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 Vol. 24; no. 5; pp. 693 - 704
Main Authors:	Moridshahi, Roghyeh, Bahreini, Masoumeh, Sharifmoghaddam, Mohammadreza, Asoodeh, Ahmad
Format:	Journal Article
Language:	English
Published:	Tokyo Springer Japan 01-09-2020 Springer Nature B.V
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 Keratinase Characterization Feather biodegradation Optimization
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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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1431-0651 1433-4909
DOI:	10.1007/s00792-020-01187-9