Abstract
Abstract A new dye affinity adsorbent was prepared by modifying glutaraldehyde-crosslinked waste beer yeast with Cibacron B1ue F-3GA. The amount of immobilized Cibacron Blue F-3GA on the crosslinked yeasts was 161.1 mg g−1. The effects of contact time, initial lysozyme concentration, medium pH, and ionic strength on the adsorption of lysozyme on modified yeasts were studied. The dye affinity adsorbents were used for purification of lysozyme from chicken egg white. The lysozyme adsorption capacity of the modified yeast was 229.1 mg g−1, and its adsorption performance was better than the unmodified yeast. The high desorption ratio (89.1%) was achieved by using 1.0 mM NaSCN as eluent, and the ratio of activity-preserving was 91.0%. In the extraction of lysozyme from chicken egg white, the purification fold was 26.7 and average recovery of enzyme activity was 73.5%. The adsorbents could be reused without significant decreases in the adsorption capacities.
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