Purification and Characterization of γ-Glutamyl Transpeptidase from Toona sinensisand Its Function on Formation of Sulfur-Containing Volatiles

Abstract

γ-Glutamyl transpeptidase (GGT) in Toona sinensis shoot (TS) was extracted and purified through salt precipitation, ion-exchange column, and gel filtration chromatography methods. The GGT had two peptides with M.W. 35 and 50 kDa. Its function in the formation of TS sulfur-containing volatiles (SCVs) was evaluated. The highest GGT hydrolytic activity was at pH 7.0 and 50 °C. Its activity was enhanced by Ca²⁺, Mg²⁺, K⁺, Na⁺, and Ba²⁺ and reduced by Cu²⁺, Fe³⁺, Mn²⁺, and Zn²⁺. The SCVs reached the highest level at GGT to TS sulfur-containing precursors extract 1:20. The aroma produced by GGT from the extract was similar to that of raw TS, especially for the cooked onion-like/TS-like flavor. These results revealed the characteristics and function of GGT in TS on sulfurous aroma formation. It could be applied to retrieve the production of sulfur-containing aroma from thermally preserved TS or similar vegetables, which lost GGT activity irreversibly during heat drying.