Title: The Effects of Substrate Concentration and Temperature on the Rate of Hydrolysis of the Enzyme Trypsin. Abstract: Quantitative measurements can relate both temperature and substrate concentration to the enzymatic activity of trypsin. By analyzing the data, it is suggested that at BAPNA concentrations below those corresponding to Vmax are rate limiting, as less active sights are available for adhesion. The values of Vmax and Km relate a temperate catalytic efficiency of trypsin. The temperature range of most efficiency for the enzyme was those between 36 and 54 degrees Celsius. Introduction: Enzymes are specialized proteins that aid in formation or breakdown of larger protein or multi-protein complexes. Trypsin is a pancreatic protease that digests proteins by hydrolyzing the peptide bonds in proteins. It has a high degree of specificity and will only hydrolize the peptide bonds that occur on the carboxyl side of the amino acids lysine or arginine. Generally hydrolytic reactions occur with the addition of water to breakdown a large protein into two protein fragments. Substrate concentration and temperature both would interfere and affect with the hydrolysis of Na-benzol-L-arginly-p-nitroanalide (BAPNA) into arginina and p-nitroaniline (PNA). An increase in the substrate concentration would most likely enhance the conversion into PNA, as collisions between the enzyme and substrate would increase. Temperature and pH can both influence the kinetics of an enzyme (Karp 100). Trypsin, being an organic enzyme, would probably work most effectively at temperatures consistent with biological life, falling in the ranges of 34C and 40C. The change in PNA concentration can be plotted against BAPNA concentration or temperature. To measure the kinetics of an enzyme, two variables can be found, Vmax and Km. Km is the estimated substrate concentration required for the reaction to advance at one half Vmax. Vmax is the…
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