Curvularia lunata

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Huh Chyun Wey - One of the best experts on this subject based on the ideXlab platform.

  • Dissolution-enzyme kinetics of 11β-hydroxylation of cortexolone by Curvularia lunata
    Enzyme and Microbial Technology, 1990
    Co-Authors: Kuo Cheng Chen, Huh Chyun Wey
    Abstract:

    The enzyme kinetics of 11β-hydroxylation of cortexolone by whole cells of Curvularia lunata were studied, taking into account the dissolution of the solid substrate. The dissolution behavior of substrate steroid was represented by an empirical expression. A mathematical model was developed to describe the heterogeneous process of steroid hydroxylation, based on the rate of enzyme reaction and the rate of substrate dissolution. The rate of 11β-hydroxylation of solubilized cortexolone coexisting with its solid form was found to be identical to Michaelis-Menten kinetics. The kinetic constants were estimated using experimental data. The good agreement between correlated and experimental values supported the suitability of the established model. © 1990.

Jie Chen - One of the best experts on this subject based on the ideXlab platform.

José María Arias - One of the best experts on this subject based on the ideXlab platform.

U. C. Banerjee - One of the best experts on this subject based on the ideXlab platform.

Kuo Cheng Chen - One of the best experts on this subject based on the ideXlab platform.

  • 11β-Hydroxylation of coxtexolone by Curvularia lunata
    Enzyme and Microbial Technology, 1990
    Co-Authors: Kuo Cheng Chen
    Abstract:

    Abstract The 11β-hydroxylase of Curvularia lunata (NRRL 2380) was demonstrated to be nonconstitutive and intracellularly inducible by cortexolone. The pH change and the color development associated with the mycelial growth can serve as convenient criteria for 11β-hydroxylation process. The feeding time of steroid substrate affects the hydroxylation rate significantly. Feeding of substrate was found to be best at around 8 h of incubation. Hydroxylation could be enhanced when induction was performed at low dissolved oxygen tension (DOT), followed later by DOT elevation in the culture. The effect of DOT on enzyme expression was investigated showing an optimum DOT value of 5.5 ppm for maximum hydroxylation rate .

  • Dissolution-enzyme kinetics of 11β-hydroxylation of cortexolone by Curvularia lunata
    Enzyme and Microbial Technology, 1990
    Co-Authors: Kuo Cheng Chen, Huh Chyun Wey
    Abstract:

    The enzyme kinetics of 11β-hydroxylation of cortexolone by whole cells of Curvularia lunata were studied, taking into account the dissolution of the solid substrate. The dissolution behavior of substrate steroid was represented by an empirical expression. A mathematical model was developed to describe the heterogeneous process of steroid hydroxylation, based on the rate of enzyme reaction and the rate of substrate dissolution. The rate of 11β-hydroxylation of solubilized cortexolone coexisting with its solid form was found to be identical to Michaelis-Menten kinetics. The kinetic constants were estimated using experimental data. The good agreement between correlated and experimental values supported the suitability of the established model. © 1990.