Add time:08/07/2019         Source:sciencedirect.com

The change in structure, function of proteinase K in the presence of MALTOSE (cas 16984-36-4) was studied using spectroscopic and computational techniques. UV–Vis spectroscopy results reveal with the addition of maltose, the peaks of proteinase K didn't show any shifts. The intrinsic fluorescence intensity was decreased regularly with rising the ligand concentration. These results suggest that the quenching mode is dynamic quenching. Far-UV circular dichroism (CD) studies showed a low decrease in the β-sheet, β-turn and the large increase in the α-helix. The activity of proteinase K was increased in the presence of maltose. Thus, maltose is an activator for proteinase K. Molecular docking results show a negative value for the Gibbs free energy. On the other hand, the thermal stability of proteinase K was investigated in the presence of maltose over the temperature range (298–353) K. Obtained data indicate the thermal stability of proteinase K will be reduced when the concentration of maltose increase. These results are confirmed by the molecular dynamic simulation technique.

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