Chaiet L, Kempf A J, Harman R, Kaczka E, Weston R, Nollstadt K, Wolf F J
Appl Microbiol. 1970 Sep;20(3):421-6. doi: 10.1128/am.20.3.421-426.1970.
A dextranase, produced by Penicillium funiculosum, was purified 1,000-fold to yield the enzyme which was demonstrated by gel electrophoresis and electrofocusing to be a homogeneous protein. The purification method included acetone partition, ammonium sulfate fractionation, gel filtration, iron defecation and precipitation, and diethylaminoethyl-cellulose chromatography. The pure enzyme was also obtained by preparative gel electrophoresis. Gel-permeation chromatography indicates a molecular weight of 41,000. An isoelectric pH of 4.6 was established by electrofocusing. A 1-mg amount of the enzyme hydrolyzes a dextran substrate to yield 27,000 isomaltose reducing units in 2 hr.
绳状青霉产生的一种葡聚糖酶经纯化1000倍后得到该酶，通过凝胶电泳和等电聚焦证明其为一种均一蛋白质。纯化方法包括丙酮分配、硫酸铵分级分离、凝胶过滤、铁盐澄清沉淀以及二乙氨基乙基纤维素色谱法。通过制备型凝胶电泳也获得了纯酶。凝胶渗透色谱法表明其分子量为41,000。通过等电聚焦确定等电点pH为4.6。1毫克该酶在2小时内可水解葡聚糖底物产生27,000个异麦芽糖还原单位。
