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苹果根皮素糖基转移酶酶学特性研究
引用本文:徐颖, 樊明涛, 张庭静, 董梅, 黄佳. 苹果根皮素糖基转移酶酶学特性研究[J]. 食品工业科技, 2016, (21): 178-182. DOI: 10.13386/j.issn1002-0306.2016.21.026
作者姓名:徐颖  樊明涛  张庭静  董梅  黄佳
摘    要:以苹果果皮为原料,通过饱和硫酸铵沉淀、DEAE-Sepharose阴离子交换法和Sephadex G75凝胶过滤色谱纯化,获得纯化后的根皮素糖基转移酶,其比酶活达到632.0 U/mg,纯化倍数为71.0倍,回收率达到42.6%。SDS-PAGE鉴定其表观分子量为50 ku。酶的最适p H为8.5,p H7.09.0有利于保持酶的稳定性。最适温度为45℃。以根皮素为底物测定的Km为3.16μmol/L,Vmax为0.77 n M/min·mg蛋白。金属离子在反应体系的终浓度为5 mmol/L时,Ca2+和Mg2+对该苹果根皮素糖基转移酶有促进作用,Na+和K+作用不明显,Al3+、Cu2+、Mn2+和Zn2+有显著的抑制作用,Cu2+的抑制作用最强(p<0.05)。结论:根皮素糖基转移酶具有较好的碱稳定性和热稳定性,在根皮苷的酶法合成方面具有应用潜力。 

关 键 词:苹果根皮素糖基转移酶    纯化    酶学性质  
收稿时间:2016-05-10

Study on the enzymatic properties of Uridine Diphosphate Glucose:phloretin-2'-O-glycosyltransferase from Malus x Domestica
XU Ying, FAN Ming-tao, ZHANG Ting-jing, DONG Mei, HUANG Jia. Study on the enzymatic properties of Uridine Diphosphate Glucose:phloretin-2'-O-glycosyltransferase from Malus x Domestica[J]. Science and Technology of Food Industry, 2016, (21): 178-182. DOI: 10.13386/j.issn1002-0306.2016.21.026
Authors:XU Ying  FAN Ming-tao  ZHANG Ting-jing  DONG Mei  HUANG Jia
Affiliation:1.School of Food and Biological Engineering,Shaanxi University of Science &Technology;2.College of Food Science and Engineering,Northwest A & F University
Abstract:Uridine Diphosphate Glucose: phloretin-2'-O-glycosyltransferase from Malus x Domestica( Md P2'GT)was purified using the ammonium sulfate precipitation,DEAE-Sepharose anion-exchange and Sephadex G75 gel filtration chromatography procedures to apparent homogeneity.Specific activity for purified enzyme was 632.0 U / mg.The purfication fold was 71.0 and recovery rate was 42.6%.The molecular weight was estimated to be 50 ku by SDS-PAGE.The purified enzyme catalyzed the glycosylation reaction with optimal activity at p H8.5 and was stable over a range of p H7.0 ~ 9.0. The optimal temperature for enzyme activity was 45 ℃. The Kmvalue for Md P2 'GT was determined to be 3.16 μmol / L,and Vmaxwas 0.77 n M / min·mg protein. At the concentration of 5 mmol / L,Md P2'GT was found to be activated by the presence of Ca2 +and Mg2 +ions. The activity of Md P2 'GT was not apparently affected by Na+or K+,but it was significantly inhibited by Al3 +,Cu2 +,Mn2 +and Zn2 +.The inhibition effect of Cu2 +was the strongest( p < 0.05).Md P2'GT exhibits p H stability under alkaline condition and thermal stability,which has potential applications in the respect of enzymatic synthesis of phloridzin.
Keywords:UDPG    phloretin-2'-O-glycosyltransferase from Malus x Domestica    purfication    enzymatic property
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