Journal article
Biochemical characterization of a novel feruloyl esterase from Penicillium piceum and its application in biomass bioconversion
Journal of molecular catalysis. B, Enzymatic, Vol.133, pp.S388-S394
11/2016
Handle:
https://hdl.handle.net/2376/118464
Abstract
[Display omitted]
•A novel feruloyl esterase was found through genome sequence of P. piceum.•The PpFAE had similar amino acid sequence to the type-C feruloyl esterase.•The substrate specificity profiling reveals PpFAE is a type-C feruloyl esterase.•The FAE had unique characteristics such as acidophilic and high temperature stability.•Supplementing low doses of PpFAE could enhance biomass conversion by 15.6–68.8%.
A putative feruloyl esterase (FAE) was successfully cloned from the genomic DNA of Penicillium piceum and expressed in E. coli. The deduced internal amino acid sequence of the novel FAE was found to have 56% sequence identity with FAE from Aspergillius flavus and was designated as PpFAE. PpFAE contained the conserved region flanking the characteristic G-X-S-X-G motif of a serine esterase, suggesting a FAE function for the protein. Substrate specificity profiling revealed that PpFAE was a type C FAE. The optimum temperature and pH for PpFAE were 70°C and 3.0, respectively. PpFAE was very stable under a pH range of 3.0–5.0 (>96% of maximum enzymatic activity) and displayed thermostability with thermal denaturing half-lives of 220min at 70°C and 150min at 60°C. Supplementation with low doses of PpFAE (120μg/g substrate) increased glucose yields released from corn stover, wheat bran, corn cob, and cassava stillage residues by 68.8%, 38.6%, 15.6%, and 20.0%, respectively. Supplementation with PpFAE could break down the intermolecular ester bonds that cross-link lignin with hemicellulose, effectively increasing the Xyl/Ara ratio and decreasing hydrogen bond intensity of the crude biomass.
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Details
- Title
- Biochemical characterization of a novel feruloyl esterase from Penicillium piceum and its application in biomass bioconversion
- Creators
- Le GaoMin WangShulin ChenDongyuan Zhang
- Publication Details
- Journal of molecular catalysis. B, Enzymatic, Vol.133, pp.S388-S394
- Publisher
- Elsevier B.V
- Identifiers
- 99900583062201842
- Language
- English
- Resource Type
- Journal article