Purification of β-Glucosidase, One of the Flavor-enhancing Food Enzymes, from Peppermint (Mentha piperita L.) and Its Biochemical Characterization

Aims: Determination of the biochemical properties β-glucosidase in peppermint, which is rich aromatic compounds.
 Study Design: was purified from mint, and characterization enzyme performed.
 Place Duration Study: This study carried out Faculty Arts Sciences Biochemistry laboratory.
 Methodology: Enzyme purification performed by hydrophobic interaction chromatography using a Sepharose 4B-L-tyrosine-1-naphthylamine gel. Optimum pH, temperature, substrate specificity were determined. The effects glucose, δ-gluconolactone some heavy metals on activity investigated.
 Results: with 8-fold 28% yield. protein mint visualized at 65 kDa SDS-PAGE. determined against para- ortho-nitrophenyl β-D-glucopyranoside (p/o-NPG) substrates. Km values 0.4 0.9 mM, Vmax 102.2 EU 96.6 EU, respectively. While optimum pH for 6, temperature 35°C. Effects Ag+2, Fe+3, Zn+2, Cu+2, Pb+2 investigated. Relative activities introduced into reaction medium as 0.75 mM samples without any known inhibitors environment. Fe+3 increased activity, Pb+2, Zn+2 inhibited enzyme, their relative 78, 76, 22, 31%, Glucose competitively when p-NPG substrate. Ki glucose 0.034±0.001 0.038±0.002 respectively.
 Conclusion: has commercial pharmacological importance due to phenolic substances it contains, will contribute studies improving food quality.