کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
71226 48888 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
β-1,4-Galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by α-lactalbumin, immobilization and solvent tolerance
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
پیش نمایش صفحه اول مقاله
β-1,4-Galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by α-lactalbumin, immobilization and solvent tolerance
چکیده انگلیسی

The influence of different parameters on the activity of the β-1,4-galactosyltransferase (β-1,4-GalT) from bovine milk has been investigated using various acceptor and donor substrates. It was found that the “specifier” protein α-lactalbumin (α-LA), which interacts with β-1,4-GalT forming the lactose synthase (LS) complex, is not necessary when the acceptors are different glucopyranosides, and, in some cases, it can even have an inhibitory effect, like with the complex glucosides ginsenoside Rg1 (1) and colchicoside (2). By optimization of the reaction conditions, the galactosylated and glucosylated derivatives of 2 were prepared, using UDP-Gal and UDP-Glc as sugar donors, respectively, and characterized. Moreover, β-1,4-GalT was covalently immobilized on Eupergit C 250 L in the absence of α-LA, and the synthetic performances of this immobilized biocatalyst were evaluated. Finally, the best organic cosolvents to be used both with β-1,4-GalT and the LS complex were identified.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 39, Issues 1–4, 2 May 2006, Pages 98–104
نویسندگان
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