Enhancing the synthesis efficiency of galacto-oligosaccharides of a β-galactosidase from Paenibacillus barengoltzii by engineering the active and distal sites
文献类型： 外文期刊
作者： Yu, Haiyan 1 ; Wang, Yulu 1 ; Yang, Zhisen 2 ; Ying, Jiabao 1 ; Guan, Feifei 3 ; Liu, Bolin 1 ; Miao, Miao 4 ; Mohamed, Abeer 1 ; Wei, Xue 1 ; Yang, Yuji 1 ; Liu, Xin 2 ; Sun, Linfeng 2 ; Jiang, Zhengqiang 4 ; Yang, Shaoqing 4 ; Xin, Fengjiao 1 ;
作者机构： 1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Lab Biomfg & Food Engn, Beijing 100193, Peoples R China
2.Univ Sci & Technol China, Affiliated Hosp USTC 1, Hefei Natl Res Ctr Phys Sci Microscale, Div Life Sci & Med,Dept Neurol,MOE Key Lab Membran, Hefei 230027, Peoples R China
3.Chinese Acad Agr Sci, Biotechnol Res Inst, Natl Key Lab Agr Microbiol, Beijing 100193, Peoples R China
4.China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China
5.Chinese Acad Agr Sci, Inst Food Sci Technol Nutr & Hlth Cangzhou, Cangzhou 061001, Peoples R China
关键词： beta-Galactosidase; GOS synthesis; Cryo-EM structure; Machine learning; Catalytic mechanism
期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）
ISSN： 0308-8146
年卷期： 2025 年 483 卷
页码：
收录情况： SCI
摘要： Previously, a glycoside hydrolase (GH) family 2 beta-galactosidase (PbBGal2A) from Paenibacillus barengoltzii is characterized for its high transglycosylation capability. Here, the cryo-electron microscopy (cryo-EM) structure of PbBGal2A was determined, revealing an enlarged acidic catalytic pocket that facilitate the binding of carbohydrate substrates. Three structure-based strategies as well as machine learning MECE platform (method for enhancing the catalytic efficiency) were employed to identify active and distal mutations with enhanced galactooligosaccharides (GOS) synthesis and their synergistic effects were evaluated. The best H331V mutation yielded a maximum GOS production of 76.57 % at 4 h when 35 % (w/v) of lactose was used as a substrate. Molecular dynamics (MD) simulation analysis further indicated that distal mutations increase the rigidity of the loops surrounding the catalytic pocket. This research sheds light on the structural and catalytic mechanisms of PbBGal2A, highlighting the importance of both active and distal mutations in the efficient design of customized beta-galactosidases.
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