Feruloyl Esterase: A Key Enzyme in Biomass Degradation

Western Regional Research Center, USDA-ARS, 800 Buchanan Street, Albany, CA 94710, USA.
Applied Biochemistry and Biotechnology (Impact Factor: 1.74). 06/2006; 133(2):87-112. DOI: 10.1385/ABAB:133:2:87
Source: PubMed


Feruloyl esterase forms a part of the enzyme complex that acts collectively and synergistically to completely hydrolyze xylan to its monomers. The enzyme has found potential uses in a wide variety of applications of interest to the agrifood and pharmaceutical industries. This review describes the enzymology of feruloyl esterases involved in xylan degradation. The occurrence of feruloyl esterases in various microorganisms and their physiochemical properties are presented. The nature of the enzyme substrates and products, the role of synergistic interactions with xylanases and other accessory enzymes, as well as the sequence-structure relating to the reaction mechanism are emphasized.

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    • "Gottschalk et al. (2010) reported a synergic action between cellulase, xylanase, b-glucosidase and feruloyl esterase from Trichoderma reesei and Aspergillus awamori in the hydrolysis of sugarcane bagasse. The capacity of feruloyl esterase to hydrolyse ester bonds between carbohydrates residues and phenolic compounds is thought to enhance the access of hydrolases to the polysaccharides (Dyk and Pletschke, 2012; Faulds et al., 2006; Wong, 2006). This synergy reduces the amount of enzyme necessary to achieve saccharification and the bioethanol production costs from lignocellulose biomass (Tabka et al., 2006). "
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    • "(b) Cross-linked pectin. Redrawn based on Wong (2006) with kind permission from Springer Science and Business Media. "
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    ABSTRACT: The biological conversion of plant lignocellulose plays an essential role not only in carbon cycling in terrestrial ecosystems but also is an important part of the production of second generation biofuels and biochemicals. The presence of the recalcitrant aromatic polymer lignin is one of the major obstacles in the biofuel/biochemical production process and therefore microbial degradation of lignin is receiving a great deal of attention. Fungi are the main degraders of plant biomass, and in particular the basidiomycete white rot fungi are of major importance in converting plant aromatics due to their ability to degrade lignin. However, the aromatic monomers that are released from lignin and other aromatic compounds of plant biomass are toxic for most fungi already at low levels, and therefore conversion of these compounds to less toxic metabolites is essential for fungi. Although the release of aromatic compounds from plant biomass by fungi has been studied extensively, relatively little attention has been given to the metabolic pathways that convert the resulting aromatic monomers. In this review we provide an overview of the aromatic components of plant biomass, and their release and conversion by fungi. Finally, we will summarize the applications of fungal systems related to plant aromatics.
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    • "e l s e v i e r . c o m / l o c a t e / b i o r t e c h polysaccharides and lignin structures (Wong, 2006). This enzyme could therefore help to improve the accessibility of glycoside hydrolase enzymes during biomass conversion (Faulds, 2010). "
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    ABSTRACT: Accessory enzymes that assist biomass degradation could be used to improve the recovery of fermentable sugar for use in biorefineries. In this study, different fungal strains isolated from the Amazon rainforest were evaluated in terms of their ability to produce feruloyl esterase (FAE) and xylanase enzymes, and an assessment was made of the contributions of the enzymes in the hydrolysis of pretreated sugarcane bagasse. In the selection step, screening using plate assays was followed by shake flask submerged cultivations. After carbon source selection and cultivation in a stirred-tank bioreactor, Aspergillusoryzae P21C3 proved to be a promising strain for production of the enzymes. Supplementation of a commercial enzyme preparation with 30% (v/v) crude enzymatic complex from A. oryzae P21C3 increased the conversion of cellulose derived from pretreated sugarcane bagasse by 36%. Supplementation with FAE and xylanase enzymes produced on-site can therefore be used to improve the hydrolysis of sugarcane bagasse.
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