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N-terminal deletion of Tk1689, a subtilisin-like serine protease from Thermococcus kodakaraensis, copes with its cytotoxicity in Escherichia coli

Paper ID Volume ID Publish Year Pages File Format Full-Text
21390 43220 2010 5 PDF Available
Title
N-terminal deletion of Tk1689, a subtilisin-like serine protease from Thermococcus kodakaraensis, copes with its cytotoxicity in Escherichia coli
Abstract

Tk1689, a subtilisin-like serine protease from Thermococcus kodakaraensis, was found to be toxic to the host cells when produced in the pro-protein form (Pro-Tk1689) in Eschericia coli. Cytotoxic effect of Pro-Tk1689 was reduced when signal and pro-peptide both were removed and the protein was produced in the mature form (MP-Tk1689). The mature protein was produced in E. coli in the soluble form. Recombinant MP-Tk1689 was catalytically active and exhibited optimum activity at 55 °C and pH 7. Specific activity of the enzyme was 700 U/mg. The enzyme displayed a half life of 80 min at 60 °C.

Keywords
Subtilisin-like serine protease; Thermococcus kodakaraensis; Cytotoxicity; N-terminal deletion
First Page Preview
N-terminal deletion of Tk1689, a subtilisin-like serine protease from Thermococcus kodakaraensis, copes with its cytotoxicity in Escherichia coli
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 110, Issue 4, October 2010, Pages 381–385
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering