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KMID : 0545120070170050761
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Journal of Microbiology and Biotechnology
2007 Volume.17 No. 5 p.761 ~ p.768
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Biochemical and Genetic Characterization of an Extracellular Metalloprotease Produced from Serratia proteamaculans
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KWAK JANGYUL
Lee Ki-Eun
Shin Dong-Ha
Maeng Jin-Soo
Park Doo-Sang
Oh Hyun-Woo
Son Kwang-Hee
Bae Kyung-Sook
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Abstract
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Serratia proteamaculans isolated from the digestive tract of a spider produces an extracellular protease with an estimated molecular mass of 51 kDa. The purified enzyme was characterized as having high activities at wide pH and temperature ranges. We further characterized biochemical features of the enzymatic reactions under various reaction conditions. The protease efficiently hydrolyzed a broad range of protein substrates including albumin, keratin, and collagen. The dependence of enzymatic activities on the presence of metal ions such as calcium and zinc indicated that the enzyme is a metalloprotease, together with the previous observation that the proteolytic activity of the enzyme was not inhibited by aspartate, cysteine, or serine protease inhibitors, but strongly inhibited by 1,10-phenanthroline and EDTA. The proA gene encoding the exoprotease was isolated as a 5.6 kb BamHI fragment after PCR amplification using degenerate primers and subsequent Southern hybridization. The nucleotide sequence revealed that the deduced amino acid sequences shared extensive similarity with those of the serralysin family of metalloproteases from other enteric bacteria. A gene (inh) encoding a putative protease inhibitor was also identified immediately adjacent to the proA structural gene.
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KEYWORD
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Arazyme, metalloprotease, Serratia proteamaculans, HY-3, serralysin, enzymatic kinetics
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