| Autor: |
Ding JW; Wilmar Innovation Centre, Wilmar International Limited, 28 Biopolis Road, Singapore 138568, Singapore.; Department of Chemical and Biomolecular Engineering, National University of Singapore, 4 Engineering Drive 4, Singapore 117585, Singapore., Kua GKB; Wilmar Innovation Centre, Wilmar International Limited, 28 Biopolis Road, Singapore 138568, Singapore., Lim SC; Wilmar Innovation Centre, Wilmar International Limited, 28 Biopolis Road, Singapore 138568, Singapore., Ng KH; Wilmar Innovation Centre, Wilmar International Limited, 28 Biopolis Road, Singapore 138568, Singapore., Yang KL; Department of Chemical and Biomolecular Engineering, National University of Singapore, 4 Engineering Drive 4, Singapore 117585, Singapore. |
| Abstrakt: |
Ferulic acid (FA) exhibits antioxidant and anti-inflammatory properties, making it valuable for numerous industrial applications. Traditionally, FA is produced by the alkaline hydrolysis of γ -oryzanol, which is typically associated with wastewater generation. Recently, an increasing demand of natural FA necessitates its green production via enzymatic hydrolysis of γ -oryzanol, a mixture comprising triterpene alcohol ferulates and phytosteryl ferulates. Thus far, γ -oryzanol can be hydrolyzed by only four commercial cholesterol esterases with low yields. Herein, we report a recombinant cholesterol esterase from Mustela putorius furo (MPFCE) for the enzymatic hydrolysis of γ -oryzanol. The enzyme yielded 25.5% FA, which is the highest reported through enzymatic means thus far. The hydrolysis profile revealed that the enhanced yield primarily resulted from the near-complete hydrolysis of phytosteryl ferulates, together with slight hydrolysis of triterpene alcohol ferulates. MPFCE serves as a potential candidate for the enzymatic production of FA through targeted hydrolysis of γ -oryzanol. |
