Kinetics and equilibria of condensation reactions between monosaccharide pairs catalyzed by Aspergillus niger glucoamylase
Arabinose, fructose, galactose, myo-inositol, lyxose, mannose, ribose, and xylose were incubated individually and with glucose in the presence of Aspergillus niger glucoamylase at pH 4.5 and 45 degrees C. Glucoamylase condenses galactose, glucose, and mannose individually into disaccharides. It also...
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Published in: | Biotechnology and bioengineering Vol. 56; no. 1; pp. 9 - 22 |
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Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
Published: |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
05-10-1997
Wiley |
Subjects: | |
Online Access: | Get full text |
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Summary: | Arabinose, fructose, galactose, myo-inositol, lyxose, mannose, ribose, and xylose were incubated individually and with glucose in the presence of Aspergillus niger glucoamylase at pH 4.5 and 45 degrees C. Glucoamylase condenses galactose, glucose, and mannose individually into disaccharides. It also produces mixed disaccharides when each of the eight carbohydrates is incubated with glucose. Many products were identified by gas chromatography of the derivatized reaction mixtures followed by mass spectroscopy of the individual chromatographic peaks. Galacto, gluco-, or mannopyranosyl rings appear to be present at the nonreducing ends of all the disaccharides produced. Molecules linked through primary hydroxyl groups have the highest equilibrium constants of all products formed, since these bonds are thermodynamically favored. However, glucoamylase is capable of forming bonds with many available hydroxyl groups, as previously demonstrated when it was incubated with glucose alone. Formation rates of different bonds linking different residues vary widely. These results demonstrate that glucoamylase has a wide selectivity toward residues it will condense into disaccharides and toward bonds it will form between them. |
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Bibliography: | ArticleID:BIT2 istex:8F51F00B34DA8E22B6EEC2474E631FBD22B691D9 ark:/67375/WNG-W4GVLJF7-0 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0006-3592 1097-0290 |
DOI: | 10.1002/(SICI)1097-0290(19971005)56:1<9::AID-BIT2>3.0.CO;2-O |