzyme using feather as the sole carbon and nitrogen sources |
Lo et al., 2012 |
Bacillus thuringiensis |
This stain is able to degrade heat-treated feather. Additives in the medium affected feather degradation |
Sahni et al., 2015 |
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A strain AD-12 was able to produce detergent-stable serine keratinolytic proteinase with a molecular weight of 39 kDa |
Gegeckas et al., 2014 |
Stenotrophomonas maltophilia |
This stain was isolated from the gut of a spider. Three enzymes were purified from this strain |
Saravanan and Dhurai, 2012 |
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Strain BBE11-1 secrets two keratinolytic proteases. These two enzymes-KerSMD (48 kDa) and KerSMDF (40 kDa) were overexpressed in E. coli
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Fang et al., 2014 |
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A strain R13 was able to produce keratinolytic enzyme using chicken feathers as the sole carbon and nitrogen sources |
Jeong et al., 2010b |
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A strain BBE11-1 was able to secrete keratinase and degrade wool waste |
Fang et al., 2013 |
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A strain R13 was isolated and able to produce keratinolytic enzyme in the chicken feather medium |
Jeong et al., 2010b |
Bacillus sp. |
Bacillus strains were able to produce keratinase |
Lin et al., 1999; Gegeckas et al., 2018
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Three strains were used to convert feather into feather hydrolysate |
Callegaro et al., 2018 |
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Quite a few Bacillus sp. strains were screened from marine environment and produced keratinase |
Herzog et al., 2016 |
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A strain was able to degrade feather by producing alkaline keratinase and disulfide reductase |
Rahayu et al., 2012 |
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A metalloprotease with a molecular weight of 134 kDa was purified from the strain |
Lee et al., 2002 |
Bacillus aerius NSMk2 |
Complete degradation of white chicken feather was observed in 3 days |
Bhari et al., 2018 |
Bacillus thuringiensis |
This stain is able to degrade heat-treated feather. Additives in the medium affected feather degradation |
Sahni et al., 2015 |
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A strain AD-12 was able to produce detergent-stable serine keratinolytic proteinase with a molecular weight of 39 kDa. The enzyme was characterized |
Gegeckas et al., 2014 |
Bacillus licheniformis |
A strain K-508 was isolated having feather degrading activity and its fermentation product exhibited protease activity |
Manczinger et al., 2003 |
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A gene of keratinolytic protease was identified in strain PWD-1 that could produce keratinase |
Lin et al., 1992, 1995
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A strain K-508 was able to degrade feather with several proteases secreted |
Manczinger et al., 2003 |
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The crude enzyme produced by strain ALW1 was able to degrade native feather up to 63% in redox free system |
Abdel-Fattah et al., 2018 |
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The strain ATCC 21415 was used to treat biostimulants which can affect bioremediation of soil |
Rodríguez-Morgado et al., 2015 |
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Extracellular proteins of this strain were identified when the strain used different feathers as substrates |
Parrado et al., 2014 |
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The keratinase from strain BBE11-1 was mutated based on computational design. The mutant was expressed in B. subtilis and exhibited enhanced thermal stability |
Liu et al., 2013 |
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A strain ER-15 was able to produce a 58 kDa keratinase which could hydrolyze several protein complexes |
Tiwary and Gupta, 2010 |
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The keratinase produced in this stain was expressed in B. subtilis
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Wang and Shih, 1999 |
Bacillus subtilis |
Whole cell mutagenesis was used to improve the enzymatic activity |
de Paiva et al., 2018 |
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A strain DP1 was isolated and was able to produce keratinase that was stable range of pH (8–12) and temperature (20–50°C) |
Sanghvi et al., 2016 |
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A strain PF1 was used to simultaneously produce keratinolytic protease and other enzymes using feather containing medium |
Bhange et al., 2016b |
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A strain NRC3 was able to produce thermal stable metallo-keratinase (32 kDa) |
Tork et al., 2013 |
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A strain BF11 was able degrade feather |
Jeevana Lakshmi et al., 2013 |
