Study On Surface Microanalysis Of The Activity Of Immobilized Enzyme

Enzyme immobilization was considered as one of very promising biotechnology, immobilized enzyme has been widely employed in the biochemistry, biotechnology, bioengineering, biomedical engineering and so on, it would play an important part in the sustainable development of human of society. So, to prepare carriers possessing higher activity, is very important. Therefore, a method of locating the active site of immobilized enzyme including papain, L-asparaginase, lactate dehydrogenase and lipase, was studied by X-ray microanalysis firstly. Reagent capturing site of enzyme activity were chosen respectively. Moreover, the relationship between immobilized enzyme activity and the structure of carriers, was indicated. Our experiment results show that the immoblization effect of immobilized enzyme determined only by observing its micrographs, is not accurate, and the X-ray microanalysis proposed by our present work is effective. The carriers with different structure were synthesized by radical suspension polymerization and immobilized enzyme prepared by different methods. Papain and L-asparaginase were immobilized with the macroporous resin microbeads synthesized by a new method. Meantime, their properties were characterized, studied, and their activity obtained by different immoblization method was compared, characters was studied and compared. The plug- flow reactor was established to hydrolyze casein with this immobilized papain; its hydrolysis ability was satisfying, which indicates that this immobilized papain is promising.