A Surfactant-stable Bacillus pumilus K9 α-Keratinase and Its Potential Application in Detergent Industry

doi:10.1007/s40242-015-4351-8

Chemical Research in Chinese Universities ›› 2015, Vol. 31 ›› Issue (1): 91-97.doi: 10.1007/s40242-015-4351-8

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A Surfactant-stable Bacillus pumilus K9 α-Keratinase and Its Potential Application in Detergent Industry

GONG Jinsong, WANG Yue, ZHANG D, an, LI Heng, ZHANG Xiaomei, ZHANG Rongxian, LU Zhenming, XU Zhenghong, SHI Jinsong

School of Pharmaceutical Science, Jiangnan University, Wuxi 214122, P. R. China

Received:2014-09-22 Revised:2014-11-26 Online:2015-02-01 Published:2014-12-01
Contact: SHI Jinsong, E-mail:shijs@163.com E-mail:shijs@163.com
Supported by:
Supported by the National High Technology Research and Development Program of China(No.2012AA022204C) and the National Natural Science Foundation of China(No.21406088).

Abstract

Abstract:

An α-keratinase producing strain was isolated with wool as the sole carbon and nitrogen source and identified as Bacillus pumilus K9. The major amino acids liberated from the keratin degradation of wool by B. pumilus K9 were glutamic acid and leucine. The α-keratinase was purified to electrophoretic homogeneity with a molecular weight of 32000. The purified enzyme exhibits an optimum activity at 60 ℃ and pH=9.0. It was stable at pH values between 8 and 11. Bacillas pumilus keratinase displays a high activity towards casein, keratin, wool and feather, which indicates its wide application range. The keratinase was completely inhibited by phenylmethyl-sulfonyl fluoride(PMSF) and β-mercaptoethanol, and moderately inhibited by ethylemediamine-tetraacetic acid(EDTA), sugges-ting it is a metallo-cysteine keratinase. This enzyme could remain stable that could even be promoted in the presence of surfactants, including sodium dodecyl sulfate(SDS), Tween and Triton. And Tween 40 and Triton X-100 could substantially enhance the activity of the enzyme by 54% and 35%, respectively. It may indicate the prominent feature of the keratinase to tolerate surfactants. The enzymatic properties distinguish this keratinase from others in the literature. Furthermore, this enzyme is extremely stable in the presence of a commercially available detergent with 1% concentration. Detergents ARIEL, Bluemoon and WhiteCat can enhance the activity of the keratinase by 43.56%, 15.22%, and 22.48%, respectively.

Key words: α-Keratinase, Bacillus pumilus K9, Wool degradation, Surfactant stability, Detergent

GONG Jinsong, WANG Yue, ZHANG D, an, LI Heng, ZHANG Xiaomei, ZHANG Rongxian, LU Zhenming, XU Zhenghong, SHI Jinsong. A Surfactant-stable Bacillus pumilus K9 α-Keratinase and Its Potential Application in Detergent Industry[J]. Chemical Research in Chinese Universities, 2015, 31(1): 91-97.

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A Surfactant-stable Bacillus pumilus K9 α-Keratinase and Its Potential Application in Detergent Industry

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