Food Engineering / Gıda Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/12
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Article Citation - WoS: 48Citation - Scopus: 59Biochemical and Thermal Properties of Ss-Galactosidase Enzymes Produced by Artisanal Yoghurt Cultures(Elsevier Ltd., 2010) Üstok, Fatma Işık; Tarı, Canan; Harsa, Şebnemβ-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. © 2009 Elsevier Ltd. All rights reserved.Article Citation - WoS: 45Citation - Scopus: 52Biochemical and Thermal Characterization of Crude Exo-Polygalacturonase Produced by Aspergillus Sojae(Elsevier Ltd., 2008) Tarı, Canan; Doğan, Nergiz; Göğüş, NihanCrude exo-polygalacturonase enzyme (produced by Aspergillus sojae), significant for industrial processes, was characterized with respect to its biochemical and thermal properties. The optimum pH and temperature for maximum crude exo-polygalacturonase activity were pH 5 and 55 °C, respectively. It retained 60-70% of its activity over a broad pH range and 80% of its initial activity at 65 °C for 1 h. The thermal stability study indicated an inactivation energy of Ed = 152 kJ mol-1. The half lives at 75 and 85 °C were estimated as 3.6 and 1.02 h, respectively. Thermodynamic parameters, ΔH*, ΔS* and ΔG*, were determined as a function of temperature. The kinetic constants Km and Vmax, using polygalacturonic acid as substrate, were determined as 0.424 g l-1 and 80 μmol min-1, respectively. SDS-PAGE profiling revealed three major bands with molecular weights of 36, 53 and 68 kDa. This enzyme can be considered as a potential candidate in various applications of waste treatment, in food, paper and textile industries.