This title appears in the Scientific Report :
2012
Please use the identifier:
http://dx.doi.org/10.1016/j.molcatb.2012.04.003 in citations.
Synthesis of UDP-activated oligosaccharides with commercial ß-galactosidase from Bacillus circulans under microwave irradiation
Synthesis of UDP-activated oligosaccharides with commercial ß-galactosidase from Bacillus circulans under microwave irradiation
We report here on the synthesis of nucleotide activated oligosaccharides by transglycosylation with beta-galactosidase from Bacillus circulans applying microwave irradiation (MWI) and conventional heating. The presented products could serve as novel inhibitors or donor substrates of Leloir-glycosylt...
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Personal Name(s): | Kamerke, C. |
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Pattky, M. / Huhn, C. / Elling, L. | |
Contributing Institute: |
Zentralabteilung für Chemische Analysen; ZCH |
Published in: | Journal of molecular catalysis / B, 79 (2012) S. 27 - 34 |
Imprint: |
Amsterdam [u.a.]
Elsevier Science
2012
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Physical Description: |
27 - 34 |
DOI: |
10.1016/j.molcatb.2012.04.003 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Journal of Molecular Catalysis B
79 |
Subject (ZB): | |
Publikationsportal JuSER |
We report here on the synthesis of nucleotide activated oligosaccharides by transglycosylation with beta-galactosidase from Bacillus circulans applying microwave irradiation (MWI) and conventional heating. The presented products could serve as novel inhibitors or donor substrates of Leloir-glycosyltransferases. Some of them have been isolated from human milk but the biological role remains unclear due to limited access to the nucleotide oligosaccharides. The synthesis with beta-galactosidases is challenging, because of competing hydrolysis of the product by the same enzyme. Effects of MWI and thermal heating on the hydrolytic and synthetic performance of the enzyme were systematically analysed and described here. We demonstrate that under both conditions similar product yields are obtained, however, the enzymatic hydrolysis of the product is significantly decreased under MWI leading to stable product formation. The obtained product yields and absence of product hydrolysis under MWI can be rationalized by time-dependent activation and inactivation of the beta-galactosidase. (C) 2012 Elsevier B.V. All rights reserved. |