气质联用法对不同介质中蒜酶催化烯丙基半胱氨酸亚砜

In the present research we used gas chromatography-mass spectrometry (GC-MS) to determine products of S-(2-Propenyl)-L-Cysteine sulphoxide under the action of alliinase in different buffer solutions. The different buffer solutions included 2-PeCSO/acetic acid (pH=2.3), 2-PeCSO/alliinase (pH=5.5) and 2-PeCSO/acetic acid/alliinase (pH=2.3). Conditions for chromatography: HP-5 chromatographic column (30 m×0.25 µm); initial column temperature: 90 ℃, which was maintained for 1 min, then the temperature was increased at a rate of 2 ℃/min to 160 ℃, and maintained for 2 min; then the temperature was increased at a rate of 1 ℃/min to 190 ℃, and maintained for 5 min; temperature for the vaporizing chamber: 220 ℃; carrier gas: helium flowing at 1.0 mL/min. Conditions for mass spectrometry: 70 eV for ionization energy; the temperature of ion source is 230 ℃; temperature for the quadrupole analyzer: 450 ℃; temperature for the detector: 250 ℃; 0.5 µL for sample size; split ratio 1:50. Under the conditions selected for GC-MS, products of S-(2-Propenyl)-L-Cysteine sulphoxide under the action of alliinase in different buffer solutions could be isolated and identified. Acetic acid did not involve in the reaction of garlic greening. Alliinase and acetic acid did not have the role of isomerization 2-PeCSO to 1-PeCSO.