Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity.

Autor:	Li J; Key Laboratory of China National Light Industry and Food Bioengineering, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China., Wang J; Department of Nutrition and Health, College of Engineering, China Agricultural University, Beijing 100083, China., Yan Q; Department of Nutrition and Health, College of Engineering, China Agricultural University, Beijing 100083, China. Electronic address: yanqj@cau.edu.cn., Guan L; Key Laboratory of China National Light Industry and Food Bioengineering, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China., Yang S; Key Laboratory of China National Light Industry and Food Bioengineering, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China., Jiang Z; Key Laboratory of China National Light Industry and Food Bioengineering, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China; Food Laboratory of Zhongyuan, Luohe 462300, China. Electronic address: zhqjiang@cau.edu.cn.
Jazyk:	angličtina
Zdroj:	Journal of dairy science [J Dairy Sci] 2024 Dec; Vol. 107 (12), pp. 10141-10152. Date of Electronic Publication: 2024 Jul 14.
DOI:	10.3168/jds.2024-24884
Abstrakt:	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. (© 2024, The Authors. Published by Elsevier Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).)
Databáze:	MEDLINE
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