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Abstract
The release kinetics of the enzyme invertase and alcohol dehydrogenase from yeast and penicillin acylase from E. coli during disruption using various techniques has been investigated. The disruption techniques used were sonication, high-pressure homogenization, and hydrodynamic cavitation. The first-order-release kinetics was applied for the determination of release rate of these enzymes and total soluble proteins. Location factor (LF) values were calculated using these release rates. The location of the enzymes as given by the values of location factor coincided well with those reported in the literature. Varying values of location factor for the same enzyme by different disruption techniques gave some indications about the selectivity of release of a target enzyme by different disruption techniques. Varying values of location factor for the same enzyme with the use of a particular equipment or disruption technique at different conditions reveals the degree to which the cell is disrupted. Few plausible applications of this location factor concept have been predicted and these speculations have been examined. This location factor concept has been used for monitoring the heat-induced translocation of ADH and location of penicillin acylase during the growth period of E. coli cells. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 75: 607–614, 2001.
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