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Egg White Lysozyme Purification by Ultrafiltration and Affinity Chromatography
Author(s) -
CHIANG B. H.,
SU C. K.,
TSAI G. J.,
TSAO G. T.
Publication year - 1993
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1993.tb04261.x
Subject(s) - diafiltration , lysozyme , chromatography , chemistry , ultrafiltration (renal) , egg white , chitin , affinity chromatography , specific activity , membrane , gel permeation chromatography , biochemistry , enzyme , chitosan , microfiltration , organic chemistry , polymer
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%.