Purification and characterization of a novel exocellular keratinase from Kocuria rosea

Bernal, Cristobal; Cairo, João Paulo L. Franco; Coello, Nereida

doi:10.1016/j.enzmictec.2005.02.021

Cited by 87 publications

(57 citation statements)

References 26 publications

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“…Keratinases from Kocuria rosea (240 kDa), Fervidobacterium islandicum (200 kDa) and Bacillus cereus 1268 (200 kDa) have been found (Bernal et al 2006;Mazotto et al 2011;Nam et al 2002). A peptidase from the pathogenic bacterium Campylobacter jejuni was described with high molecular mass (170 kDa) (Karlyshev et al 2014).…”

Section: Discussionmentioning

confidence: 97%

Extracellular peptidases from Deinococcus radiodurans

et al. 2015

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The extremophile Deinococcus radiodurans wild type R1 produces peptidases (metallo- and serine-) in TGY medium and in the media supplemented with human hair (HMY) and chicken feathers (FMY). Enzymatic screening on agar plates revealed peptidase activity. In TGY medium metallopeptidases were detected corresponding to a molecular mass range of 300-85 kDa (gelatinases); 280-130 (caseinases) and a 300 and a 170 kDa (keratinases); and a gelatinolytic serine peptidase (75 kDa). In HMY medium after 144 h, D. radiodurans produced keratinase (290 U/ml), gelatinase (619 U/ml) and sulfite (26 µg/ml). TGY medium produced higher proteolytic activity: 950 U/ml of gelatinolytic (24 h); 470 U/ml of keratinolytic (24 h) and 110 U/ml of caseinolytic (72 h). In the FMY medium, we found gelatinolytic (317 U/ml), keratinolytic (43 U/ml) and caseinolytic (85 U/ml) activities. The sulfite had a maximum release at 48 h (8.1 µg/ml). Enzymography analysis revealed that the keratinases degraded keratin after 24 h of reaction. The addition of sodium sulfite (1.0 %) improved the keratin degradation. Environmental Scanning Electron microscopy revealed alterations such as damage and holes in the hair fiber cuticle after D. radiodurans growth. This work presents for the first time D. radiodurans as a new keratinolytic microorganism.

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Section: Discussionmentioning

confidence: 97%

Extracellular peptidases from Deinococcus radiodurans

et al. 2015

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“…The majority of keratinases reported are alkaline in nature [2]. It is assumed that alkaline conditions aid in the breaking of disulfide bonds and assist rapid feather degradation.…”

Section: Discussionmentioning

confidence: 99%

“…By virtue of their ability to attack hard-to-degrade proteins, keratinases occupy a special niche among proteases [6]. They find immense biotechnological applications in the leather and cosmetic industries, where they have the advantage of being used in non-polluting processes [2]. Lately, it has been reported that keratinases that degrade feather could be potential catalysts for dissolution of prion plaques since both these proteins have similarly aggregated b-sheet structures [7].…”

Section: Introductionmentioning

confidence: 99%

Substrate specificity characterization of a thermostable keratinase from Pseudomonas aeruginosa KS-1

Sharma

Gupta

2010

J Ind Microbiol Biotechnol

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A feather-degrading strain of Pseudomonas aeruginosa KS-1 was used in the present study. Its crude cell-free fermentation broth completely degraded chicken feather within 12 h, in the absence of disulphide reductase activity. Keratinase from its extracellular broth was purified and characterized, assuming that it would be a potential beta-keratin-degrading enzyme with prospective applications in degradation of beta-plaques of prions. The keratinase was purified by using Q-Sepharose anion exchange chromatography and its molecular weight, as determined by SDS-PAGE analysis, was 45 kDa. It was an alkaline, serine protease with pH and temperature optima of 9 and 60 degrees C, respectively. The enzyme was highly thermostable with a t (1/2) > 2 h at 80 degrees C and had a very high K to C (keratinolytic to caseinolytic) ratio of 2.5. Besides feather keratin, it also hydrolyzed a variety of other complex substrates including fibrin, gelatin and meat protein. Its activity on synthetic substrates revealed that it efficiently cleaves them in the order phenylalanine > lysine > alanine > leucine p-nitroanilides. It also cleaved insulin B chain between Val(12)-Glu(13), Ala(14)-Leu(15), Gly(20)-Glu(21) and Arg(22)-Gly(23) residues.

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“…Other substrates that are susceptible to keratinase degradation include: collagen (Fang et al 2013;Bernal et al 2006a;Farag and Hassan 2004); elastin Bressollier et al 1999); gelatine (Tork et al 2013;Lopes et al 2008); albumin and haemoglobin (Benkiar et al 2013;Lopes et al 2008), fibrin (Tiwary and Gupta 2010;Tork et al 2013). …”

Section: Keratinous Substrates and Their Specificitiesmentioning

confidence: 99%

Microbial keratinases: characteristics, biotechnological applications and potential.

Purchase

2016

The Handbook of Microbial Bioresources

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Keratinases are a group of proteolytic enzymes that can catalyse the cleavage and hydrolysis of the highly stable and fibrous proteins: keratins. A diverse range of microorganisms, including fungi, actinomycetes and bacteria, have been reported to produce keratinases that have biotechnological applications and potential. These keratinases have been usefully applied in agricultural, pharmaceutical, leather and textile processes as well as within environmentally friendly waste management solutions. Potential uses of keratinases include the fields of biomedicine, cosmetics, biological control and the generation of green energy. Herein we aim to provide an overview of the properties of this group of versatile enzymes, including the mechanisms of keratin degradation. The diversity of microbial sources of keratinases is discussed and the optimisation of keratianse production examined.We conclude with an assessment of the established biotechnological applications of keratinases in different industries and current research that highlights other promising potential uses.

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Purification and characterization of a novel exocellular keratinase from Kocuria rosea

Cited by 87 publications

References 26 publications

Extracellular peptidases from Deinococcus radiodurans

Extracellular peptidases from Deinococcus radiodurans

Substrate specificity characterization of a thermostable keratinase from Pseudomonas aeruginosa KS-1

Microbial keratinases: characteristics, biotechnological applications and potential.

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