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Characterization of an alkaline serine protease from an alkaline-resistantPseudomonassp.: Cloning and expression of the protease gene inEscherichia coli

✍ Scribed by Won Hee Jang; Eun Kyung Kim; Hwanghee Blaise Lee; Jae Hoon Chung; Ook Joon Yoo

Publisher: Springer Netherlands
Year: 1996
Tongue: English
Weight: 877 KB
Volume: 18
Category: Article
ISSN: 0141-5492
DOI: 10.1007/bf00137811

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✦ Synopsis

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,,tlK, value of this enzyme was 9.2 x lo3 S'mM', which is much higher than those of subtilisins.

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