节杆菌β-呋喃果糖苷酶的纯化及性质研究  

Purification and Properties of β-fructofuranosidase from Arthrobacter 10137

作　　者：童群义[1] 朱桂兰[1] 

机构地区：[1]江南大学食品学院,江苏无锡214036

出　　处：《食品科学》2004年第12期121-124,共4页Food Science

摘　　要：采用硫酸铵盐析、透析脱盐、Sepharose6B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pH6.0～8.0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。The crudeβ -fructofuranosidase preparation from Arthrobacter sp. 10137 was fractioned in a sequence of operation 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℃ and in the range of pH 6.0～8.0. The Ag+ and Cu2+ was strongly inhibited β - fructofuranosidase activity, while EDTA and Mg2+ had no significant effect on it.

关 键 词：节杆菌 Β-呋喃果糖苷酶 纯化 性质 

分 类 号：Q55[生物学—生物化学]