# Purification and characterization of α-glucosidase enzyme from rice groats > Papriani N.P. URL kanonis: https://discover.unhas.ac.id/publications/purification-and-characterization-of-glucosidase-enzyme-from-rice-groats Jurnal / Konferensi: Journal of Physics Conference Series Tahun terbit: 2019 DOI: https://doi.org/10.1088/1742-6596/1341/3/032017 ISSN: 17426588 Citations: 1 ## Authors - Papriani N.P. ## Abstract Abstract Groat rice is the side product of rice milling process and potentially producing α-glucosidase. The enzyme has an important role in starch degradation process by breaking α-glycosidic bods to form glucose. This research aimed to understand the optimum activity of the purified α-glucosidase. The research stages are isolation, purification, characterization of substrate concentration, pH level, incubation time, temperature, and effect of metal ion, and dinitrosalicylic acid (DNS) method to determine the activity of α-glucosidase. The result showed the specific activity of α-glucosidase crude extract at 0.003 IU/mg. Fractionation of the highest specific activity on fraction 4 revealed at 0.042 IU/mg and constantly increasing on the dialysis stage at 1.121 IU/mg. α-glucosidase reached optimum activity at substrate concentration 2%, pH of 7, incubation time of 40 minutes, at 37°C, with metal ion Mn 2+ , Co 2+ , Na + , Mg 2+ , Ca 2+ and K + as activators and Zn 2+ as inhibitor. α-glucosidase could be used to find analog compounds as the cure of type 2 diabetes mellitus. ## Keywords - Chemistry - Incubation - Substrate (aquarium) - Enzyme - Starch - Chromatography - Fractionation - Hydrolysis - Enzyme assay - Metal ions in aqueous solution - Metal - Nuclear chemistry - Food science - Biochemistry - Organic chemistry - Biology - Ecology --- Sumber: Discover Unhas — RIMS Universitas Hasanuddin. Saat mengutip, gunakan DOI bila tersedia atau URL kanonis di atas.