EGG-WHITE LYSOZYME PURIFICATION BY ULTRAFILTRATION AND AFFINITY-CHROMATOGRAPHY

被引：20

作者：

CHIANG, BH ^{[1
]}

SU, CK ^{[1
]}

TSAI, GJ ^{[1
]}

TSAO, GT ^{[1
]}

机构：

[1] PURDUE UNIV, RENEWABLE RESOURCES ENGN LAB, W LAFAYETTE, IN 47907 USA

来源：

JOURNAL OF FOOD SCIENCE | 1993年 / 58卷 / 02期

关键词：

EGG WHITES; LYSOZYME; PURIFICATION; AFFINITY CHROMATOGRAPHY;

D O I：

10.1111/j.1365-2621.1993.tb04261.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Isolation and purification of lysozyme from hen egg white was studied using a two-step procedure. The egg white was diluted 5- to 9-fold with sodium phosphate buffer, and then processed by sequential dilution diafiltration using a UF membrane (molecular weight cut-off 300,000 dalton). The membrane process increased the specific activity of lysozyme 6-fold, and recovered 96% of lysozyme activity. The permeate from diafiltration was further purified by affinity chromatography using chitin as adsorbent. The second step of the process yielded a product of specific activity of 70,400 units/mg protein. The overall lysozyme recovery was 79%.

引用

页码：303 / 306

页数：4