نتایج جستجو برای: keratinase activity

تعداد نتایج: 1134469  

2013
Emeka A. Okoroma Diane Purchase Hemda Garelick Roger Morris Michael H. Neale Otto Windl Oduola O. Abiola

The prion agent is notoriously resistant to common proteases and conventional sterilisation procedures. The current methods known to destroy prion infectivity such as incineration, alkaline and thermal hydrolysis are harsh, destructive, environmentally polluting and potentially hazardous, thus limit their applications for decontamination of delicate medical and laboratory devices, remediation o...

2010
MS Ranjith

Dermatophytes can digest keratin and other proteinaceous substrates present in skin and its appendages such as nail, hair, and feather and use it as its sole source of carbon and nitrogen. Proteolytic and keratinolytic activities of dermatophytes have been a subject of interest for several years to understand the pathogenicity of infection. In this study we intend to elucidate the keratinase ac...

Journal: :IOP conference series 2022

Abstract This study aims to evaluate the capability of extracellular protease hydrolyze keratin substrates local poultry feathers and observing amino acid profile. The indigenous strains ( Bacillus cereus TD5B, LS2B, Pseudomonas sp. PK4) were used in this study, obtained data analysed descriptively. TD5B has a maximum activity at 0.003849062 unit/ml 0.000310042 on casein commercial substrates. ...

2011
E Vijay Kumar M Srijana K Chaitanya Y Harish Kumar Reddy Gopal Reddy

Keratinolytic microorganisms have great importance in feather waste degradation and its use for improvement of livestock feed and production of protein hydrolysates. Bacillus altitudinis GVC11, a novel, raw chicken feather degrading bacterium, previously isolated and identified by morphological, biochemical and 16s rDNA sequencing in our laboratory, was used in the present study. It was grown i...

Journal: :The Biochemical journal 2005
R P Hobson

IT is well known that sclero-proteins are not readily digested by the enzymes of vertebrates; both pepsin and trypsin act upon elastin, collagen is very resistant to trypsin but is digested by pepsin, and keratin is not attacked by either enzyme. However, Stankovic, Arnovlzevic and Matavulj [1929] have described a keratinase from the crops of certain birds of prey and Ssadikov [1927] has claime...

Journal: :Fermentation 2023

A distinctive isolate was discovered and visually recognized as a member of the genus Didymella during routine examination Coelomycetes isolated from diverse fruit juices. Based on sequencing internal transcribed spacer (ITS), fungus identified keratinophila since it showed 100% identity to type strain. The strain thrived produced keratinase collagenase enzymes by hydrolyzing native chicken fea...

Journal: :Process Biochemistry 2021

Two novel extracellular keratinases were produced by Actinomadura keratinilytica strain Cpt20. Both enzymes purified to homogeneity using heat-treatment (60 °C for 30 min) and ammonium sulfate salt fractionation (40 %–70 %), followed anion-exchange chromatography with fast protein liquid (FPLC) system. The keratinases, designated as KERA-71 KERB-19, are monomeric named according their molecular...

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