Characterization of intracellular β-galactosidase from Bacillus subtilis 4NK and Bacillus paralicheniformis 5NK isolated from a hot water spring and effects of various inhibitors on enzyme activity

Özet

In this study, the intracellular ?-galactosidases of Bacillus subtilis 4NK and Bacillus paralicheniformis 5NK isolated from Bingöl Binkap hot spring was partially purified and characterized. As a result of purification, the yield of the enzyme for B. subtilis 4NK was 85.2% and the purification fold was 2.8. The yield for B. paralicheniformis 5NK was 76.8% and the purification fold was 2.0. The optimum temperature of the enzyme was determined as 45oC for B. subtilis 4NK and 55oC for B. paralicheniformis 5NK and the optimum pH was 6.0 for both. In addition, in the thermal stability experiments even at the end of 120 min both enzymes were stable at 50oC. It was determined that the partially purified enzyme activity increased in the presence of iodoacetamide and phenylmethylsulfonylfluoride for B. subtilis 4NK, dithiothreitol, N-ethylenemaleimide and phenylmethylsulfonylfluoride for B. paralicheniformis 5NK. The metals were found to activate the enzyme at low concentrations of Co2+, Cd2+ and Mn2+ for B. subtilis 4NK, Cu2+ and Cd2+ were found to inhibit the enzyme at high rates for B. paralicheniformis 5NK. Km and Vmax values for 4NK and 5NK, respectively; 23.80 mM, 1.978 µmol/min and 5.61 mM, 1.869 µmol/min.

Açıklama

Anahtar Kelimeler

Bacillus paralicheniformis 5nk, Bacillus subtilis 4nk, β-galactosidase characterisation

Kaynak

Biotech Studies

WoS Q Değeri

Scopus Q Değeri

Q3

Cilt

30

Sayı

2

Künye

Tunç, Ş., Bekler, F. M. ve Güven, K. (2021). Characterization of intracellular β-galactosidase from Bacillus subtilis 4NK and Bacillus paralicheniformis 5NK isolated from a hot water spring and effects of various inhibitors on enzyme activity. Biotech Studies, 30(2), 71-78.