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

机译:手工酸奶培养物产生的β-半乳糖苷酶的生化和热学性质

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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 ℃, 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 (K_m and V_(max)) 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.
机译:从嗜热链球菌95/2(St 95/2)和德氏乳杆菌保加利亚乳杆菌77(Lb 77)的纯培养物和混合培养物中产生的β-半乳糖苷酶的生化和热特性进行了表征属性。确定了最大活性的最佳pH和温度,这些酶在7-9的pH范围和20-37℃的温度范围内稳定,保留了其初始活性的80-90%。 Lb 77,St 95/2和混合培养物(Lb 77和St 95/2)的β-半乳糖苷酶的失活能分别为51.3、44.0和48.3 kcal mol〜(-1)。此外,测定了热力学(ΔG,ΔS,ΔH)和动力学常数(K_m和V_(max)),并研究了金属离子的作用。结果,这些酶可以被认为是牛奶和奶制品乳糖水解的潜在候选者。

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