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A. T. Carey, K. Holt, S. Picard, R. Wilde, G. A. Tucker, C. R. Bird, W. Schuch and G. R. Seymour, “Tomato Exo-1 → 4-β-D-Galactanase: Isolation, Changes during Ripening in Normal and Mutant Tomato Fruit and Characterization of a Related cDNA Clone,” Plant Physiology, Vol. 108, No. 3, 1995, pp. 1099-1107. doi:10.1104/pp.108.3.1099

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.