Purification and biochemical characterization of an alkaline feruloyl esterase from Penicillium sumatrense NCH-S2 using rice bran as substrate
Feruloyl esterases (FAEs) are essential accessory enzymes in the hydrolysis of plant cell wall structure. A novel FAE was obtained from Penicillium sumatrense NCH-S2. Enzyme purification was conducted by ultrafiltration, ammonium sulfate precipitation, anion exchange, and gel filtration chromatograp...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2021-01-01
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| Series: | CyTA - Journal of Food |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/19476337.2020.1844300 |
| Summary: | Feruloyl esterases (FAEs) are essential accessory enzymes in the hydrolysis of plant cell wall structure. A novel FAE was obtained from Penicillium sumatrense NCH-S2. Enzyme purification was conducted by ultrafiltration, ammonium sulfate precipitation, anion exchange, and gel filtration chromatography. This FAE has a molecular mass of 36 kDa. Its optimum temperature and pH were 50°C and pH 9.0–10.0, respectively. The FAE demonstrated high pH stability at the pH ranging from 6.0 to 10.0. After enzymatic hydrolysis with FAE, the DPPH free radical scavenging capacity, ferrous ion chelating ability, and total phenolic content (TPC) of defatted rice bran (DRB) hydrolysate significantly increased. Furthermore, the amount of released FA from DRB under a synergistic interaction of FAE and hemicellulose increased by 18–21% in comparison with that of either enzyme acting alone. |
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| ISSN: | 1947-6337 1947-6345 |