Kinetic studies on exploring lactose hydrolysis potential of β galactosidase extracted from Lactobacillus plantarum HF571129.

ABSTRACT: A novel intracellular β-galactosidases produced by Lactobacillus plantarum HF571129, isolated from an Indian traditional fermented milk product curd was purified and characterized. The β-galactosidases is a hetrodimer with a molecular weight of 60 kDa (larger subunit) and 42 kDa (smaller subunit), as estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was purified 7.23 fold by ultrasonication, ultrafiltration and gel filtration chromatography with an overall recovery of 30.41 %. The optimum temperature for hydrolysis of its preferred substrates, o-nitrophenyl- β-D-galactopyranoside (ONPG) and lactose, are 50 °C (both), and optimum pH for these reactions is 6.5 and 7.5, respectively. The β-galactosidases showed higher affinity for ONPG (Km, 6.644 m

SUBMITTER: Selvarajan E 

PROVIDER: S-EPMC4573140 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature