Influences of nonuniform activity distributions on the apparent maximum reaction rate and apparent Michaelis constant of immobilized enzyme reactions |
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| Institution: | 1. Department of Biochemical Engineering and Science, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Fukuoka 820, Japan;2. Department of Chemical and Biological Engineering, Sasebo College of Technology, 1-1 Okishin, Sasebo, Nagasaki 857-11, Japan;1. University of Belgrade, School of Medicine, Institute of Chemistry in Medicine, Visegradska 26, 11000 Belgrade, Serbia;2. University of Belgrade, The Vin?a Institute of Nuclear Sciences, 11000 Belgrade, Serbia;3. University of Belgrade, Faculty of Technology and Metallurgy, Karnegijeva 4, 11001 Belgrade, Serbia;1. Ege University, Faculty of Science, Biochemistry Department, Bornova, 35100 Izmir, Turkey;2. Ege University, Faculty of Science, Chemistry Department, Bornova, 35100 Izmir, Turkey;3. University of Perugia, Civil and Environmental Engineering Department, UdR INSTM, Strada di Pentima4, Italy;4. Dicle University, Faculty of Science, Chemistry Department, 21280 Diyarbakir, Turkey;5. Ege University, Institute of Drug Abuse Toxicology & Pharmaceutical Sciences, Bornova, 35100 Izmir, Turkey;1. Dipartimento di Chimica, Università di Bari, Italy;2. CSGI (Research Center for Colloids and Nanoscience), Bari, Italy;3. CNR-IPCF, Istituto per i Processi Chimico-Fisici, UO di Bari, Italy |
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| Abstract: | The influences of nonuniform activity distribution within a porous solid support on the apparent kinetic parameters, Vmapp and Kmapp, of immobilized enzyme reactions following the Michaelis-Menten kinetics were theoretically investigated. As the enzyme is distributed to the neighborhood of the external surface of the support, Vmapp and Kmapp approach their respective intrinsic values over a wide range of substrate concentration. There is a close relationship between the nonuniform distribution and internal diffusional resistance. Changes in these two factors provide similar effects on Vmapp and Kmapp. As long as the immobilized enzyme reaction follows Michaelis-Menten kinetics, the nonuniform activity distribution never makes Kmapp less than its intrinsic value. |
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