Studies on the maturation of glutamine transaminase modified by protease

Abstract

Glutamine transaminase (glutamine transaminase) is a kind of enzyme that exists widely in many organisms. Its main function is to catalyze covalent cross-linking of proteins within or between molecules. And has development prospects in many fields. In order to promote the modification and maturation of glutamine transaminase, we selected a neutral protease from a variety of proteases at the initial stage of the experiment. This protease has stronger activity and better promotion effect on glutamine transaminase compared with other proteases. Therefore, we immobilized the neutral protease to realize the efficient maturation of glutamine transaminase.2 Later, we calculated the specific improvement of glutamine transaminase by neutral protease, and set the control experiment variable as whether neutral protease was added or not. The results showed that the enzyme activity of the group with neutral protease was about 75% higher than that of the group without neutral protease. Neutral proteases exhibit high activity in neutral to weakly alkaline environments, with an optimal pH operating range of 6.5 to 8.0. The optimum temperature is 50℃ to 60℃. The incubation pH needs to reach pH8 to reach the optimal pH, and the incubation temperature needs to be maintained at about 30℃. Then, the immobilized neutral protease was compared with the free neutral protease, and it was found that the immobilized protease was significantly better than the unfixed group when incubated at pH 5 for 60 minutes. Immobilization improves thermal stability and pH stability. Immobilization significantly improved the thermal stability and pH stability of neutral protease. Finally, the reusability analysis of neutral protease was carried out, and the results showed that the immobilized enzyme had adaptability