Characterization of an alkaline serine protease from an alkaline-resistant Pseudomonas sp.: Cloning and expression of the protease gene in Escherichia coli |
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Authors: | Won Hee Jang Eun Kyung Kim Hwanghee Blaise Lee Jae Hoon Chung Ook Joon Yoo |
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Institution: | (1) Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Kusong-Dong, 305-701 Yusong-Gu, Taejon, Korea;(2) Department of Biology, College of Natural Sciences, Chonnam National University, 300 Yongbong-dong, 500-757 Kwangju, Korea |
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Abstract: | Summary 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 × 103 S–1mM–1, which is much higher than those of subtilisins. |
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