Design of Selective Release and Recovery of Enzymes from Escherichia Coli Based on Their Location Using Nonionic Detzergent, Triton X-Series

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The factors to control the selective release and recovery of enzymes from Escherichia coli cells were examined quantitatively based on kinetic analysis of cell lysis in the treatment with Triton X-100/EDTA. The release rate constant of an enzyme i (k i ) , determined from the first-order kinetics, was found to increase with an increase in the Triton concentration ( C Triton ) at less than 0.02M. The ki values decreased with an increase in molecular weight ( M W ) at 0.65 ∼ 2.0 kDa. The effect of a subcellular distribution of each enzyme on the k i values was also analysed by using the evaluated location factor of the enzymes ( LF i ). The k i values for various enzymes were successfully correlated with the operational parameters regardless of their subcellular location on the single quantitative equation in the range of: 0.002M C Triton M W LF i

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