immobilization of puerarin glycosidase from microbacterium oxydans cgmcc 1788 increases puerarin transformation efficiency
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2014
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Abstract
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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liu2014brazilianimmobilization
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| Authors | ;Guiyou Liu;Lei Sun;Xiuxiu Wu;Wen Zhang;Jianshu Feng;Yi Cui;Zhou Lu;Jiaojiao Shen;Zhonghua Liu;Sheng Yuan |
| Journal | database and network journal |
| Year | 2014 |
| DOI |
10.1590/0104-6632.20140312s00002768
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