Egg White Lysozyme Purification by Ultrafiltration and Affinity Chromatography
Journal
Journal of Food Science
Journal Volume
58
Journal Issue
2
Pages
303-306
Date Issued
1993
Author(s)
Abstract
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%. Copyright ? 1993, Wiley Blackwell. All rights reserved
Subjects
affinity chromotography
egg whites
lysozyrne
purification
Type
journal article