大蒜γ-谷氨酰转肽酶的分离纯化和部分酶学性质研究  

Studies on the Purification and Partial Enzymology Characterization of γ-Glutamyl Transpeptidase in Garlic

作　　者：赵飞[1] 乔旭光[1] 

机构地区：[1]山东农业大学食品学院,山东泰安271018

出　　处：《中国食品学报》2009年第1期41-45,共5页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家自然科学基金资助(30571303)

摘　　要：对大蒜中γ-谷氨酰转肽酶进行分离纯化并对其部分酶学性质进行研究。依次采用硫酸铵沉淀法、Phenyl-SepharoseCL-4B疏水层析法、ConA-Sepharose亲和层析法纯化γ-谷氨酰转肽酶。经SDS-PAGE测定,酶的分子质量为68000Da,其所含2个亚基的分子质量分别为54000Da和14000Da;由苯酚-硫酸法测得酶的含糖量为11.31%;根据β-消除反应推测其糖肽键类型为N-型,其最大吸收波长为275nm。Purification and study partial Enzymology characterization of γ-Glutamyl transpeptidase from garlic. γ- Glutamyl transpeptidase was purified to homogeneity using various steps, including ammonium sulfate precipitation method, hydrophobic interaction chromatography on Phenyl-Sepharose CL-4B, affinity chromatography on ConA-sepharose. Its molecule mass was estimated to be 68 000 Da by SDS-polyacrylamide gel electrophoresis, and it was comprised of two subunits, with molecular mass of 54 000 Da and 14 000 Da. The content of carbohydrate was determined to be 11.31% by phenol-sulphuric acid method. The glycosidic linkage of γ-Glutamyl transpeptidase was inferred to be N-type by β-Eliminations. The maximum absorption wavelength of γ-Glutamyl transpeptidase was detected to be 275 nm.

关 键 词：大蒜 Γ-谷氨酰转肽酶 纯化 

分 类 号：TS201.2[轻工技术与工程—食品科学]