Specificity of amylases and cyclodextrin-glucanotransferase in reactions with 2-deoxy-maltooligosaccharides
2-Deoxy-maltooligosaccharides of different chain length were tested as substrates for exo- and endo-amylases. Cleavage occurred with β-amylase, yielding 2,2′-dideoxy-maltose, and with amyloglucosidase. With the α-amylase from Thermomonospora curvata tris-(2-deoxy)maltotriose and the corresponding te...
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Veröffentlicht in: | Carbohydrate research 1997-05, Vol.300 (2), p.153-159 |
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Sprache: | eng |
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Zusammenfassung: | 2-Deoxy-maltooligosaccharides of different chain length were tested as substrates for exo- and endo-amylases. Cleavage occurred with β-amylase, yielding 2,2′-dideoxy-maltose, and with amyloglucosidase. With the α-amylase from
Thermomonospora curvata tris-(2-deoxy)maltotriose and the corresponding tetra- and pentasaccharides were formed. Porcine pancreatic α-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.
Various 2-deoxy-maltooligomers could be obtained by either selective degradation employing amylases or by transfer reactions with CGTs. |
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ISSN: | 0008-6215 1873-426X |
DOI: | 10.1016/S0008-6215(97)00040-2 |