Purification of lysozyme using ultrafiltration
2000; Wiley; Volume: 68; Issue: 2 Linguagem: Inglês
10.1002/(sici)1097-0290(20000420)68
ISSN1097-0290
Autores Tópico(s)Enzyme Production and Characterization
ResumoThis article examines the separation of lysozyme from chicken egg white by ultrafiltration with 25 kDa and 50 kDa MWCO polysulfone membranes. The effects of pH, system hydrodynamics, feed concentration, and transmembrane pressure on permeate flux, lysozyme transmission, purification factor, and productivity have been discussed. With both types of membranes, higher permeate flux and lysozyme transmission were observed at higher pH. Higher lysozyme purity was generally obtained with the 25 kDa MWCO membrane. Purity of lysozyme decreased when the feed concentration was increased. With the 50 kDa MWCO membrane permeate flux, productivity and the purity of lysozyme were found to increase with increase in transmembrane pressure. The possibility of using a two-step ultrafiltration process for achieving high productivity along with high purity of lysozyme was also investigated. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 68: 191–203, 2000.
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