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In relation to this article, we declare that there is no conflict of interest.
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Received March 8, 2001
Accepted October 5, 2001
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Immobilization of GL-7-ACA Acylase for the Production of 7-ACA

Graduate School of Biotechnology, Korea University, Seoul 136-701, Korea 1Department of Chemical Engineering, Korea University, Seoul 136-701, Korea 2Chong Kun Dang Pharmaceutical Corporation, Seoul 120-010, Korea
Korean Journal of Chemical Engineering, March 2002, 19(2), 261-266(6), 10.1007/BF02698411
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Abstract

Glutaryl-7-aminocephalosporanic acid(GL-7-ACA) acylase is an important enzyme for the production of 7-ACA (7-aminocephalosporanic acid). For an efficient immobilization of GL-7-ACA acylase, various carriers were tested. A high-porous hydrophilic carrier (FPHA) among various carriers tested was found to be the best for the immobilization of GL-7-ACA acylase. In order to develop an effective immobilization method of GL-7-ACA acylase, the parameters that affect the immobilization of GL-7-ACA acylase were also investigated under different conditions of buffer solution and different concentrations of glutaraldehyde. The highest value of GL-7-ACA acylase activity (70 Unit/g-matrix) was obtained when immobilized with 1% glutaraldehyde in a 0.1M Tris buffer (pH 8.0). Also, in order to enhance the activity of the immobilized GL-7-ACA acylase, unreacted aldehyde groups were quenched by reaction with a low molecular weight agent such as L-lysine after immobilization. The highest activity of immobilized GL-7-ACA acylase was obtained at 0.1% of L-lysine. The immobilized GL-7-ACA acylase was tested for long-term_x000D_ stability and it was found that the activity was retained at about 62% of the initial value after 72 times of reuse at 25 ℃.

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