期刊名称：International Journal of Innovative Research in Science, Engineering and Technology
印刷版ISSN：2347-6710
电子版ISSN：2319-8753
出版年度：2014
卷号：3
期号：6
页码：13216
出版社：S&S Publications
摘要：The present study was designed to explore potential of thermostable protease in leather processing and furtherhost optimization studies to produce enzymes to fulfill commercial demand. Thermostable protease gene from Geobacillusstearothermophilus was cloned in pET28a vector and expressed in E. coli BL21 (DE3). The new generation expression hostsystems were used in the current study to enhance expression fold and we have used E. coli C41 (DE3) and E. coli Rosettaand achieved more than three time expression of conventional host system. An average molecular weight 60 kDathermostable protease was produced by recombinant DNA technology and the enzyme has shown tremendous scope inleather processing especially dehairing. The expressed thermostable protease was stable and active in different range oftemperature (20-900C) and pH (5-13). The protease inhibitors have shown minimal inhibition on protease activity andstability. The expressed thermostable protease was reported significant kinetics parameters Km (0.9mM) and Vamx (0.084mM/Sec) and maximum enzymatic activity was reported 0.18U/ml (E. coli rosetta) and 0.17 U/ml (E. coli C41) at pH 8 and650C. The expressed protease was analyzed for proteolytic activity, dehairing activity and shown tremendous scope forleather processing.
