Production and characterization of a thermostable <i>β</i>‐galactosidase from <i>Bacillus coagulans</i> RCS3

Abstract

A strain of Bacillus coagulans RCS3 isolated from a hot-water spring produced significant beta-galactosidase activity at 10 days of growth in a flask. While enzyme production was maximum at 50 degrees C, the highest activity was at 65 degrees C, where the half-life was 2 h. A 2 degrees C decrease in temperature increased the half-life to 15 h without significantly changing the activity, suggesting that 63 degrees C is the temperature of preference compared with 65 degrees C for a combination of good activity and stability. The beta-galactosidase was also stable over pH 5-8, with peak activity at pH 6-7. It was strongly and competitively inhibited by the hydrolysis product galactose. Bivalent cations (Cu(2+), Ni(2+) and Hg(2+)) in the concentration range of 0.5-2.0 mM also inhibited enzyme activity. Both lactose solution and whey could be hydrolysed substantially within 36 h at 50 degrees C. The thermostability and pH-stability and good hydrolytic capability make this enzyme potentially useful in the dairy industry.