Keratin hydrolysis by dermatophytes

2018 ◽  
Vol 57 (1) ◽  
pp. 13-22 ◽  
Author(s):  
Derry K Mercer ◽  
Colin S Stewart
Keyword(s):  
1933 ◽  
Vol 10 (3) ◽  
pp. 237-246
Author(s):  
M. J. MACKERRAS ◽  
M. R. FRENEY

1. Larvae of L. cuprina and Ch. rufifacies are capable of liquefying and digesting protein media without the intervention of bacteria. Both species and L. sericata secrete tryptic and peptic enzymes and at least L. cuprina does so from the moment of hatching. Tryptase is more abundant than peptase. Predatory activity, though a normal habit of Ch. rufifacies, is not necessary for any of these species and did not occur in the masses of Lucilia larvae used for extraction of the enzymes, although they were kept for periods up to 24 hours without food. 2. Partial development of larvae occurred in sheep dung, faeces-stained wool and in the products of keratin hydrolysis. Complete development took place in wool containing a "gummy crust" of dried exudate and in some samples of faeces-stained wool. Some of the samples of faeces-stained wool and those containing a "crust" have been demonstrated serologically by Dr I. M. Mackerras to have an increased content of soluble sheep protein as compared with normal wool. A marked increase of soluble protein has been demonstrated in struck wool both chemically and serologically. 3. Moisture, warmth, shelter and aeration are essential physical conditions for larval development. In addition, an alkaline reaction is relatively favourable and an acid reaction relatively unfavourable. 4. There are normally two stages in the development of a primary strike, the first stage being from hatching up to the time the larvae attack the skin, the outer layer or epidermis of which is approximately 36µ thick (Whitnall, 1931). During this stage they must feed, if at all, on materials already present. The second stage is from the commencement of an actual skin lesion up to full development of the maggots. During this stage there is a more or less copious serous exudation, which has been shown to be an adequate food for the full development of the maggots. Faeces-staining, presence of exudate due to a prior lesion, and products of wool hydrolysis have been shown to be adequate to carry the larvae through the first stage. Wool hydrolysis on the living sheep is probably not an important factor, judging by an examination of wool samples, but we have isolated organisms which, when growing on a nutrient medium, are capable of disintegrating wool fibre. 5. The rôle of bacterial activity in strike is complex and appears to be substantially as follows: (a) to produce substances which attract the flies and stimulate them to oviposit; (b) to provide food for the initial growth of the maggots, either by rendering assimilable the inert proteins, or by causing a skin reaction with a serous exudation. 6. The immediate work for the future is a more exact determination of: (a) the nature of the food of the larvae in the early stage of growth on the living sheep; (b) the factors which influence its production; and (c) the mechanism by which the larvae invade the skin.


Author(s):  
Jing-Iong Yang ◽  
Jen-Min Kuo ◽  
Wen-Ming Chen ◽  
Huei-Jing Ke ◽  
Yi-Ju Chou

After undergoing keratinase digestion, feather wastes could have a great potential as a source of proteins and amino acids for many applications. In this study, the fermentation conditions of feather-degrading Meiothermus sp. strain I40 (I40) were optimized to enhance the biodegradation of chicken feather to hydrolysates. Initially, the factors essential for I40 keratinase production in submerged fermentation were screened, whereas response surface methodology (RSM) was then employed to evaluate the interactions among the effective factors. At first stage, eight fermentation parameters were screened using a Plackett-Burman (PB) design. Four effective factors identified by PB screening, namely feather concentration, tryptone concentration, yeast extract concentration, and incubation temperature, were further investigated their effects on keratinase production by RSM using central composite design (CCD). The I40 fermentation conditions for maximal keratinase activity were as follows: tryptone concentration 0.16 percent (w/v), yeast extract concentration 0.27 percent (w/v), feather concentration 0.08 percent (w/v), and incubation temperature at 51.7°C for 72 hr under 120 rev/min shaking. Compared to the initial stage, a 13.3-fold increase in keratinase activity was achieved when I40 incubated in the optimized conditions.


2000 ◽  
Vol 46 (11) ◽  
pp. 1004-1011 ◽  
Author(s):  
Kristie L Evans ◽  
Jamie Crowder ◽  
Eric S Miller

