Engineering Bacillus pumilus alkaline serine protease to increase its low-temperature proteolytic activity by directed evolution.

ABSTRACT:

Background

Mesophilic alkaline serine proteases from various bacteria have been commercially applied in a range of industries owing to their high catalytic efficiency and wide substrate specificity. However, these proteases have an optimal catalytic temperature of approximately 50 °C, and their activity decreases significantly at low temperature. Therefore, to enhance their cold activity, it is necessary to improve the catalytic performance of these proteases at low temperature. The alkaline serine protease (DHAP) from Bacillus pumilus BA06 is a typical mesophilic enzyme, which has demonstrated great potential in various industrial applications. Here we attempted to improve the cold activity of DHAP via directed evolution.

Results

Seven variants (P9S, A1G/K27Q, A38V, A116T,

SUBMITTER: Zhao HY 

PROVIDER: S-EPMC5984802 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature