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Cold adaptation of a mesophilic serine protease, subtilisin, by in vitro random mutagenesis.

Abstract：

:Artificial cold adaptation of a mesophilic protease, subtilisin BPN' was attempted by means of random mutagenesis of its entire gene coupled with screening of cleared-zone-forming colonies on skim-milk plates at a low temperature. Out of sixty clones screened at 10 degrees C, one mutant enzyme (termed M-15) was found to acquire higher proteolytic activities, specifically dependent on low temperatures ranging from 10 degrees C to 1 degree C, in comparison with those of the wild-type. DNA sequencing analysis revealed that, by this mutation, the 84th amino acid residue, valine, was substituted by isoleucine, which is located 1.5 nm from the center of the catalytic triad in the tertiary structure of subtilisin. By kinetic analysis of the purified enzyme samples, the higher proteolytic activities of M-15 at low temperatures were found to be due to the decrease in the Km value. There was no difference in thermostability between the wild-type and mutant enzymes, when tested by heat treatment. Circular dichroism spectra also showed no difference between them at 10 degrees C, indicating that the mutation of V841 had no effect on the secondary structure of subtilisin.

journal_name

Appl Microbiol Biotechnol

journal_title

Applied microbiology and biotechnology

authors

Kano H,Taguchi S,Momose H

doi

10.1007/s002530050886

subject

Has Abstract

pub_date

1997-01-01 00:00:00

pages

46-51

issue

1

eissn

0175-7598

issn

1432-0614

journal_volume

47

pub_type

杂志文章

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