High production of genistein diglucoside derivative using cyclodextrin glycosyltransferase from Paenibacillus macerans

Abstract

Genistein has been regarded as one important soy isoflavone with multiple health benefits, whereas its applications are limited by the low hydrophilicity. To improve the water solubility, codon optimized cyclodextrin glycosyltransferase from Paenibacillus macerans was employed for genistein transglycosylation in this study. At least four transglycosylation products were produced and identified by HPLC and LC-MS: genistein monoglucoside, diglucoside, triglucoside, and tetraglucoside derivatives. Obviously, the yields of genistein monoglucoside and genistein diglucoside exhibited great superiority compared with other two products. To maximize the yield of genistein diglucoside, various reaction conditions such as genistein dissolvents, glycosyl donors, substrates concentrations and ratios, enzyme concentrations, reaction pH, temperature, and time were optimized. Finally, the yield of genistein diglucoside was enhanced by 1.5-fold under the optimum reaction system. Our study demonstrates that the production of genistein diglucoside could be specifically enhanced, which is one important genistein derivative with better water solubility and stability.

Enzymatic Synthesis of a Novel Pterostilbene α-Glucoside by the Combination of Cyclodextrin Glucanotransferase and Amyloglucosidase

“…It is worth emphasizing that the α-linkage between glucose and pterostilbene is resistant to the action of amyloglucosidase. This resistance was also reported in the case of ascorbic acid [ 43 ] and hydroquinone [ 29 ], but not with genistein α-glucoside [ 31 ].…”

“…(Toruzyme 3.0L) worked better than that from Bacillus macerans (CGTase Amano). The transglycosylation activity of CGTase is well reported, as it is able to glucosylate other phenolic compounds such as resveratrol [ 26 , 27 ], catechin [ 28 ], hydroquinone [ 29 ], kaempferol [ 30 ] or genistein [ 31 ].…”

“…Although the CGTase displays a low hydrolytic activity on such linkages [ 41 ], we incorporated a glycosidase to accelerate the hydrolytic process and thus increase the yield of monoglucoside. A similar strategy was successfully employed for the glucosylation of inositol [ 42 ], genistein [ 31 ], ascorbic acid [ 43 ] or hydroquinone [ 29 ]. In the case of pterostilbene, after 10 h reaction with CGTase, we incubated the mixture with a recombinant glucoamylase from S. cerevisiae (var.…”

Production and Surfactant Properties of Tert-Butyl α-d-Glucopyranosides Catalyzed by Cyclodextrin Glucanotransferase

“…For compound 2, the major signal of the MS spectrum in positive mode was at m/z 421.17 that fits with the M+[Na] + ion of the tert-butyl maltoside. The identity of the products was clearly established by 13 C and 1 H NMR analysis. NMR data confirmed the α-configuration of the glucosyl moieties.…”

“…The enzyme CGTase has proved an exceptional capability to glucosylate compounds of different nature employing starch, maltodextrins, or cyclodextrins as glucosyl donors [9,10]. Apart from monosaccharides and disaccharides [11,12], other compounds such as flavonoids [13,14], vitamins [15], sugar alcohols [16], sweet glycosides [17], and polyols [18] have been successfully used as acceptor molecules for the intermolecular transglycosylation. Unfortunately, one of the main drawbacks of CGTases is that their product selectivity is not very high, because the enzyme displays its four activities simultaneously [19].…”