Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review

Abstract

β-glucosidases (BGLs) play a crucial role in the degradation of lignocellulosic biomass as well as in industrial applications such as pharmaceuticals, foods, and flavors. However, the application of BGLs has been largely hindered by issues such as low enzyme activity, product inhibition, low stability, etc. Many approaches have been developed to engineer BGLs to improve these enzymatic characteristics to facilitate industrial production. In this article, we review the recent advances in BGL engineering in the field, including the efforts from our laboratory. We summarize and discuss the BGL engineering studies according to the targeted functions as well as the specific strategies used for BGL engineering.

Characterization of a novel cold-adapted GH1 β-glucosidase from Psychrobacillus glaciei and its application in the hydrolysis of soybean isoflavone glycosides

“…This process has been investigated by directly using of β-glucosidases from leguminous plants and microorganisms ( Kaya et al, 2008 ; Cao et al, 2018 ; Li et al, 2018 ; Abdella et al, 2018 ). However, in the industrial production of isoflavones, the low solubility of isoflavones and the poor stability of β-glucosidase, product inhibition, limited enzymatic hydrolysis efficiency, and other scientific problems reduce the conversion efficiency of isoflavone aglycones ( Godse et al, 2021 ; Ouyang et al, 2023 ; Jin et al, 2023 ). Therefore, the hydrolysis rate of soybean isoflavones by recombinant β-glucosidase PgBgl1 was determined using soybean isoflavone glycosides as substrates.…”

Characterization of a Novel Hyperthermophilic GH1 β-Glucosidase from Acidilobus sp. and Its Application in the Hydrolysis of Soybean Isoflavone Glycosides

“…In addition, the enzymatic hydrolysis of β-glucosidase to prepare soybean isoflavone glycosides is an important application with high commercial value [ 42 ], which has been investigated through the direct use of β-glucosidases from leguminous plants and microorganisms [ 3 , 9 , 15 ]. However, in the industrial production of isoflavones, the low solubility of isoflavones, the poor stability of β-glucosidase, product inhibition, limited enzymatic hydrolysis efficiency, and other scientific problems reduce the conversion efficiency of isoflavone aglycones [ 1 , 18 , 43 ]. In view of these issues, the hydrolysis rate of soybean isoflavones by recombinant β-glucosidase BglAc was determined using soybean isoflavone glycosides (daidzin, glycitin, and genistin) as substrates.…”

“…The GH1 family is also grouped within GH-A, which contains 26 families and more than 120 family members ( 6 January 2024). Prior to this study, the crystal structures of more than four glucosidases were resolved, and it was demonstrated that the 3D structure of glycosidase GH1 is composed of a (β/α) 8 barrel [ 1 , 18 ]. The β-glucosidase investigated in this study is derived from the archaea Acidilobus sp., which belongs to the first glycosidase family (GH1).…”

Hotspot Wizard‐informed engineering of a hyperthermophilic β‐glucosidase for enhanced enzyme activity at low temperatures

“…Thus, supplementation of β-glucosidase from a different source is usually required for these cellulase cocktails (Erkanli et al, 2024). Consequently, considerable efforts have been put into the development of engineered β-glucosidases more suitable for various industrial applications (Ouyang et al, 2023).…”