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Mol. Cells 2003; 15(1): 68-74
Published online January 1, 1970
© The Korean Society for Molecular and Cellular Biology
Purification and Characterization of a b-Galactosidase from Peach (Prunus persica)
A b-galactosidase (EC 3.2.1.23) from peach (Prunus persica cv Mibackdo) was purified and characterized. The purified peach b-galactosidase was 42 kDa in molecular mass and showed high enzyme activity against a the b-galactosidase substrate, r-nitrophenyl-b-D-galactopyranoside. The Km and Vmax values of the enzyme activity of the peach b-galactosidase were 5.16 and 0.19 mM for r-nitrophenyl-b-D-galactopyranoside mM/h, respectively. The optimum pH of the enzyme activity was pH 3.0, but it was relatively stable from pH 3.0-10.0. The temperature optimum was 50
Keywords B-galactosidase, Protein Purification, Prunus persica,
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Research Article
Mol. Cells 2003; 15(1): 68-74
Published online February 28, 2003
Copyright © The Korean Society for Molecular and Cellular Biology.
Purification and Characterization of a b-Galactosidase from Peach (Prunus persica)
Jae Kyun Byun, Dong Hoon Lee, Sang-Gu Kang, Sang-Gon Suh
Abstract
A b-galactosidase (EC 3.2.1.23) from peach (Prunus persica cv Mibackdo) was purified and characterized. The purified peach b-galactosidase was 42 kDa in molecular mass and showed high enzyme activity against a the b-galactosidase substrate, r-nitrophenyl-b-D-galactopyranoside. The Km and Vmax values of the enzyme activity of the peach b-galactosidase were 5.16 and 0.19 mM for r-nitrophenyl-b-D-galactopyranoside mM/h, respectively. The optimum pH of the enzyme activity was pH 3.0, but it was relatively stable from pH 3.0-10.0. The temperature optimum was 50
Keywords: B-galactosidase, Protein Purification, Prunus persica,
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