Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Brazilian Journal of Chemical Engineering

Guiyou Liu¹  Lei Sun¹  Xiuxiu Wu¹  Wen Zhang¹  Jianshu Feng¹  Yi Cui¹  Zhou Lu¹  Jiaojiao Shen¹  Zhonghua Liu¹  Sheng Yuan¹ 

[1] ,Nanjing Normal University College of Life Science Technology Research Center for Industrialization of Microbial Resources Jiangsu Province ,China

关键词: Puerarin;    Immobilized enzyme;    Puerarin-7-O-Glucoside;    Microbacterium oxydans;    DEAE-52 Cellulose;   

DOI  :  10.1590/0104-6632.20140312s00002768

来源: SciELO

【 摘 要 】

For immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 on DEAE-52 cellulose, the optimal amount of enzyme protein was 12 mg protein: 1 g DEAE-52 cellulose; the optimal pH was 6.5; and the optimal immobilization time was 6 hr. The specific activity of immobilized enzyme was 36.67 mU.g-1 carrier with an immobilization yield of 98.87% and an enzyme recovery yield of 92.43%. The molar transformation rates of puerarin by immobilized enzyme and by the relative bacterial cell amount equal to the same amount of enzyme were 53.3% and 2.2%, respectively, after 1 hr of transformation. The former molar transformation rate, which was similar to that for free enzyme, was more than 24-fold greater than the latter. The immobilized puerarin glycosidase showed improved enzymatic properties and stability. The immobilized puerarin glycosidase retained 88% of its initial activity after being reused 10 times.

【 授权许可】

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