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Isolation and characterization of a possible native cucumisin from developing melon fruits and its limited autolysis to cucumisin

Isolation and characterization of a possible native cucumisin from developing melon fruits and its limited autolysis to cucumisin

Agricultural and Biological Chemistry 53(4): 1009-1018

ISSN/ISBN: 0002-1369

DOI: 10.1271/bbb1961.53.1009

A serine proteinase was purified to an electrophoretically homogenous state from developing fruits of Prince melon (Cucumis melo L. var. Prince). Its molecular mass was 67 kD by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which was apparently different from that of cucumisin (50 kD), a serine proteinase previously isolated from Prince melon. When the purified 67-kD enzyme was incubated at and pH 7.2, it was split into a 54-kD proteinase and a 14-kD polypeptide by limited autolysis without any loss of the caseinolytic activity. Commerical cucumisin preparation was found to contain the 67- and 54-kD proteinases. The content of each amino acid residue in 67-kD enzyme was higher than that in the 54-kD proteinase or cucumisin. Thus, it was concluded that the purified 67-kD enzyme is a native form of cucumisin, and that cucumisin is a product derived by the limited autolysis of the 67-kD proteinase. The 67-kD proteinase was more stable than the 54-kD one at acidic pHs.

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Accession: 001871391

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