ADSORPTION OF PROTEASES ON NOVEL LIGNIN DERIVATIVES

摘要

Lignin derivatives, HBS-lignophenol and EH-lignin aminophenol, were prepared in this article, which could be used as adsorbents for enzyme immobilization. The chemical structure and the content of functional groups of these derivatives were then characterized by FT-IR. The adsorption of three proteases (papain, trypsin and pepsin) on lignin and lignin derivatives were investigated regarding the adsorption capacity and activity recovery as well as the influence of adsorption time and pH value on the adsorption capacity. Results showed that lignin and lignin derivatives were able to adsorb these proteases effectively and the adsorption capacity of HBS-lignophenol and EH-lignin aminophenol was higher than that of HBS lignin. The activity recovery of papain and pepsin adsorbed on lignin derivatives under acid and neutral conditions was very high, which may indicate a supramolecular interaction between enzymes and lignin derivatives that has little side-effect on enzyme activity. Meanwhile, the activity recovery of trypsin was extremely low under alkaline condition. Therefore, HBS-lignophenol and EH-lignin aminophenol are promising adsorbents for enzyme immobilization under acid and neutral conditions.