NOVEL IMMOBILIZATION OF ENZYME IN MOLECULAR ASSEMBLY OF NONIONIC SURFACTANT ADSORBED ON SILICA-GEL

As a novel procedure to immobilize enzymes, lysozyme was dissolved in the molecular assembly of the nonionic surfactant Triton X-100 adsorbe d on silica gel. The adsorption isotherms of Triton X-100 on silica ge l, and of lysozyme in the molecular assembly of adsorbed Triton X-100 on silica gel, were obtained. The isotherms for the latter are signifi cantly influenced by pH and buffering agents, while the isotherms for the former are not. Moreover, the adsorption of lysozyme was affected by the ionic strength of the buffering agents. Leakage of immobilized lysozyme is influenced by pH and temperature; it is found that much ly sozyme leaked when pH and temperature were low. However, under limited conditions the immobilized enzyme is very stable. The immobilized lys ozyme was used in the enzymatic hydrolysis reaction of the water-solub le chitin derivative glycol chitin. The enzymatic reaction obeys the M ichaelis-Menten mechanism and the values of kinetic parameter, Michael is constant K-m and maximum velocity V-max, are estimated. The apparen t activation energy E-a is also obtained.