Biochemical characterization of a novel feruloyl esterase from Burkholderia pyrrocinia B1213 and its application for hydrolyzing wheat bran.

ABSTRACT: In this study, a novel feruloyl esterase (BpFae) from Burkholderia pyrrocinia B1213 was purified, biochemically characterized, and applied in releasing ferulic acid from wheat bran. The molecular mass of BpFae was approximately 60 kDa by SDS-PAGE, and the enzyme was a homomultimer in solution. BpFae displayed maximum activity at pH 4.5-5.0 and was stable at pH 3.0-7.0. The optimal temperature for BpFae was 50 °C. BpFae activity was not affected by most metal ions tested and was significantly increased by Tween-20 and Triton-100. Purified BpFae exhibited a preference for methyl ferulate (41.78 U mg^-1) over methyl p-coumarate (38.51 U mg^-1) and methyl caffeate (35.36 U mg^-1) and had the lowest activity on methyl sinapate (1.79 U mg^-1)

SUBMITTER: Fu Z 

PROVIDER: S-EPMC8695398 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature