期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1997
卷号：43
期号：5
页码：581-589
DOI：10.3177/jnsv.43.581
出版社：Center for Academic Publications Japan
摘要：Kiwifruit ( Actinidia chinensis ) contains abundant protease, actinidin, and two possible components which were named Al and A2. However, a comparison of the two components has not been thoroughly conducted. We have previously shown the presence of six proteases named KPI, KP2, KP3, KP4, KP5 and KP6 in kiwifruit, and that each purified kiwifruit protease was chromatographically pure. It was also indicated that the two representative components, KP4 and KP6, must be Al and A2. To establish whether or not the two proteases, KP4 and KP6, have the same specificity in proteolytic activity, their enzymatic properties were compared. Between the two proteases, differences in substrate specificity against several protein-substrates (casein, gelatin, collagen, ovalbumin and bovine serum albumin) were not observed by digestion-product analysis with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The kinetic parameters of KP4 against N-α-carbobenzoxyl-lysinep-nitrophenyl esters were different from those of KP6. The pH-activity profiles of KP4 and KP6 against S-3-trimethylaminopropyl-lysozyme, a wide-pH range soluble substrate, and N-α-carbobenzoxyl-lysine p -nitrophenyl esters were different.
