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作 者:Ran Bi Jing Wu Lingqia Su Wei Xia
机构地区:[1]State Key Laboratory of Food Science and Technology,Jiangnan University,1800 Lihu Avenue,Wuxi 214122,China [2]School of Biotechnology and Key Laboratory of Industrial Biotechnology Ministry of Education,Jiangnan University,1800 Lihu Avenue,Wuxi 214122,China [3]International Joint Laboratory on Food Safety,Jiangnan University,1800 Lihu Avenue,Wuxi 214122,China
出 处:《Systems Microbiology and Biomanufacturing》2023年第3期498-508,共11页系统微生物学与生物制造(英文)
基 金:the National Natural Science Foundation of China(31730067,31801472);the national first-class discipline program of Light Industry Technology and Engineering(LITE2018-03).
摘 要:Nigerose is a kind of rare disaccharide connected by anα-1,3 glucosidic bond,which is a potential probiotic due to its antidigestive properties and beneficial functions.This study identified and characterized a novel GH65 glycoside phosphorylase derived from Anaerosporobacter mobilis(AmNP).This new protein could specifically catalyze the phospholysis of nigerose to generate glucose and glucose-1-phosphate in the presence of phosphate,indicating it was a typical nigerose phosphorylase.Compared to the previously reported nigerose phosphorylases,AmNP exhibited lower affinity towards nigerose in phosphorolysis reaction and higher affinity towards glucose in reverse phosphorolysis reaction,which indicated that AmNP might be superior in the synthetic capability of disaccharide.Then AmNP was employed to synergize with maltose phosphorylase from Lactobacillus brevis(LbMP)to catalyze the synthesis of nigerose using maltose as the substrate.After optimization of reaction conditions,the highest nigerose yield reached 132.0 g/L with a 66.3%conversion rate,which was higher than ever reported cases using the same reaction pathway to our knowledge.These findings on AmNP in this work were expected to provide a new candidate for large-scale enzymatic synthesis of nigerose and have important theoretical significance for studying nigerose phosphorylase.
关 键 词:Nigerose Nigerose phosphorylase Coupling reaction Enzymatic synthesis
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