Egg White Lysozyme Purification by Ultrafiltration and Affinity Chromatography

摘要

ABSTRACTIsolation 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 recover