Immobilization of ß-galaktosidase on different carriers and investigation of some properties

The galactosidases are well-known class of the exoglicosidases. According to the effect to the kind of ?- or ß- of glycosidic bond the galactosidases divide in two subclass as ß- galactosidases and ?- galactosidases. Not only the ß-galactosidase hydrolase the oligo-sacckarids which containe ß-D galactosyl groups but also it is a glicosidase which shows the activity of transferase by carrying the galactosyl moieties from a molecule to another ß- galactosidase is used in the industry for hydrolysis of milk, getting the productions of lactose free milk, manufacturing the ice-cream, hydrolysis of whey and the practises in animal nutrition.In this study, the partial purification of ß- galactosidase than the fungus of Hypocrea jecorina was done. For the first time, the ß- galactosidase of H. jecorina was immobilized by the methods of adsorption by linking to various carriers. Carriers used in this study; chitosan beads, chitosan beads which contains PEG 6000, amberlite-XAD16, bentonite, sea sand, silica, hydoxy apatite, celite, alumina. The proper method for the immobilization of the ß-galactosidase of H. jecorina was chosen. Later on, the optimum pH, the optimum temperature, thermal stability, of Km and Vmax values of the immobilized enzyme were determined. It is examined the effect of various ions and compounds on immobilized ß-galactosidase by using the immobilization method which was chosen for labour characterization. Storage stability of the immobilized enzyme were determined.As a result of the study, the proper method for immobilization of the ß-galactosidase of H. jecorina were emerged as: the adsorption of chitosan beads. According to the adsorption method, the characteristics of the immobilized ß-galactosidase are found as the following; the optimum pH is 8, the optimum temperature is 80?C, the Km value is 1,026.10-3 g/ml, the Vmax value is 0,1447 U/ml. Storage stability was found to be 50 days. Co+2, Cu+2, Ag+ ions and surface active-agent triton X-100 activity of immobilized enzyme was found to increase by over 100%.