Cyclomaltodextrin glucanotransferase-catalyzed transglycosylation from dextrin to alkanol maltosides.
نویسندگان
چکیده
Maltosides of butanol, octanol, and lauryl alcohol were found for the first time to serve as substrates for cyclomaltodextrin glucanotransferase (CGTase), and glycosyl residue was transfered from dextrin to the substrate affording novel maltosides with 3-4 glucose units.
منابع مشابه
Transglycosylation of glycosyl residues to cyclic tetrasaccharide by Bacillus stearothermophilus cyclomaltodextrin glucanotransferase using cyclomaltodextrin as the glycosyl donor.
Cyclomaltodextrin glucanotransferase (EC 2.4.1.19, abbreviated as CGTase) derived from Bacillus stearothermophilus produced a series of transfer products from a mixture of cyclomaltohexaose and cyclic tetrasaccharide (cyclo[-->6)-alpha-D-Glcp-(1-->3)-alpha-D-Glcp-(1-->6)-alpha-D-Glcp-(1-->3)-alpha-D-Glcp-(1-->], CTS). Of the transfer products, only two components, saccharides A and D, remained ...
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The production of hesperetin glycosides was investigated using glycosylation with Xanthomonas campestris and cyclodextrin glucanotransferase (CGTase). X. campestris glucosylated hesperetin to its 3'-, 5-, and 7-O-glucosides, and CGTase converted hesperetin glucosides into the corresponding maltosides. The resulting 7-O-glucoside and 7-O-maltoside of hesperetin showed inhibitory effects on IgE a...
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Cyclodextrins are non-reducing cyclic glucose oligosaccharides resulting from the cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19; CGTase) catalyzed degradation of starch. Their structures have been reviewed. There are three common cyclodextrins with 6, 7 or 8 D-glucopyranonsyl residues (α-, β-, and γ-cyclodextrin respectively) linked by α-1,4 glycosidic bonds. The glucose residues have the...
متن کاملStructures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.
The enzymes from the alpha-amylase family all share a similar alpha-retaining catalytic mechanism but can have different reaction and product specificities. One family member, cyclodextrin glycosyltransferase (CGTase), has an uncommonly high transglycosylation activity and is able to form cyclodextrins. We have determined the 2.0 and 2.5 A X-ray structures of E257A/D229A CGTase in complex with ...
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عنوان ژورنال:
- Bioscience, biotechnology, and biochemistry
دوره 72 11 شماره
صفحات -
تاریخ انتشار 2008