The Potency of Indigenous Lactobacillus farciminis LIPI12-2-LAB033 Isolated from Non-Dairy Product of Indonesian Fermented Food as a New Source of β-galactosidase Enzyme
The β-galactosidase is an enzyme that plays an essential role in the lactose hydrolysis into glucose and galactose. This study examines the potential of β-galactosidase from several lactic acid bacteria (LAB) isolated from non-dairy products Indonesian fermented foods and purifies them to increase their specific activity. The enzyme was extracted using ultrasonication, purified with ammonium sulfate, and dialyzed with a cellulose membrane (11 kDa). The result of isolates tests showed that Lactobacillus farciminis LIPI12-2-LAB033 had the highest specific activity of 13.9 U/mg protein. Precipitation using 40% ammonium sulfate increased the specific activity up to 19.6 U/mg protein. This enzyme works optimally at a temperature of 40 °C and pH of 7. The specific activity of this enzyme increases to 75.6 U/mg protein after dialysis. The dialysis process purifies the enzyme 5.44 times with a yield of 26.7%. These findings indicate that Lactobacillus farciminis LIPI12-2-LAB033 can be considered as a source of β-galactosidase enzyme production.