Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis

A new keratinase producer, Bacillus sp. BK111, isolated from a poultry feather was identified as Bacillus zhangzhouensis , which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical ass...

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Bibliographic Details
Published in:Extremophiles : life under extreme conditions 2020-09, Vol.24 (5), p.693-704
Main Authors: Moridshahi, Roghyeh, Bahreini, Masoumeh, Sharifmoghaddam, Mohammadreza, Asoodeh, Ahmad
Format: Article
Language:English
Subjects:
Acetone
Bacillus zhangzhouensis
Biochemistry
Biomedical and Life Sciences
Biotechnology
Calcium
Calcium ions
Dimethyl sulfoxide
Dithiothreitol
Enzymatic activity
Enzyme activity
Enzymes
Ethanol
Feathers
Keratinase
Keratinocytes
Life Sciences
Metal ions
Metals
Microbial Ecology
Microbiology
Molecular weight
Original Paper
pH effects
Propanol
Reducing agents
Serine
Serine proteinase
Space life sciences
Stability
Substrates
Temperature effects
Water purification
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Summary:A new keratinase producer, Bacillus sp. BK111, isolated from a poultry feather was identified as Bacillus zhangzhouensis , which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical assays. A 2.34-fold increase was observed in the enzyme production under optimized conditions. The enzyme was characterized as a serine protease with 42 kDa molecular weight, stable in a wide range of temperature and pH with maximum keratinolytic activity at 60 °C and pH 9.5. The enzyme had a wide range of different substrates with the best performance on the feather meal substrate. Metal ions of Ca 2+ , K + , Na + and Mn 2+ enhanced the enzyme activity. The enzyme showed a great deal of stability in the presence of ethanol, methanol, acetone, 2-propanol, dimethyl sulfoxide, Tween-80 and Triton X-100. Dithiothreitol (DTT), as a reducing agent, caused a twofold increase in keratinolytic activity. The half-life of the enzyme at optimum temperature was calculated to be 125 min and the ratio of keratinolytic:caseinolytic for the enzyme was 0.8. Our results showed the remarkable features of the enzyme that make it suitable for biotechnological usages.
ISSN:1431-0651
1433-4909
DOI:10.1007/s00792-020-01187-9