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		题名	作者	年代	出处	被引量
	1	Purification and characterization of CHpro1, a thermotolerant, alkali-stable and oxidation-resisting protease of Chumathang hotspring显示文摘Metagenomic approaches are recently used for searching novel open reading frames(ORFs) coding enzymes employed in pharmaceutical, food industries, etc.In this study, a metagenomic library was constructed from Chumathang hotspring sediment DNA. The library consisted of approximately 9,000 clones and was screened for protease activity. A clone exhibiting protease activity was identified and named CHpro1. Sequencing of CHpro1 revealed that the ORF encoded a functional protein of 363 amino acids belonging to peptidase S8–S53 superfamily.CHpro1 shared 41 % sequence similarity with a reported protease(subtilase family) and 35 % structural similarity with the crystal structure of Pro-Tk sps. of Thermococcus kodarkaenasis. In silico modeling the 3D structure of CHpro1 showed that it has two beta sheets, 10 alpha helices and 11 strands. Catalytic triad prediction implied CHpro1 to be a serine protease. The optimum temperature and p H of the purified protease were found to be 80 °C and 11.0,respectively. The enzyme was active at 5 % concentration of hydrogen peroxide and retained 60 % of activity at 10 %concentration. The thermotolerant, alkalophilic and oxidantstable properties of the protease make it a potential candidate for biotechnological applications.	Reena Singh Chirag Chopra Vishnu Kumar Gupta Bashir Akhlaq Vijeshwar Verma Shafaq Rasool	2015	Science Bulletin2015，60，14：	0

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