Purification and some properties of a protease from the sarcocarp of musk melon fruit

M Kaneda, H Yonezawa, T Uchikoba

Index: Kaneda, Makoto; Yonezawa, Hiroo; Uchikoba, Tetsuya Bioscience, Biotechnology, and Biochemistry, 1997 , vol. 61, # 12 p. 2100 - 2102

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Citation Number: 20

Abstract

A protease has been purified from sarcocarp of musk melon, Cucumis melo ssp. melo var. reticulatus Naud. Earl's Favourite. The protease was mostly present in the placenta part of the fruit and next in the inside mesocarp. The molecular mass of the enzyme was estimated to be about 62kDa on SDS-PAGE. The enzyme had a carbohydrate moiety. The optimum pH of the enzyme was 11 at 35° C using casein as a substrate. The enzyme was stable ...