Enzymatic Synthesis of Polyphenol Glycosides by Amylosucrase

Abstract

The capability of synthesizing polyphenol glycosides was examined using recombinant amylosucrase from the hyperthermophilic bacterium Deinococcus geothermalis. Based on the action mode of amylosucrase, sucrose and twenty-one polyphenols were used as a donor and acceptors respectively. The transglycosylation reaction by amylosucrase produced one or two major polyphenol glycosides depending on the type of polyphenols used. The synthesized polyphenol glycosides were detected by thin-layer chromatography. The structures of the newly synthesized polyphenol glycosides were predicted based on the transglycosylation mechanism of the enzyme. According to the acceptability of the polyphenols, the structural characteristics of polyphenol as an efficient acceptor were evaluated. The results indicate that amylosucrase is an efficient catalyst for the enzymatic synthesis of polyphenol glycosides, which have high potentials in food, cosmetics, and pharmaceutical industries.

Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase

“…The transglycosylation reaction of NpAS was also carried out with catechin as well as (-)-epicatechin, as acceptor molecules (Overwin et al, 2015b). The acceptor substrate promiscuity of DgAS is explored by 21 polyphenols (Park et al, 2011). The DgAS preferentially transfers glucose to the glycoside of the polyphenol, and efficiently synthesizes glycosides for polyphenols that exist with one or more hydroxyl group, and in the z isomer form.…”

Enzymatic modification of daidzin using heterologously expressed amylosucrase in Bacillus subtilis

“…ASase has been applied to modify various bioactive compounds in their aglycone or glycone forms (Kim et al, 2016;Park et al, 2012), and among the ASases, DGAS and NPAS are the most popular enzymes to be used for this purpose (Cho et al, 2011;Jung et al, 2009;Park et al, 2011;Seo et al, 2009). Even though the enzymatic activities of DGAS and NPAS are very similar, their transglycosylation reaction products are somewhat different.…”

“…In addition, isoflavones showed various positive biological activities such as anti-cancer, anti-inflammatory, neuroprotective, and anti-carcinogenic activities, and protective activity against bone loss, cardiovascular diseases, and autoimmune diseases (Shimoda and Hamada, 2010b). However, they have several drawbacks including water-insolubility and low absorbability to be applied in food and pharmaceutical industries (Park et al, 2011;Shimoda et al, 2011). Therefore, the use of isoflavones as functional food ingredients and cosmetic constituents has been limited (Ko, 2014;Shimoda and Hamada, 2010b).…”

“…It has been reported that glycosyl conjugation was much more effective than cyclodextrin complexation to improve the watersolubility of hydrophobic compounds (Shimoda and Hamada, 2010a). Recently, glycosylation has been achieved using various enzymes from microbial sources rather using the high temperatures and pressures required for chemical glycosylation (Park et al, 2011). For example, puerarin transglycosylation reacted with maltogenic amylase from Geobacillus stearothermophilus resulted in the highly water-soluble puerarin derivatives a-D-glucosyl-(1 ?…”

Flavonoid glucosylation by non-Leloir glycosyltransferases: formation of multiple derivatives of 3,5,7,3′,4′-pentahydroxyflavane stereoisomers

“…Nonetheless, AS and GS catalytic domains and active sites, responsible for Glc transfer, show the same structural features and use the same mechanism, leading inevitably to α-glycosidic bonds. In spite of their high donor specificity, both enzyme classes appear more relaxed in their acceptor ranges (Daudé et al 2013;Demuth et al 2002;Fu and Robyt 1991;Park et al 2011Park et al , 2012Schneider et al 2011;Seibel et al 2006;Seo et al 2012;van Hijum et al 2006;Yoon et al 2004). One significant difference between the two enzyme classes is the specificity of formation of inter-sugar linkages.…”