Keratinase is a serine protease produced by Bacillus licheniformis PWD-1 that effectively degrades keratin and confers the ability to grow on feathers to a protease-deficient B. subtilis strain. Studies presented herein demonstrate that B. licheniformis Carlsberg strain NCIMB 6816, which produces the well-characterized serine protease subtilisin Carlsberg, also degrades and grows on feathers. The PWD-1 and Carlsberg strains showed a similar time-course of enzyme production, and the purified serine proteases have similar enzymatic properties on insoluble azokeratin and soluble FITC-casein. Kinetic analysis of both enzymes demonstrated that they have high specificity for aromatic and hydrophobic amino acids in the P1 substrate position, although keratinase discriminates more than subtilisin Carlsberg against charged residues at this site. Nucleotide sequence analysis of the serine protease genes from B. licheniformis strains PWD-1, Carlsberg NCIMB 6816, ATCC 12759, and NCIMB 10689 showed that the kerA-encoded protease of PWD-1 differs from the others only by having V222, rather than A222, near the active site serine S220. Further, high-level expression of subE-encoded subtilisin from B. subtilis (78% similar to subtilisin Carlsberg) also confers growth on feathers on a protease-deficient B. subtilis strain. While strain PWD-1 and the kerA protease efficiently degrade keratin, keratin hydrolysis and growth on feathers is a property that can be conferred by appropriate expression of the major subtilisins, including the industrially produced enzymes.Key words: keratin hydrolysis, Bacillus, subtilisin, keratinase.


Author(s):  
Wafa A. Alshehri ◽  
Ashjan Khalel ◽  
Khaled Elbanna ◽  
Iqbal Ahmad ◽  
Hussein H. Abulreesh

Plastic materials have become a necessity of human life especially in the packaging of food commodities and biomedical procedures. Bioplastic is emerging as an effective alternative to fossil oil-based materials to avoid the environmental hazards of the plastic industry. During this study, chicken feathers were used as a substrate to isolate keratin degrading bacteria. Among 14 identified isolates, Bacillus sp BAM3 was found to be the most promising isolate. Partial 16S rDNA analysis-based molecular characterization revealed it is a strain of Bacillus cereus. Bacillus sp BAM3 can grow and produce keratinase in feathers containing basal medium as the sole carbon and energy source. The maximum keratinase production (730U/ml) was achieved within 24 h under optimum reaction conditions. The optimized reaction pH and temperature were noted as 9.0 and 50 °C for crude keratinase activity, respectively. The chicken feathers were used as a substrate in 2, 5, and 10 wt% glycerol to synthesize keratin-based bioplastic with keratinolytic bacterium Bacillus cereus BAM3. Bioplastic prepared from keratin with 2% of glycerol was found to possess good mechanical properties. Therefore, the results present a novel keratinolytic isolate of Bacillus cereus BAM3, which may have potential biotechnological applications in keratin hydrolysis processes. The development of keratin-based bioplastics possessing superior crystalline morphology requires further investigations to substitute fossil oil-based materials.


2000 ◽  
Vol 89 (5) ◽  
pp. 735-743 ◽  
Author(s):  
S. Sangali ◽  
A. Brandelli

Author(s):  
Hesham Elkomy ◽  
Sahar Al-Dosary ◽  
Mohamed El-Naghy ◽  
Mohamed Abdelhamid ◽  
Mohamed Immam
Keyword(s):  

2013 ◽  
Vol 133 ◽  
pp. 635-637 ◽  
Author(s):  
Lisheng Xu ◽  
Zhiyuan Wang ◽  
Pingting Mao ◽  
Junzhong Liu ◽  
Hongjuan Zhang ◽  
...  

2014 ◽  
Vol 02 (01) ◽  
pp. 49-53 ◽  
Author(s):  
Nanami Hara ◽  
Shintaro Morisada ◽  
Keisuke Ohto ◽  
Hidetaka Kawakita

2022 ◽  
Vol 28 ◽  
Author(s):  
Antoni Taraszkiewicz ◽  
Izabela Sinkiewicz ◽  
Agata Sommer ◽  
Małgorzata Dąbrowska ◽  
Hanna Staroszczyk

Background: Keratin is among the most abundant structural proteins of animal origin, however it remains broadly underutilized. Objective: Bioinformatic investigation was performed to evaluate selected keratins originating from mass-produced waste products, i.e., chicken feathers and pig hair, as potential sources of bioactive peptides. Methods: Pepsin, trypsin, chymotrypsin, papain, and subtilisin were used for in silico keratinolysis with the use of “Enzyme(s) action” and fragmentomic analysis of theoretical products was performed using “Profiles of potential biological activity” in BIOPEP-UWM database of bioactive peptides. Bioactivity probability calculation and toxicity prediction of the peptides obtained were estimated using PeptideRanker and ToxinPred tools, respectively. Results: Our results showed that the keratins are a potential source of a variety of biopeptides, including dipeptidyl peptidase IV, angiotensin converting enzyme, prolyl endopeptidase inhibitory and antioxidative. Papain and subtilisin were found to be the most appropriate enzymes for keratin hydrolysis. This study presents possible structures of keratin-derived bioactive peptides that have not been previously described. Conclusion: Our data suggest additional in vitro and in vivo studies to verify theoretical predictions and further investigate the possibility of using keratin-rich waste as a source of peptide nutraceuticals.


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