Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity
ABSTRACT: The transgalactosylase activity of β-galactosidases offers a convenient and promising strategy for conversion of lactose into high-value oligosaccharides, such as galactooligosaccharides (GOS) and human milk oligosaccharides. In this study, we cloned and biochemically characterized a novel...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2024-12-01
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| Series: | Journal of Dairy Science |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022030224009974 |
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| Summary: | ABSTRACT: The transgalactosylase activity of β-galactosidases offers a convenient and promising strategy for conversion of lactose into high-value oligosaccharides, such as galactooligosaccharides (GOS) and human milk oligosaccharides. In this study, we cloned and biochemically characterized a novel C-terminally truncated β-galactosidase (PaBgal2A-D) from Paenibacillus antarcticus with high transglycosylation activity. PaBgal2A-D is a member of glycoside hydrolase family 2. The optimal pH and temperature of PaBgal2A-D were determined to be pH 6.5 and 50°C, respectively. It was relatively stable within pH 5.0–8.0 and up to 50°C. PaBgal2A-D showed high transglycosylation activity for GOS synthesis, and the maximum yield of 50.8% (wt/wt) was obtained in 2 h. Moreover, PaBgal2A-D could synthesize lacto-N-neotetraose (LNnT) using lactose and lacto-N-triose II, with a conversion rate of 16.4%. This study demonstrated that PaBgal2A-D could be a promising tool to prepare GOS and lacto-N-neotetraose. |
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| ISSN: | 0022-0302 |