Cloning, Expression, and Identification of a Novel Extracellular Cold-Adapted Alkaline Protease Gene of the Marine Bacterium Strain YS-80-122 |
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Authors: | Fang Wang Jianhua Hao Chengye Yang and Mi Sun |
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Institution: | (1) Yellow Sea Fisheries Research Institute, Academy of Fishery Science of China, No. 106, Nan Jing Road, Qingdao, 266071, Shandong Province, People’s Republic of China; |
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Abstract: | As one of the most important groups of industrial enzymes, cold-adapted protease has been studied widely. An extracellular
cold-adapted alkaline protease metalloproteinase (MP), produced by a marine bacterium strain YS-80-122, has been purified.
The NH2-amino acid sequence of the purified alkaline protease MP was ANGTSSAFTQ, which was identical to that of the serralysin from
Pseudomonas sp. “TAC II 18”. The MP structural gene (lupA gene) was cloned by inverse PCR, and the open reading frame of 1,443 bp encoded a 463 amino acid protein (without signal
peptide). Sequence alignment reveals that the alkaline protease MP belongs to the serralysin-type metalloproteases. The recombinant
protein LupA was expressed in Escherichia coli, and Western blotting confirmed that the LupA was homologous to the cold-adapted alkaline protease MP. |
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