Effect of Phytate on Solubility, Activity and Conformation of Trypsin and Chymotrypsin

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Abstract
Phytate:proteinase interactions and their effects on the solubility, activity, and conformation of trypsin and chymotrypsin were investigated in model systems. At pH 3.0, phytate at 0.167‐0.250 (w/w) ratios formed insoluble complexes with both the enzymes, while at pH 7.8, Ca++ was required for the complex formation. At pH 7.8, phytate increased trypsin and chymotrypsin activity by 5‐7%. The mean chymotrypsin activity was increased by about 18% when interactions were carried out at pH 3.0, whereas under similar conditions, trypsin activity was strongly inhibited. Circular dichroism spectroscopic studies revealed conformational changes in the enzyme secondary structure that seemed to have influenced their activity. The role of phytate in protein metabolism and the possible ramifications of present findings in human nutrition were addressed.