Partial purification and properties of beta-D-galactosidase from persimmon fruit
2003
Ishimaru, M. (Osaka Prefectural Univ., Sakai (Japan)) | Chachin, K. | Ueda, Y.
v-D-galactosidase was partially purified to homogeneity from persimmon (Diospyros kaki Thunb. cv. Tonewase) fruit. The enzyme of G-2 fraction was purified 38. 1-fold with a total yield of 14.6%. The molecular weight of native v-D-galactosidase was estimated to be about 120 kDa by ND-PAGE. After SDS-PAGE of the enzyme electroeluted from native gels, two subunits with estimated molecular masses of 35 kDa and 46 kDa were observed. The optimum pH of the enzyme activity was found to be pH 5.0, and the enzyme stable in the range of pH 5 - 8.
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