Proteolytic reactions were investigated by using enzymes with different specificities, namely trypsin and savinase under the optimal conditions for each enzyme. The proteolytic products were analyzed by high performance liquid chromatography and fractionated according to the molecular weight. Removal of protein substrate from fibers was simultaneously evaluated by determining nitrogen content before and after proteolysis. Thus, the relationship between removability of protein from fibers and the proteolytic behavior was studied with the progress of the proteoylsis. Large differences were observed between proteolytic behavior of trypsin with high specificity and that of savinase with low specificity, i.e., proteoylsis by trypsin gave products of relatively high molecular weights in a range of M
w 10
4-10
5, and ratios of lower molecular weight fractions were considerably low. On the other hand, savinase produced much larger amounts of lower molecular weight fractions in the order of M
w 10
2 or of the level of amino acids. Savinase gave all peaks of hydrolyzates after 10 min-incubation and every peak showed a large enhancement with incubation time, while 30 min-incubation was required in the case of trypsin before appearing all peaks, and less increase was obverved even after 60 min-incubation. Removability of protein substrate from fibers showed a good agreement with such proteolytic behavior, particularly producing of low molecular weight fractions, and was dominated mainly by the ratio of fractions with low molecular weights in the order of M
w 10
2. Savinase was less affected by a surfactant showing less inhibition of proteolytic activity and lower reduction of removability of protein substrate by the addition of a surfactant.
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