文献类型：期刊文献

英文题名：Immobilization of β-Galactosidase onto Magnetic Beads

作者：Zhang, Shengtang[1];Gao, Sufang[2];Gao, Guoqiang[1]

第一作者：Zhang, Shengtang

通信作者：Gao, GQ[1]

机构：[1]Lanzhou Ind Res Inst, Lanzhou 730050, Gansu, Peoples R China;[2]Gansu Coll Tradit Chinese Med, Lanzhou 730000, Peoples R China

第一机构：Lanzhou Ind Res Inst, Lanzhou 730050, Gansu, Peoples R China

通信机构：[1]corresponding author), Lanzhou Ind Res Inst, Lanzhou 730050, Gansu, Peoples R China.

年份：2010

卷号：160

期号：5

起止页码：1386

外文期刊名：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY

收录：;EI(收录号：20101112767943);Scopus(收录号：2-s2.0-77949277214);WOS:【SCI-EXPANDED(收录号:WOS:000274398500012)】；

语种：英文

外文关键词：Magnetic beads; beta-galactosidase; Enzyme immobilization; Properties

摘要：A study of the cross-linking of beta-galactosidase on magnetic beads is reported here. The magnetic beads were prepared from artemisia seed gum, chitosan, and magnetic fluid in the presence of a cross-linking regent (i.e., glutaraldehyde). The reactive aldehyde groups of the magnetic beads allowed the reaction of the amino groups of the enzymes. The animated magnetic beads were used for the covalent immobilization of beta-galactosidase. The effect of various preparation conditions on the activity of the immobilized beta-galactosidase, such as immobilizing time, amount of enzyme, and the concentration of glutaraldehyde, were investigated. The influence of pH and temperature on the activity and the stability of the enzyme, both free and immobilized, have been studied. And o-nitrophenyl-beta-d-galactopyranoside (ONPG) was chosen as a substrate. The beta-galactosidase immobilized on the magnetic beads resulted in an increase in enzyme stability. Optimum operational temperature for immobilized enzyme was 10 A degrees C higher than that of free enzyme and was significantly broader.