Keratin degradation: a cooperative action of two enzymes from Stenotrophomonas sp.

Yamamura, Shohei; Morita, Yasutaka; Hasan, Quamrul; Yokoyama, Kenji; Tamiya, Eiichi

doi:10.1016/s0006-291x(02)00580-6

Cited by 181 publications

(129 citation statements)

References 22 publications

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“…Majority of the feather meal production involves fermentation using keratinolytic microbes and subsequent fermentation broth was regarded as feather meal [2,6,11,15]. During fermentation, feather degradation is supposed to be achieved by co-operative action of protease and cell redox [16][17][18]. In this context, present process is better than the existing ones since no fermentation is required for feather meal production.…”

Section: Effect Of Enzyme Concentrationmentioning

confidence: 99%

Rapid Conversion of Chicken Feather to Feather Meal Using Dimeric Keratinase from Bacillus licheniformis ER-15

Tiwary¹,

Gupta²

2012

J Bioproces Biotechniq

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Section: Effect Of Enzyme Concentrationmentioning

confidence: 99%

Rapid Conversion of Chicken Feather to Feather Meal Using Dimeric Keratinase from Bacillus licheniformis ER-15

Tiwary¹,

Gupta²

2012

J Bioproces Biotechniq

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“…Similar results were reported by Cheng et al (4) for the bacterial keratinase of Bacillus licheniformis. Generally, the keratinases reported in the literature were 5-to 20-fold more active on keratinous substrates than other proteases (2,3,21,39).…”

mentioning

confidence: 97%

Similarities and Specificities of Fungal Keratinolytic Proteases: Comparison of Keratinases of Paecilomyces marquandii and Doratomyces microsporus to Some Known Proteases

Gradišar

Friedrich

Križaj

et al. 2005

Appl Environ Microbiol

207

112

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Based on previous screening for keratinolytic nonpathogenic fungi, Paecilomyces marquandii and Doratomyces microsporus were selected for production of potent keratinases. The enzymes were purified and their main biochemical characteristics were determined (molecular masses, optimal temperature and pH for keratinolytic activity, N-terminal amino acid sequences). Studies of substrate specificity revealed that skin constituents, such as the stratum corneum, and appendages such as nail but not hair, feather, and wool were efficiently hydrolyzed by the P. marquandii keratinase and about 40% less by the D. microsporus keratinase. Hydrolysis of keratin could be increased by the presence of reducing agents. The catalytic properties of the keratinases were studied and compared to those of some known commercial proteases. The profile of the oxidized insulin B-chain digestion revealed that both keratinases, like proteinase K but not subtilisin, trypsin, or elastase, possess broad cleavage specificity with a preference for aromatic and nonpolar amino acid residues at the P-1 position. Kinetic studies were performed on a synthetic substrate, succinyl-Ala-Ala-Pro-Phe-p-nitroanilide. The keratinase of P. marquandii exhibited the lowest K m among microbial keratinases reported in the literature, and its catalytic efficiency was high in comparison to that of D. microsporus keratinase and proteinase K. All three keratinolytic enzymes, the keratinases of P. marquandii and D. microsporus as well as proteinase K, were significantly more active on keratin than subtilisin, trypsin, elastase, chymotrypsin, or collagenase.Keratins are the most abundant proteins in epithelial cells of vertebrates and represent the major constituents of skin and its appendages such as nail, hair, feather, and wool. The protein chains are packed tightly either in ␣-chain (␣-keratins) or in ␤-sheet (␤-keratins) structures. Keratins belong to the superfamily of intermediate filament proteins. Their high degree of cross-linking by disulfide bonds, hydrophobic interactions, and hydrogen bonds stabilizes keratin filament structure (11). Therefore, keratinous material is water insoluble and extremely resistant to degradation by proteolytic enzymes such as trypsin, pepsin, and papain.A group of proteolytic enzymes which are able to hydrolyze insoluble keratins more efficiently than other proteases are called keratinases (29). They are produced by some insects and mostly by microorganisms. The best studied are keratinases from the dermatophytic genera Microsporum (26, 37) and Trichophyton (30, 38) as well as from bacteria of the genera Bacillus (4,14,20,24,34,35) and Streptomyces (2, 3, 27). There are relatively few reports on characterization of the keratinases from nondermatophytic fungi (5,7,12,25,32,33).Most keratinases have some common characteristics despite their different origins. They belong mainly to the extracellular serine proteases, with the exception of keratinases from yeasts, which belong to the aspartic proteases (23, 28). The molecular masses of ...

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“…Keratin is a stiff structural protein extensively cross-linked by intermolecular disulphide bonds (-S-S-) between the thiol groups of cysteine residues (Alibardi andToni 2005, Swadźba et al 2009). As Savinase hydrolyzes only the peptide bonds in proteins and does not exhibit disulphide reduction properties, the keratin part is left undigested (Letourneau et al 1998, Yamamura et al 2002.…”

Section: Preparation Of Skeletal Materials From Formalin-fixed Specimensmentioning

confidence: 99%

Enzymatic detection of formalin-fixed museum specimens for DNA analysis and enzymatic maceration of formalin-fixed specimens

Sørensen¹,

Rasmussen²,

Симонсен³

2016

Collection Forum

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Abstract.-A simple enzymatic screening method has been developed to detect whether a tissue sample has been preserved with formalin or with ethanol only because such a method is a useful tool for predicting the quality of genetic test results. The method is based on enzymatic digestion at 55uC at neutral pH. The screening method shows that only ethanol-preserved tissue samples are dissolved, whereas formalin-preserved samples remain undissolved. The method was developed by the incorporation of laboratory rats preserved under controlled conditions in either 4% neutral buffered formalin or 96% ethanol. The method was subsequently tested on wild-living preserved specimens and an archived specimen. The protease enzyme used was SavinaseH 16 L, Type EX from Novozymes A/S. The enzymatic screening test demands only simple laboratory equipment. The method is useful for natural history collections in museums where DNA analyses of archived specimens are performed. Wasted time and resources can be avoided through the detection of formalin-fixed specimens because these specimens yield low-quality, damaged DNA. In addition to the screening method, it is shown that formalin-preserved specimens can be macerated by enzymatic digestion under alkaline conditions at 55uC.

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Keratin degradation: a cooperative action of two enzymes from Stenotrophomonas sp.

Cited by 181 publications

References 22 publications

Rapid Conversion of Chicken Feather to Feather Meal Using Dimeric Keratinase from Bacillus licheniformis ER-15

Rapid Conversion of Chicken Feather to Feather Meal Using Dimeric Keratinase from Bacillus licheniformis ER-15

Similarities and Specificities of Fungal Keratinolytic Proteases: Comparison of Keratinases of Paecilomyces marquandii and Doratomyces microsporus to Some Known Proteases

Enzymatic detection of formalin-fixed museum specimens for DNA analysis and enzymatic maceration of formalin-fixed specimens

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