Transferase Activity of Lactobacillal and Bifidobacterial β-Galactosidases with Various Sugars as Galactosyl Acceptors
© 2016 American Chemical Society. The β-galactosidases from Lactobacillus reuteri L103 (Lreuβgal), Lactobacillus delbrueckii subsp. bulgaricus DSM 20081 (Lbulβgal), and Bifidobacterium breve DSM 20281 (Bbreβgal-I and Bbreβgal-II) were investigated in detail with respect to their propensity to transf...
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| Main Authors: | , , , , , |
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| Format: | Journal |
| Published: |
2018
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| Subjects: | |
| Online Access: | https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84963579469&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/55034 |
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| Institution: | Chiang Mai University |
| Summary: | © 2016 American Chemical Society. The β-galactosidases from Lactobacillus reuteri L103 (Lreuβgal), Lactobacillus delbrueckii subsp. bulgaricus DSM 20081 (Lbulβgal), and Bifidobacterium breve DSM 20281 (Bbreβgal-I and Bbreβgal-II) were investigated in detail with respect to their propensity to transfer galactosyl moieties onto lactose, its hydrolysis products D-glucose and D-galactose, and certain sugar acceptors such as N-acetyl-D-glucosamine (GlcNAc), N-acetyl-d-galactosamine (GalNAc), and L-fucose (Fuc) under defined, initial velocity conditions. The rate constants or partitioning ratios (kNu/kwater) determined for these different acceptors (termed nucleophiles, Nu) were used as a measure for the ability of a certain substance to act as a galactosyl acceptor of these β-galactosidases. When using Lbulβgal or Bbreβgal-II, the galactosyl transfer to GlcNAc was 6 and 10 times higher than that to lactose, respectively. With lactose and GlcNAc used in equimolar substrate concentrations, Lbulβgal and Bbreβgal-II catalyzed the formation of N-acetyl-allolactosamine with the highest yields of 41 and 24%, respectively, as calculated from the initial GlcNAc concentration. |
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