Characterization of an alkaline active thiol forming extracellular serine keratinase by the newly isolated Bacillus pumilus

被引:76
作者
Kumar, A. Ganesh [1 ]
Swarnalatha, S. [1 ]
Gayathri, S. [1 ]
Nagesh, N. [2 ]
Sekaran, G. [1 ]
机构
[1] Cent Leather Res Inst, Dept Environm Technol, Madras 600020, Tamil Nadu, India
[2] Ctr Cellular & Mol Biol, Hyderabad 500007, Andhra Pradesh, India
关键词
Bacillus; biotechnology; degradation; metabolism; solid waste;
D O I
10.1111/j.1365-2672.2007.03564.x
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
Aims: The aim of the study was to optimize microbial degradation of keratinous waste and to characterize the alkaline active keratinase showing its biotechnological importance. Methods and results: An extracellular keratinase enzyme was purified from the culture medium of a bacterial isolate and the conditions were optimized. The molecular weight of DEAE-Sepharose-purified keratinase was determined by SDS-PAGE. Instrumental analyses were investigated to study the mechanism of bovine hair hydrolysis. Isolate was identified as Bacillus pumilus based on phenotypic characteristics and 16S rDNA sequence. The optimized condition for its growth was pH 8 and 35 degrees C. The molecular weight of the keratinase was estimated as 65 kDa. Activity inhibition by phenyl methyl sulphonyl fluoride confirmed keratinase as serine protease type. Instrumental analysis revealed the sulphitolysis and proteolysis involved mechanism in bovine hair hydrolysis. Conclusions: This study indicates that the isolated keratinase is an alkaline active serine protease with a high degree of activity towards bovine hair. Significance and Impact of the Study: This study examines a serine protease with high keratinolytic activity and degradation mechanism for bovine hair. The keratinolytic activity of the isolated strain and its reaction mechanism on bovine hair could show biotechnological potential in the leather industry.
引用
收藏
页码:411 / 419
页数:9
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