食品科学2012，Vol.33Issue(5)：129-133,5.
香葱中蒜氨酸酶的分离纯化及其酶学性质
Purification and Enzymatic Properties of Alliinase from Chive （Allium schoenoprasum L.）
付一帆 1周宇 1李星鑫 1刘莹 1王鲁峰 1潘思轶1
作者信息
- 1. 华中农业大学食品科学技术学院,湖北武汉430070
- 折叠
摘要
Abstract
Abstract： Alliinase （EC 4.4.1.4） was isolated from stalks of chive （Allium schoenoprasum L.）, and its enzymatic properties were investigated. The enzyme was purified to apparent homogeneity using various steps, including homogenizing, centrifuging, ammonium sulfate precipitating, dialyzing, DEAE-52 ion exchange chromatography and Sephadex G200 gel filtration chromatography. SDS-PAGE electrophoresis was used to analyze the purity of alliinase. The results showed that the purity of alliinase was high and reached up to electrophoresis purity. The molecular weight of the subunit was 54.5 ku. The specific activity of the pure alliinase was 11.44 U/mg, and the activity recovery rate was 32.1%, which exhibited 19.6-fold enhancement in purity. The optimal reaction temperature and pH of purified alliinase were 45 ℃ and 7.0, respectively. Kinetic studies showed that Kmax and Vmax of alliinase using S-methyl-L-cysteine sulfoxide as the substrate were 45.31 mmol/L and 40.32 μmol/ （mg· min）, respectively.关键词
香葱/蒜氨酸酶/分离纯化/酶学性质Key words
chive (Allium schoenoprasum L.)/alliinase/isolation and purification/enzymatic properties分类
轻工纺织引用本文复制引用
付一帆,周宇,李星鑫,刘莹,王鲁峰,潘思轶..香葱中蒜氨酸酶的分离纯化及其酶学性质[J].食品科学,2012,33(5):129-133,5.
