Characterization of beta-galactosidase enzyme from thermophilic geobacillus vulcani 2Çx in Çermik hot spring

In this study, it was aimed to purify the Geobacillus vulcani 2Çx strain isolated from the Çermik hot water spring in Diyarbakır province, since it produces β-galactosidase in large quantities and the enzyme is thermostable. For this, intracellular and extracellular enzyme production was investigated in different nutrient media. Various purification steps such as precipitation and gel filtration were applied to obtain extracellular β-galactosidase. Partially purified β-galactosidase had a purification coefficient of 206.6, a yield of 4.17% and a specific activity of 8651.4 U/mg. The molecular weight of the purified enzyme was determined as ~104 kDa by SDS PAGE. The optimum temperature of the partially purified enzyme was determined as 55 ºC and it was determined that it maintained its stability at a rate of 73.93% until the first hour at 55 ºC. It was determined that the optimum pH and pH stability of the enzyme was 7.0. Partially purified enzyme can be used in biotechnological applications. Key words Extracellular β-galactosidase, Geobacillus vulcani 2Çx, thermophilic, purification