Keratinolytic enzyme-mediated biodegradation of recalcitrant poultry feathers waste by newly isolated Bacillus sp. NKSP-7 under submerged fermentation

Microbial and enzymatic degradation of keratin waste is more preferred over various conventional approaches which are costly and not environmentally suitable. Diverse niches are auspicious for the discovery of new microorganisms. To discover novel keratinolytic bacteria, 60 isolates from different p...

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Bibliographic Details
Published in:Folia microbiologica 2020-10, Vol.65 (5), p.823-834
Main Authors: Haq, Ikram ul, Akram, Fatima, Jabbar, Zuriat
Format: Article
Language:English
Subjects:
Animal wastes
Animals
Applied Microbiology
Bacillus
Bacillus - classification
Bacillus - genetics
Bacillus - isolation & purification
Bacillus - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bioconversion
Biodegradation
Biodegradation, Environmental
Biomedical and Life Sciences
Cadmium
Cations
Chickens
Dehairing
Detergents
Dumping
Environmental Engineering/Biotechnology
Enzymatic activity
Enzyme activity
Enzymes
Ethylenediaminetetraacetic acids
Feathers
Feathers - chemistry
Feathers - metabolism
Fermentation
Hydrogen-Ion Concentration
Immunology
Industrial applications
Keratin
Keratinase
Keratinocytes
Keratins - analysis
Keratins - metabolism
Leather
Life Sciences
Microbiology
Microorganisms
Molecular Weight
Organic solvents
Original Article
Peptide Hydrolases - chemistry
Peptide Hydrolases - genetics
Peptide Hydrolases - metabolism
pH effects
Physical characteristics
Physiochemistry
Poultry
Proteolysis
Refuse Disposal - methods
RNA, Ribosomal, 16S - genetics
rRNA 16S
Substrates
Temperature
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Summary:Microbial and enzymatic degradation of keratin waste is more preferred over various conventional approaches which are costly and not environmentally suitable. Diverse niches are auspicious for the discovery of new microorganisms. To discover novel keratinolytic bacteria, 60 isolates from different poultry dumping sites were initially screened, and among these found a potent keratinolytic isolate (NKSP-7) that displayed higher feather-degrading ability. The selected isolate was identified as Bacillus sp. NKSP-7 based on 16S rDNA sequencing as well as physiochemical and morphological characteristics. The strain NKSP-7 showed complete hydrolysis of native chicken feathers (10 g/L) in nutrient medium after 24 h of incubation at 37 °C under agitation (150 rev/min) and produced thermostable extracellular keratinase. The crude enzyme displayed maximal keratinolytic activity (34.7 U/mL) in phosphate buffer of pH 7.0, and at 60 °C using keratin azure as a substrate. Keratinolytic enzyme showed stability at 20–65 °C for 4 h over the pH range of 5.5–8.0. No obvious inhibitory influence was perceived by cations, organic solvents, EDTA, and detergents. Whereas, enzyme activity was enhanced by adding β-mercaptoethanol, Na + , Cd 2+ , and Mn 2+ . All these notable features of keratinase make it a promising candidate for various industrial applications especially for dehairing process in leather industry, bioconversion of poultry waste, and in detergents formulations.
ISSN:0015-5632
1874-9356
DOI:10.1007/s12223-020-00793-6