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European journal of molecular biology and biochemistry

Volume 11, Issue 1, 2024
Mcmed International
European journal of molecular biology and biochemistry
Issn
2348 - 2192 (Print), 2348 - 2206 (Online)
Frequency
bi-annual
Email
editorejmbb@mcmed.us
Journal Home page
http://mcmed.us/journal/ejmbb
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Abstract
Title
THERMOSTABLE PROTEASE FOR COMMERCIAL DEMAND: MOLECULAR CLONING AND HOST OPTIMIZATION
Author
Gandharv Singh Rawat*, Satish Mohabe
Email
gandharvsinghrwt@gmail.com
keyword
Expression Host, Leather Dehairing, Leather Processing, Thermostable Protease
Abstract
The present study was designed to explore potential of thermostable protease in leather processing and further host optimization studies to produce enzymes to fulfill commercial demand. Thermostable protease gene from Geobacillus stearothermophilus was cloned in pET28a vector and expressed in E. coli BL21 (DE3). The new generation expression host systems were used in the current study to enhance expression fold and used E. coli C41 (DE3) and E. coli rosetta used and achieved more than three time expression of conventional host system. An average molecular weight 60 kDa thermostable protease was produced by recombinant DNA technology and the enzyme has shown tremendous scope in leather processing especially dehairing. The expressed thermostable protease was stable and active in different range of temperature (20-900C) and pH (5-13). The protease inhibitors have shown minimal inhibition on protease activity and stability. The expressed thermostable protease was reported significant kinetics parameters Km (0.9mM) and Vamx (0.084 mM/Sec) and maximum enzymatic activity was reported 0.18U/ml (E. coli rosetta) and 0.17 U/ml (E. coli C41) at pH 8 and 650C. The expressed protease was analyzed for proteolytic activity, dehairing activity and shown tremendous scope for leather processing
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