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A strain RM-01 produced keratinase in solid-state fermentation using chicken feathers as substrate |
Rai et al., 2009 |
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Strain S8 was able to degrade feather and produce indoleacetic acid. This strain also exhibited antifungal activities |
Jeong et al., 2010a |
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A strain was able to degrade feathers and the products could also inhibit bacterial growth |
Liu et al., 2017 |
Bacillus pumilus |
Adding cysteine in feather medium could increase enzyme activity |
Kim et al., 2005 |
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A strain was able to produce keratinase using feather as substrate. The produced enzyme was able to remove the blood stains from cloth without affecting its fiber properties |
Ramakrishna Reddy et al., 2017 |
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A strain FH9 was able to produce keratinase which was characterized. KS12 produced a thermal stable enzyme |
Rajput et al., 2010; Abdel-Naby et al., 2017
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A strain A1 was able to degrade feathers and the produced feather protein hydrolysate exhibited antioxidant activity |
Fakhfakh et al., 2011 |
Bacillus sphaericus and Bacillus thuringiensis israelensis
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This entomopathogenic bacterial were able to degrade feathers, indicating that this waste can be converted into mosquitocidal biopesticides |
Poopathi and Abidha, 2008 |
Bacillus tequilensis |
A 28 kDa protease was overexpressed in E. coli and purified |
Zaraî Jaouadi et al., 2015 |
Bacillus pseudofirmus |
A strain FA30-1 was able to degrade feather completely and an enzyme was purified |
Kojima et al., 2006 |
Brevibacillus parabrevis |
A surfactant-resistant enzyme was purified from this strain |
Zhang et al., 2016 |
Bacillus megaterium |
A strain SN1 was able to degrade feather and produce caesinolytic enzyme in feather medium |
Agrahari and Wadhwa, 2012 |
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A strain was found to be able to degrade feathers and other keratin-rich materials |
Park and Son, 2009 |
Brevibacillus sp. |
Production and purification of one 83.2 kDa keratinase from strain AS-S10-II were carried out |
Rai and Mukherjee, 2011 |
Chryseobacterium sediminis |
This strain was able to grow using feather as sole carbon and nitrogen sources. It degraded feather and antioxidant and indole-3-acetic acid production were observed |
Kshetri et al., 2019 |
Fusarium sp. |
This strain was found to be efficient in keratin degradation |
Cǎlin et al., 2017 |
Fervidobacterium islandicum |
A thermophilic anaerobe was able to produce amino acids by degrading feathers. A 97 kDa enzyme could form oligomers |
Nam et al., 2002 |
Stenotrophomonas sp. |
Screened strains mostly identified as S. maltophilia and S. rhizophila were able to produce keratinase |
Herzog et al., 2016 |
Geobacillus stearothermophilus |
The genome of this strain encodes a keratinolytic protease which was overexpressed in E. coli. The enzyme was purified and characterized |
Gegeckas et al., 2015 |
Chryseobacterium sp. |
A bacterium kr6 was able to produce feather hydrolysates which exhibited antioxidant and antihypertensive activities |
Lin et al., 1992; Fontoura et al., 2014
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Effect of nutritional conditions on enzyme product by kr6 was explored |
Riffel et al., 2011 |
Micrococcus sp. |
A study showed that this strain was able to produce several keratinases with high molecular weights |
Laba et al., 2015 |
Pseudomonas stutzeri |
This strain K4 was able to metabolize chicken feather. It could produce five keratinases |
Chaturvedi et al., 2014 |
Pseudomonas aeruginosa |
A 33 kDa keratinase was purified from strain C11 which could degrade feathers |
Han et al., 2012 |
Pseudomonas sp. |
A 30 kDa keratinase was isolated from a Pseudomonas strain |
Tork et al., 2010 |
Paenibacillus woosongensis |
A strain could grow in a feather medium and produce keratinases. The resulting product promoted plant growth |
Paul et al., 2013 |
Xanthomonas sp. |
A strain P5 was able to degrade feather through enzymes |
Jeong et al., 2010c |
Nesterenkonia sp. |
A strain AL20 produced protease in the presence of chicken feather. The substrate specificity was explored |
Bakhtiar et al., 2005 |
Serratia sp. |
A feather hydrolyzing enzyme was obtained from this strain. Feather substrate was able to increase the enzyme production. This enzyme was active at 60°C and pH 10 |
Khardenavis et al., 2009 |
Stenotrophomonas sp. |
A strain D-1 was isolated and able to degrade chicken feather at 20°C in 2.5 days |
Yamamura et al., 2002a |
Serratia marcescens |
Strain P3 was able to be produce a 53 kDa keratinase belonging to the serralysin family |
Bach et al., 2012 |
Vibrio sp. |
A strain was able to degrade feathers |
Bockle and Muller, 1997; Grazziotin et al., 2007
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