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Position: Home > Articles > Purification and Properties of β-fructofuranosidase from Arthrobacter 10137 FOOD SCIENCE 2005 (3) 69-71

节杆菌β-呋喃果糖苷酶的纯化及性质研究

作  者:
童群义;朱桂兰
单  位:
江南大学食品学院
关键词:
节杆菌;β-呋喃果糖苷酶;纯化和性质
摘  要:
采用硫酸铵盐析、透析脱盐、Sepharose 6B凝胶色谱等分离纯化技术,从节杆菌培养液分离纯化了β-呋喃果糖苷酶,纯化倍数为18.29,回收率为44.81%,经SDS-聚丙烯酰胺凝胶电泳后有一条明显的蛋白质谱带。相对分子量为55800左右,该酶的最适pH为6.5,最适温度为30℃,在pH 6.0~8.0之间和45℃以下稳定,Ag+和Cu2+对该酶有较强烈的抑制作用,EDTA和镁离子对酶活的影响较小。
译  名:
Purification and Properties of β-fructofuranosidase from Arthrobacter 10137
作  者:
TONG Qun-yi,ZHU Gui-lan (School of Food Science and Technology, Southern Yangtze University, Wuxi 214036, China)
关键词:
Arthrobacter 10137;β-fructofuranosidase;purification;properties
摘  要:
The crudeβ-fructofuranosidase prepared from Arthrobacter sp. 10137 was fractioned in a sequence of operations including ammonium sulfate fraction, dialysis and column chromatography with Sepharose 6B. Purification of about 18.29 fold was achieved with an overall yield of 44.81%. The pure enzyme showed a single protein band by SDS-PAGE. Its molecular weight was estimated to be about 55800 by SDS-PAGE. The optimum temperature and pH of the enzyme were 30℃ and 6.5 respectively. The enzyme was stable under 45℃ in the range of pH 6.0~8.0. The Ag+ and Cu2+ strongly inhibited β- fructofuranosidase activity, while EDTA and Mg2+ had no significant effect on it.

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