Abstract
Human lysozyme and hen egg-white lysozyme have numerous applications due to their antibacterial, antiviral, and antifungal properties. Currently, hen egg-white lysozyme dominates low cost applications but the recent high-level expression of human lysozyme in rice could provide an economical source of lysozyme if purification costs are comparable. This paper evaluates human lysozyme and hen egg-white lysozyme adsorption to the cation exchange resin, SP-Sepharose FF, and the effect of rice extract on lysozyme purification. The dynamic binding capacities of human lysozyme were lower than those of hen egg-white at pH 4.5, 6, and 7.5 with ionic strengths from 0 to 100 mM (5-20 mS). Ionic strength and pH had similar effects on the capacities, but human lysozyme was more sensitive to these factors than hen egg-white lysozyme. At pH 4.5 and in the presence of rice extract, the dynamic binding capacities were reduced 20-30%. Therefore, it appears that the different physico-chemical properties of human lysozyme and hen egg-white lysozyme are the major contributors to the inferior binding ability of human lysozyme from rice.
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