Characterization of an alkaline serine protease from an alkaline-resistant Pseudomonas sp: Cloning and expression of the protease gene in Escherichia coli

被引：13
|
作者：
Jang, WH
Kim, EK
Lee, HB
Chung, JH
Yoo, OJ
机构：
[1] KOREA ADV INST SCI & TECHNOL,DEPT BIOL SCI,YUSONG GU,TAEJON 305701,SOUTH KOREA
[2] CHONNAM NATL UNIV,COLL NAT SCI,DEPT BIOL,KWANGJU 500757,SOUTH KOREA
来源：
BIOTECHNOLOGY LETTERS | 1996年 / 18卷 / 01期
关键词：
D O I：
10.1007/BF00137811
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
A gene, aprP, encoding an extracellular alkaline serine protease from a newly isolated Pseudomonas sp. KFCC 10818 was cloned and characterized. Nucleotide sequence analysis revealed an open reading frame of 1,266 nucleotides which could encode a polypeptide comprised of 422 amino acids. The C-terminal 283 residues showed an overall sequence homology with the subtilisin-type serine proteases. When expressed in E. coli, the alkaline protease, AprP, was released to the culture medium. The purified AprP was most active at pH 11. The k(cat)/K-m value of this enzyme was 9.2 x 10(3)S(-1)mM(-1), which is much higher than those of subtilisins.
引用
收藏
页码：57 / 62
页数：6
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