Preparation of Genipin by Hydrolysis of Geniposide with Co-Immobilized Enzyme

Abstract:

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Co-immobilize enzyme by cross-linking and embedding, optimize conditions for immobilizing, determinate the enzymatic properties of co-immobilized enzyme and study the methods for preparation of genipin using co-immobilized enzyme to hydrolyze geniposide. Optimized immobilizing conditions include glutaraldehyde concentration being 0.15%, cross-linking temperature being 20°C, cross-linking time being 2 hours, the activity of co-immobilized β-glucosidase and cell reaches to 65.33U/mg and the enzyme activity recovery being 52.63%. Enzymatic properties of co-immobilized enzyme are following: optimum temperature is 55°C and optimum pH is 5.0. The transformation experiments are carried out with co-immobilized enzyme. The results show that half-life of co-immobilized enzyme reaches around 40 days, higher than the normal immobilized enzyme. The conversion rate of geniposide is above 95% after 8 hours. The genipin is isolated, purified and recrystallized to reach more than 98% of purity by High Performance Liquid Chromatography. Advantages to prepare genipin using co-immobilized enzyme include low cost, high yield, environmental friendly and easy to manufacturing.

Info:

Periodical:

Advanced Materials Research (Volumes 236-238)

Edited by:

Zhong Cao, Yinghe He, Lixian Sun and Xueqiang Cao

Pages:

1793-1798

DOI:

10.4028/www.scientific.net/AMR.236-238.1793

Citation:

H. Z. Liang et al., "Preparation of Genipin by Hydrolysis of Geniposide with Co-Immobilized Enzyme", Advanced Materials Research, Vols. 236-238, pp. 1793-1798, 2011

Online since:

May 2011

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Price:

$35.00

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