Paper Title:
Preparation of Genipin by Hydrolysis of Geniposide with Co-Immobilized Enzyme
  Abstract

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, H. Chen, J. F. Wang, Y. L. He, "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
$32.00
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