Kinetic studies of the enzymatic isomerization of xylose |
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Authors: | Graciela N Roman Norman B Jansen Humg-Yu Hsiao George T Tsao |
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Institution: | Laboratory of Renewable Resources Engineering, Purdue University, West Lafayette, IN 47907, USA |
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Abstract: | d-Xylose isomerase catalyses the conversion of the common pentose, d-xylose, to its keto-isomer, d-xylose. This reaction is of interest because many microorganisms that are unable to metabolize d-xylose can utilize d-xylulose. The kinetics of a commonly used immobilized whole-cell isomerase, Sweetzyme Q, have been determined from initial rate studies on the forward and reverse reactions. The effect of pH, temperature, and substrate and product concentration on enzyme activity have all been examined. Reaction rates were modelled with the Michaelis-Menten equation. Using constants determined from Lineweaver-Burk plots, the rate equation accurately simulated experimental conversion data. |
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Keywords: | Kinetics xylose isomerase xylulose |
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