Biochemical and thermal properties of β-galactosidase enzymes produced by artisanal yoghurt cultures

Abstract

Abstract β-Galactosidases, produced by pure and mixed cultures of Streptococcus thermophilus 95/2 (St 95/2) and Lactobacillus delbrueckii ssp bulgaricus 77 (Lb 77) isolated from the Toros mountain region of Turkey, were characterised with respect to their biochemical and thermal properties. Optimum pH and temperature for maximum activity were determined and these enzymes were stable in the pH range 7–9 and in the temperature range 20–37 °C, retaining 80–90% of their initial activities. The inactivation energies of β-galactosidase from Lb 77, St 95/2 and mixed culture (Lb 77 and St 95/2) were 51.3, 44.0 and 48.3 kcal mol−1, respectively. Moreover, thermodynamic (ΔG, ΔS, ΔH) and kinetic constants (Km and Vmax) were determined and effects of metal ions were investigated. As a result, these enzymes could be considered as potential candidates for lactose hydrolysis of milk and milk products.