Article citationsMore>>

T. Kotake, S. Dina, T. Konishi, S. Kaneko, K. Igarashi, et al., “Molecular Cloning of a β-Galactosidase from Radish That Specifically Hydrolyzes β-1 → 3- and β-1 → 6-Galactosyl Residues of Arabinogalactan Protein,” Plant Physiology, Vol. 138, No. 3, 2005, pp. 1563-1576. doi:10.1104/pp.105.062562

has been cited by the following article:

• TITLE: Kinetic Studies on β-Galactosidase Isolated from Apricots (Prunus armeniaca kaisa)

  AUTHORS: Sadaf Gulzar, Shajrul Amin

  KEYWORDS: β-Galactosidase; Apricots; Chromatography; Enzyme Kinetics

  JOURNAL NAME: American Journal of Plant Sciences, Vol.3 No.5, May 30, 2012

  ABSTRACT: β-galactosidase was extracted from apricots (Prunus armeniaca kaisa) and characterized biochemically. Three isoenzymes (β-gal I, β-gal II and β-gal III) were obtained by salt fractionation and ionexchange and Sephadex G-100 column chromatography. β-galactosidase II showed a high ability to hy-drolyze the substrate p-nitrophenyl β-D-galactopyranoside than that of β-galactosidase I and III. The individual peaks showed charge homogeneity as revealed by single band on polyacrylamide gel. The molecular weight of β-gal I, β-gal II and β-gal III as determined by gel filtration was found to be 44.15, 34.70 and 23.71 KDa respectively. The optimum pH for the activity different isozymes was found between 4 and 6. The isoenzymes were determined to be thermally stable upto 40?C. The Km value for β-gal I was 1.85 mM which was higher than that of β-gal II (Km = 1.7), and β-gal III (Km = 1.19). The Vmax value for β-gal I, β-gal II and β-gal III was found to be 0.52, 0.70 and 0.38 μmole/min respectively.