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Specificity of amylases and cyclodextrin-glucanotransferase in reactions with 2-deoxy-maltooligosaccharides
被引:4
|作者:
Evers, B
Petricek, M
Thiem, J
机构:
[1] UNIV HAMBURG, INST ORGAN CHEM, D-20146 HAMBURG, GERMANY
[2] ACAD SCI CZECH REPUBL, INST MICROBIOL, DEPT BIOL MOL, CR-14220 PRAGUE 4, CZECH REPUBLIC
关键词:
cyclodextrin;
exo- and endo-amylases;
glucanotransferase;
ALPHA-AMYLASE;
THERMOMONOSPORA-CURVATA;
SUBSITE BINDING;
SUBSTRATE;
PHOSPHORYLASE;
GLYCOSYLTRANSFERASE;
HYDROLYSIS;
GENE;
D O I:
10.1016/S0008-6215(97)00040-2
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
2-Deoxy-maltooligosaccharides of different chain length were tested as substrates for exoand endo-amylases. Cleavage occurred with beta-amylase, yielding 2,2'-dideoxy-maltose, and with amyloglucosidase. With the alpha-amylase from Thermomonospora curvata tris-(2-deoxy)-maltotriose and the corresponding tetra- and pentasaccharides were formed. Porcine pancreatic a-amylase did not tolerate the deoxygenated substrate, nor were cyclization experiments with cyclodextrin-glucanotransferase (CGT) successful. In a coupling reaction with CGT, however, a series of transfer products to the acceptor 2-deoxyglucose were obtained. (C) 1997 Elsevier Science Ltd.
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页码:153 / 159
页数:7
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