Open AccessThe 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
Author(s) -
Fitri Setiyoningrum,
Gunawan Priadi,
Fifi Afiati,
Rohmatussolihat Rohmatussolihat,
Aulia Hesti Anjani
Publication year - 2021
Publication title -
industria
Language(s) - English
Resource type - Journals
eISSN - 2549-3892
pISSN - 2252-7877
DOI - 10.21776/ub.industria.2021.010.02.1
Subject(s) - food science , lactose , fermentation , enzyme assay , enzyme , galactose , lactobacillus , bacteria , biochemistry , chemistry , ammonium sulfate , biology , chromatography , genetics
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.