Hydroxycinnamic acids release during bioconversion of corn stover and their effects on lignocellulolytic enzymes. (December 2019)

• Record Type: Journal Article
• Authors: Liu, Tongjun; Yang, Li; Liu, Bin; Tan, Liping
• Is Part Of: Bioresource technology. Volume 294(2019)
• Publication Date: 2019-12
• Subjects: P-coumaric acid -- Ferulic acid -- Alkaline hydrogen peroxide pretreatment -- Enzymatic hydrolysis -- Molecular docking; Biomass -- Periodicals; Biomass energy -- Periodicals; Bioremediation -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Bioénergie -- Périodiques; Déchets agricoles -- Périodiques; Déchets industriels -- Périodiques; Déchets organiques -- Périodiques; Déchets (Combustible) -- Périodiques; 662.88
• DOI: 10.1016/j.biortech.2019.122116
• Languages: English
• ISSNs: 0960-8524

Abstract

Highlights: FA and p -CA were released during alkaline hydrogen peroxide pretreatment. p -CA and FA can be called the "inhibitors of enzyme activity". p- CA and FA interact with EGI by non-covalent bindings according to molecular docking study . Abstract: Hydroxycinnamic acids released during alkaline pretreatment of lignocellulose, especially p- coumaric acid ( p -CA) and ferulic acid (FA), negatively affect the enzymatic hydrolysis and fermentation. However, the mechanism of this effect is not well understood. In this study, we investigated the releasing behavior and negative effect and examined the underlying mechanisms. The results demonstrated that the hydrogen peroxide concentration and biomass loading affected the release of p -CA and FA significantly during alkaline hydrogen peroxide (AHP) pretreatment of corn stover. p -CA and FA mainly inhibited the activity of endoglucanase, xylanase, and filter paper activity (FPA), while the amount of lignocellulolytic enzyme protein was not affected. Thus, they acted as inhibitors of enzyme activities. Molecular docking study indicated that p -CA and FA inhibited the lignocellulolytic enzyme activity and enzymatic hydrolysis efficiency mainly by forming non-covalent bonds to specific amino acids in the active sites of the lignocellulolytic enzymes.