Summary
The reaction velocity of immobilized β-glucosidase was approximated by the first-order reaction kinetics. A plug flow reactor was used for continuous hydrolysis of geniposide with this immobilized enzyme. The activity of this immobilized enzyme was retained 100% for 600 h. The amount of genipin formed by using the immobilized enzyme was 17 fold that formed using the native enzyme without reuse. Using immobilized enzyme, purity and yield of genipin, which is a hydrolyzate of geniposide, was improved comparing with the native enzyme.
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Djerassi, C., Gray, J.D. and Kincl, F.A. (1960). J. Org. Cem., 25, 2174
Fujikawa, S., Fukui, Y., Koga, K. and Kumada, J., (1987-a). J. Ferment. Technol., in press
Fujikawa, S., Yokota, T. and Koga, K., (1987-b. submitted
Sundstrom, D.W., Klei, H.E., Coughlin, R.W., Biederman, G.J. and Brouwer, C.A., (1981). Biotechnol. Bioeng., 23, 473
Vernaldos, D., Klei, H.E. and Sundstrom, D.W, (1980). Enzyme Microbiol. Technol., 2, 112
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Fujikawa, S., Yokota, T., Koga, K. et al. The continuous hydrolysis of geniposide to genipin using immobilized β-glucosidase on calcium alginate gel. Biotechnol Lett 9, 697–702 (1987). https://doi.org/10.1007/BF01024600
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DOI: https://doi.org/10.1007/BF01024600