99A-7 |
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S.-W. CHANG1, C.-J. Shieh2, G.-C. Lee3, and J.-F. Shaw3. (1) Institute of Bioscience and Biotechnology, National Taiwan Ocean University, 2 Pei-Ning Road, Keelung, 202, Taiwan, (2) Department of Bioindustry Technology, Dayeh University, 112 Shan-Jiau Road, Changhua, 51505, Taiwan, (3) Institute of Botany, Academia Sinica, Nankang, 11529, Taiwan Candida rugosa lipase (CRL) has been employed to catalyze a wide range of chemical reactions such as nonspecific, stereo-specific hydrolysis and esterification for industrial application. There are different isoforms encoded by lip gene family, namely LIP1 to LIP7, in which the recombinant LIP1 showed a distinguished catalytic activity. To higher lipolytic activity of LIP1, the recombinant CRL lip1 has been expressed in the P. pastoris. In this study, response surface methodology (RSM) and 4-factor-5-level central composite rotatable design (CCRD) were adopted to evaluate the effects of growth parameters, such as temperature (21.6 to 38.4 C), glucose concentration (0.3 to 3.7%), yeast extract (0.16 to 1.84%), pH (5.3 to 8.7) on lipolytic activity of LIP1 and biomass of P. pastoris. Based on ridge max analysis, the optimum LIP1 production conditions were: temperature 24.1 C, glucose concentration 2.6%, yeast extract 1.4%, and pH 7.6. The predicted value of lipolytic activity was 246.9 U/mL and the actual value was 253.3 U/mL.
Session 99A, Biotechnology: General
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