PURIFICATION AND CHARACTERIZATION OF A KERATINASE FROM A FEATHER-DEGRADING BACILLUS-LICHENIFORMIS STRAIN

被引:268
作者
LIN, XA
LEE, CG
CASALE, ES
SHIH, JCH
机构
[1] N CAROLINA STATE UNIV,DEPT POULTRY SCI,RALEIGH,NC 27695
[2] SHENYANG AGR UNIV,SHENYANG,PEOPLES R CHINA
[3] N CAROLINA STATE UNIV,BIOTECHNOL PROGRAM,RALEIGH,NC 27695
关键词
D O I
10.1128/AEM.58.10.3271-3275.1992
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A keratinase was isolated from the culture medium of feather-degrading Bacillus licheniformis PWD-1 by use of an assay of the hydrolysis of azokeratin. Membrane ultrafiltration and carboxymethyl cellulose ion-exchange and Sephadex G-75 gel chromatographies were used to purify the enzyme. The specific activity of the purified keratinase relative to that in the original medium was approximately 70-fold. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and Sephadex G-75 chromatography indicated that the purified keratinase is monomeric and has a molecular mass of 33 kDa. The optimum pH and the pI were determined to be 7.5 and 7.25, respectively. Under standard assay conditions, the apparent temperature optimum was 50-degrees-C. The enzyme is stable when stored at -20-degrees-C. The purified keratinase hydrolyzes a broad range of substrates and displays higher proteolytic activity than most proteases. In practical applications, keratinase is a useful enzyme for promoting the hydrolysis of feather keratin and improving the digestibility of feather meal.
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页码:3271 / 3275
页数:5
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