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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Elsevier
2024-12-01
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| Series: | Journal of Dairy Science |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022030224009974 |
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| author | Jing Li Jianyu Wang Qiaojuan Yan Leying Guan Shaoqing Yang Zhengqiang Jiang |
| author_facet | Jing Li Jianyu Wang Qiaojuan Yan Leying Guan Shaoqing Yang Zhengqiang Jiang |
| author_sort | Jing Li |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-461afcd9ae3740e8b2dade8a2df19159 |
| institution | OA Journals |
| issn | 0022-0302 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Dairy Science |
| spelling | doaj-art-461afcd9ae3740e8b2dade8a2df191592025-08-20T02:07:00ZengElsevierJournal of Dairy Science0022-03022024-12-0110712101411015210.3168/jds.2024-24884Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activityJing Li0Jianyu Wang1Qiaojuan Yan2Leying Guan3Shaoqing Yang4Zhengqiang Jiang5Key Laboratory of China National Light Industry and Food Bioengineering, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, ChinaDepartment of Nutrition and Health, College of Engineering, China Agricultural University, Beijing 100083, ChinaDepartment of Nutrition and Health, College of Engineering, China Agricultural University, Beijing 100083, China; Corresponding authorsKey Laboratory of China National Light Industry and Food Bioengineering, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, ChinaKey Laboratory of China National Light Industry and Food Bioengineering, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, ChinaKey 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; Corresponding authorsABSTRACT: 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.http://www.sciencedirect.com/science/article/pii/S0022030224009974β-galactosidasetransglycosylationgalactooligosaccharideshuman milk oligosaccharideslacto-N-neotetraose |
| spellingShingle | Jing Li Jianyu Wang Qiaojuan Yan Leying Guan Shaoqing Yang Zhengqiang Jiang Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity Journal of Dairy Science β-galactosidase transglycosylation galactooligosaccharides human milk oligosaccharides lacto-N-neotetraose |
| title | Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity |
| title_full | Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity |
| title_fullStr | Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity |
| title_full_unstemmed | Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity |
| title_short | Biochemical characterization of a novel C-terminally truncated β-galactosidase from Paenibacillus antarcticus with high transglycosylation activity |
| title_sort | biochemical characterization of a novel c terminally truncated β galactosidase from paenibacillus antarcticus with high transglycosylation activity |
| topic | β-galactosidase transglycosylation galactooligosaccharides human milk oligosaccharides lacto-N-neotetraose |
| url | http://www.sciencedirect.com/science/article/pii/S0022030224009974 |
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