Optimization of Activities of Immobilized Lysozyme, α-Chymotrypsin, and Lipase
Two areas of recent development are enzyme immobilization on solid matrices (1) and chemical modification of proteins by soluble reagents (2). Surprisingly, in development of optimum immobilization recipes, there appear to have been no attempts to correlate results between these clearly related areas of enzyme catalysis. As the specific activity (rate per enzyme) of soluble modified enzymes is easily determined by comparison with that of immobilized enzymes, it may be expected that the existence of such correlations would prove a useful screening device for new immobilization recipes. Prior to presenting this study, several pertinent papers are summarized.
KeywordsNitrite Immobilization Lysine Trypsin Polyacrylamide
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