Production of isocyclomaltopentaose from starch using isocyclomaltooligosaccharide glucanotransferase
Production of a novel cyclomaltopentaose cyclized by an alpha-1,6-linkage, [ICG5; cyclo-(-6)-alpha-D-Glcp-(1-4)alpha-D-Glcp-(1-4)-alpha-D-Glcp-(1-4)-alpha-D-Glcp-(1-4)-alpha-D-Glcp-(1-)], from starch was performed using isocyclomaltooligosaccharide glucanotransferase (IGTase) derived from Bacillus c...
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Published in | Bioscience, biotechnology, and biochemistry Vol. 70; no. 12; pp. 3013 - 3018 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Tokyo
Japan Society for Bioscience, Biotechnology, and Agrochemistry
01.12.2006
Japan Society for Bioscience Biotechnology and Agrochemistry Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | Production of a novel cyclomaltopentaose cyclized by an alpha-1,6-linkage, [ICG5; cyclo-(-6)-alpha-D-Glcp-(1-4)alpha-D-Glcp-(1-4)-alpha-D-Glcp-(1-4)-alpha-D-Glcp-(1-4)-alpha-D-Glcp-(1-)], from starch was performed using isocyclomaltooligosaccharide glucanotransferase (IGTase) derived from Bacillus circulans AM7. The optimal conditions for ICG5-production from partially hydrolyzed starch were as follows: substrate concentration, 1.0% (w/v); pH, 5.5; temperature, 45 deg C; reaction time, 24 h, IGTase, 1.0 unit/g-dry solid (DS); isoamylase, 2500 units/g-DS. The yield of ICG5 reached 25.9% under optimal conditions. ICG5-production was achieved from partially hydrolyzed starch using a crude enzyme preparation containing IGTase. Finally, ICG5 was obtained in a yield of 17.9 % (99.3% purity, 2681 g-DS). A digestive test with a human salivary amylase, an artificial gastric juice, a pancreatic amylase, and small intestinal enzymes showed that ICG5 was an indigestible oligosaccharide. |
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Bibliography: | 2007006122 Q02 U30 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.60404 |