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Researchers at Institute of Microbiology Report Findings in Microbiology and Biotechnology

May 28, 2014

By a News Reporter-Staff News Editor at Biotech Week -- Fresh data on Biotechnology are presented in a new report. According to news reporting originating from Beijing, People's Republic of China, by NewsRx correspondents, research stated, "A novel protease gene from Bacillus gibsonii, aprBG, was cloned, expressed in B. subtilis, and characterized. High-level expression of aprBG was achieved in the recombinant strain when a junction was present between the promoter and the target gene."

Our news editors obtained a quote from the research from the Institute of Microbiology, "The purified recombinant enzyme exhibited similar N-terminal sequences and catalytic properties to the native enzyme, including high affinity and hydrolytic efficiency toward various substrates and a superior performance when exposed to various metal ions, surfactants, oxidants, and commercial detergents. AprBG was remarkably stable in 50% organic solvents and retained 100% activity and stability in 0-4 M NaCl, which is better than the characteristics of previously reported proteases. AprBG was most closely related to the high-alkaline proteases of the subtilisin family with a 57-68% identity. The secretion and maturation mechanism of AprBG was dependent on the enzyme activity, as analyzed by site-directed mutagenesis."

According to the news editors, the research concluded: "Thus, when taken together, the results revealed that the halo-solvent-tolerant protease AprBG displays significant activity and stability under various extreme conditions, indicating its potential for use in many biotechnology applications."

For more information on this research see: Secretory expression, functional characterization, and molecular genetic analysis of novel halo-solvent-tolerant protease from Bacillus gibsonii. Journal of Microbiology and Biotechnology, 2014;24(2):197-208 (see also Biotechnology).

The news editors report that additional information may be obtained by contacting A. Deng, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China. Additional authors for this research include G. Zhang, N. Shi, J. Wu, F. Lu and T. Wen.

Keywords for this news article include: Asia, Biotechnology, Beijing, Genetics, Protease, Enzymes and Coenzymes, People's Republic of China.

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Source: Biotech Week

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