کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10801031 | 1054723 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Glycosylation of internal sugar residues of oligosaccharides catalyzed by α-galactosidase from Aspergillus fumigatus
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Glycosylation of internal sugar residues of oligosaccharides catalyzed by α-galactosidase from Aspergillus fumigatus Glycosylation of internal sugar residues of oligosaccharides catalyzed by α-galactosidase from Aspergillus fumigatus](/preview/png/10801031.png)
چکیده انگلیسی
Purified α-galactosidase from a thermotolerant fungus Aspergillus fumigatus IMI 385708 was found to catalyze efficiently transgalactosylation reactions using 4-nitrophenyl α-d-galactopyranoside as glycosyl donor. Self-transfer reactions with this substrate afforded in low yields several 4-nitrophenyl galactobiosides. Monosaccharides also served as poor glycosyl acceptors. Disaccharides and particularly higher oligosaccharides of α-1,4-gluco- (maltooligosaccharides), β-1,4-gluco- (cellooligosaccharides) and β-1,4-manno-series were efficiently galactosylated, the latter being the best acceptors that were also doubly galactosylated. With mannooligosaccharides product yields increased with polymerization degree of acceptors reaching 50% at DP of 4-6. Longer oligosaccharide acceptors were galactosylated at internal sugar residues. All galactosyl residues were transferred exclusively to the primary hydroxyl group(s) at C-6 position of oligosaccharide acceptors. This is in accordance with the inability of the enzyme to transfer galactose to β-1,4-linked xylooligosaccharides. This is the first report of glycosyl transfer reaction to internal sugar residues of oligosaccharides catalyzed by a glycosidase. High affinity to oligosaccharide acceptors also opens a way toward enzymatic glycosylation of polysaccharides, thus modulating their physico-chemical and biological properties.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1726, Issue 2, 15 November 2005, Pages 206-216
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1726, Issue 2, 15 November 2005, Pages 206-216
نویسندگان
VladimÃr Puchart, Peter Biely,