Cloning and characterization of an oxiranedicarboxylate hydrolase from Labrys sp. WH-1.

ABSTRACT:

Objective

This study aimed to clone and characterize the oxiranedicarboxylate hydrolase (ORCH) from Labrys sp. WH-1.

Methods

Purification by column chromatography, characterization of enzymatic properties, gene cloning by protein terminal sequencing and polymerase chain reaction (PCR), and sequence analysis by secondary structure prediction and multiple sequence alignment were performed.

Results

The ORCH from Labrys sp. WH-1 was purified 26-fold with a yield of 12.7%. It is a monomer with an isoelectric point (pI) of 8.57 and molecular mass of 30.2 kDa. It was stable up to 55 °C with temperature at which the activity of the enzyme decreased by 50% in 15 min (T₅₀¹⁵) of 61 °C and the half-life at 50 °C (t_{1/2, 50 °C}) of 51 min and was als

SUBMITTER: Bao WN 

PROVIDER: S-EPMC6885406 | biostudies-literature | 2019 Dec.

REPOSITORIES: biostudies-literature