Some characteristics and isolation of novel thermostable β-galactosidase from Thermus oshimai DSM 12092
Makaleler > Tam Makale · 2013
Yazarlar: Yüksel GEZGİN, Muhammed Bahattin TANYOLAÇ, Rengin ELTEM
Food Science and Biotechnology, SCI Expanded İndekslerine Giren Dergi, Uluslararası, Wos, 2013, cilt 22, ss 63-70
DOI: 10.1007/s10068-013-0009-9
Özet
<p>The β-galactosidases belong to the class of hydrolytic enzymes and have been used as lactose hyrolysis. The enzyme is used in reducing lactose milk production, an outstanding industrial product used by a large lactoseintolerant population. This is the first detailed report of some characteristics of β-galactosidase and the gene encoding β-galactosidase in <em>Thermus oshimai</em> DSM 12092. The growth rate (μ, 1/h), and the doubling time (tD, h) for <em>T. oshimai</em> grown both in shaking flasks and in a bioreactor were determined. The optimal temperature and pH for β-galactosidase were determined as 75°C and 7.4, respectively. This enzyme was thermostable and was retained by more than 70% at 90°C for 3 h. The β-galactosidase from <em>T. oshimai</em> DSM 12092 was more stable in basic pH and Zn2+ was the most effective divalent cation. Also, 2 steps of purification consisting of ammonium sulfate precipitation and gel filtration were employed and purified 32-fold.</p>