Characterization of a cold-active esterase from Serratia sp. and improvement of thermostability by directed evolution.

ABSTRACT:

Background

In recent years, cold-active esterases have received increased attention due to their attractive properties for some industrial applications such as high catalytic activity at low temperatures.

Results

An esterase-encoding gene (estS, 909 bp) from Serratia sp. was identified, cloned and expressed in Escherichia coli DE3 (BL21). The estS encoded a protein (EstS) of 302 amino acids with a predicted molecular weight of 32.5 kDa. It showed the highest activity at 10 °C and pH 8.5. EstS was cold active and retained ~92 % of its original activity at 0 °C. Thermal inactivation analysis showed that the T1/2 value of EstS was 50 min at 50 °C (residual activity 41.23 %) after 1 h incubation. EstS is also quite stable in high salt conditions and displayed better catalytic ac

SUBMITTER: Jiang H 

PROVIDER: S-EPMC4722774 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature