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

Unlabelled: In this study, a novel feruloyl esterase (BpFae) from 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) over methyl -coumarate (38.51 U mg) and methyl caffeate (35.36 U mg) and had the lowest activity on methyl sinapate (1.79 U mg). Under the optimum conditions, the and for methyl ferulate were 0.53 mM and 86.74 U mg, respectively. Residues Ser209, His492, and Glu245 in the catalytic pocket of BpFae could form hydrogen bonds with the substrate and were crucial for catalytic activity and substrate specificity. When G11 xylanase XynA and BpFae were used separately for hydrolyzing de-starched wheat bran (DSWB), the ferulic acid released was undetectable and 1.78%, respectively, whereas it was increased to 59.26% using the mixture of the two enzymes. Thus, BpFae is considered an attractive candidate for the production of ferulic acid from agricultural by-products.

Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-021-03066-2.