Enzymatic glucosylation of polyphenols using glucansucrases and branching sucrases of glycoside hydrolase family 70

Abstract

Polyphenols exhibit various beneficial biological activities and represent very promising candidates as active compounds for food industry. However, the low solubility, poor stability and low bioavailability of polyphenols have severely limited their industrial applications. enzymatic glycosylation is an effective way to improve the physicochemical properties of polyphenols. As efficient transglucosidases, glycoside hydrolase family 70 (GH70) glucansucrases naturally catalyze the synthesis of polysaccharides and oligosaccharides from sucrose. Notably, GH70 glucansucrases show broad acceptor substrate promiscuity and catalyze the glucosylation of a wide range of non-carbohydrate hydroxyl group-containing molecules, including benzenediol, phenolic acids, flavonoids and steviol glycosides. Branching sucrase enzymes, a newly established subfamily of GH70, are shown to possess a broader acceptor substrate binding pocket that acts efficiently for glucosylation of larger size polyphenols such as flavonoids. Here we present a comprehensive review of glucosylation of polyphenols using GH70 glucansucrase and branching sucrases. Their catalytic efficiency, the regioselectivity of glucosylation and the structure of generated products are described for these reactions. Moreover, enzyme engineering is effective for improving their catalytic efficiency and product specificity. The combined information provides novel insights on the glucosylation of polyphenols by GH70 glucansucrases and branching sucrases, and may promote their applications.

Resveratrol glucosylation by GTF-SI from Streptococcus mutans: computational insights into a GH70 family enzyme

“…While factors such as substrate and enzyme concentrations, optimal temperature, and reaction time can affect catalysis, theoretical activation barriers often serve as reliable indicators of reaction feasibility. 13,50,51…”

How many α-amylase GH families are there in the CAZy database?

“…At the higher hierarchical level, CAZy has implemented clans comprising more than one GH family and GH13 belongs to the clan GH-H together with families GH70 and GH77 [32][33][34][35]. Both of the latter families contain enzymes (Table 1) which possess fair hydrolytic side activities toward starch [36][37][38][39][40][41][42][43][44][45]. At a lower hierarchical level, GH13 has been divided into subfamilies [46].…”

Reaction intensification for biocatalytic production of polyphenolic natural product di‐C‐β‐glucosides

“…They are generally considered important in a healthy human diet and contribute to the efficacy of traditional medicines (Luo et al, 2021; Mithul Aravind et al, 2021; Shakoor et al, 2021; C. Sun, Zhao, et al, 2020). Polyphenol biosynthesis often involves the late‐stage attachment of one or more sugar residues to the aglycone core structure (Li et al, 2021; Thuan & Sohng, 2013). A distinct natural motif of polyphenol glycosylation is that of the di‐ C ‐glycoside.…”

“…Sun, Zhao, et al, 2020). Polyphenol biosynthesis often involves the late-stage attachment of one or more sugar residues to the aglycone core structure (Li et al, 2021;Thuan & Sohng, 2013). A distinct natural motif of polyphenol glycosylation is that of the di-C-glycoside.…”