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

AUTOR(ES)

Liu, Guiyou, Sun, Lei, Wu, Xiuxiu, Zhang, Wen, Feng, Jianshu, Cui, Yi, Lu, Zhou, Shen, Jiaojiao, Liu, Zhonghua, Yuan, Sheng

FONTE

Braz. J. Chem. Eng.

DATA DE PUBLICAÇÃO

2014-06

RESUMO

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.

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