Enzymatic Syntheses of Two Stable (–)-Epigallocatechin Gallate-glucosides by Sucrose Phosphorylase

Sucrose phosphorylase as cross‐linked enzyme aggregate: Improved thermal stability for industrial applications

“…The enzyme has long been used for the production of G1P, an efficient donor for chemical and enzymatic glycosylation reactions [15]. Furthermore, SPase can also transfer a glucosyl group to different carbohydrate and non-carbohydrate acceptors thanks to its broad substrate specificity [16,17]. Goedl et al, for example, have developed an exceptionally efficient and selective process for the production of glyceryl α-D-glucoside, a moisturizing agent for cosmetics that is marketed under the tradename Glycoin® [18,19].…”

Transglucosylation of ascorbic acid to ascorbic acid 2-glucoside by a recombinant sucrose phosphorylase from Bifidobacterium longum

“…As for glycosyl acceptors, broad substrate specificity towards phenolic and alcoholic OH group compounds has been reported (Kitao and Sekine 1994). The broad acceptor specificity of SPase from Leuconostoc mesenteroides has been applied to xylitol (Kitao and Sekine 1992), to catechins (Kitao et al 1993(Kitao et al , 1995, to hydroquinone (Kitao and Sekine 1994), and to hydroxyfuranones (Kitao et al 2000) for the stability increment of each compound by glucosylation, but glucosylation of AA was not successful (Kitao and Sekine 1992). In spite of the broad acceptor specificity of the enzyme, the difference in enzyme specificity between bacterial species was recognized by Vandamme et al (1987).…”

Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization

“…of glycosylated compounds (Kitao et al, 1995). At the industrial scale, such carbohydrate conversions are preferably run at 60 • C or higher, mainly to avoid microbial contamination (Bruins et al, 2001;Eijsink et al, 2005;Vieille and Zeikus, 1996).…”