?-Galactosidase enzyme from indigenous Leuconostoc mesenteroides: extraction, partial purification and characterization

Abstract

Priadi G, Setiyoningrum F, Afaiti F. 2018. ?-Galactosidase enzyme from indigenous Leuconostoc mesenteroides: extraction,
partial purification and characterization. Pros Sem Nas Masy Biodiv Indon 4: 184-189. Dairy industry uses ?-galactosidase in product
development for lactose intolerance. The aim of this study was to determine the characterization of ?-galactosidase partially purified
from indigenous Leuconostoc mesenteroides to temperature and pH. Purification of enzymes using ammonium sulfate with
concentration 40%, 50%, and 60%. Characterization was carried out at 30, 40, 50 and 60 0C, as well as at pH 5, 6 and 7. The results
showed that ?-galactosidase with 50% ammonium sulfate precipitation had the highest specific activity. The optimal work of ?-
galactosidase in hydrolyzing ?-NPG is obtained at temperature 30 0C and pH 7. Ammonium sulfate concentration and temperature
influenced the specific activity of ?-galactosidase enzyme from Leuconostoc mesenteroides.