Inactivation and process intensification of β-glucosidase in biomass utilization.

Mu, Yinghui; Meng, Fanjin; Ju, Xin; Li, Liangzhi

Lignocellulosic biomass has emerged as a promising environmental resource. Enzyme catalysis, as one of the most environmentally friendly and efficient tools among various treatments, is used for the conversion of biomass into chemicals and fuels. Cellulase is a complex enzyme composed of β-glucosidase (BGL), endo-β-1,4-glucanase (EG), and exo-β-1,4-glucanase (CBH), which synergistically hydrolyzes cellulose into monosaccharides. BGL, which further deconstructs cellobiose and short-chain cellooligosaccharides obtained by EG and CBH catalysis into glucose, is the most sensitive component of the synergistic enzyme system constituted by the three enzymes and is highly susceptible to inactivation by external conditions, becoming the rate-limiting component in biomass conversion. This paper firstly introduces the source and catalytic mechanism of BGL used in the process of biomass resource utilization. The focus is on the review of various factors affecting BGL activity during hydrolysis, including competitive adsorption of lignin, gas–liquid interface inactivation, thermal inactivation, and solvent effect. And the methods to improve BGL inactivation are proposed from two aspects—substrate initiation and enzyme initiation. In particular, the screening, modification, and alteration of the enzyme molecules themselves are discussed with emphasis. This review can provide novel ideas for studies of BGL inactivation mechanism, containment of inactivation, and activity enhancement. Key points: • Factors affecting β-glucosidase inactivation are described. • Process intensification is presented in terms of substrate and enzyme. • Solvent selection, protein engineering, and immobilization remain topics of interest.

LIGNIN structure; MULTIENZYME complexes; BIOMASS; BIOMASS chemicals; GAS-liquid interfaces; BIOMASS conversion; GLUCOSIDASES

Applied Microbiology & Biotechnology, 2023, Vol 107, Issue 10, p3191

0175-7598

Academic Journal

10.1007/s00253-023-12483-7