Evaluation of biological activities, structural and conformational properties of bovine beta- and alpha-trypsin isoforms in aqueous-organic media

The study of the biological activity of trypsin isoforms in aqueous-organic media is of great interest to various fields of knowledge and biochemistry applications. Thus enzymatic, structural, and energetic properties of bovine beta- and alpha-trypsin isoforms were compared in aqueous-organic media using 30 mg of each isoform. The results showed that the changes induced on the structure and activity of the same trypsin isoform occur at different concentrations. Better results for activity (ionic strength of 0.11 mol.L-1, at 37 degrees C and pH 8.0) were found in 0-40% of ethanolic media in which the activity for beta-trypsin was about 60% higher than.-trypsin. The ethanolic system does not cause significant changes in the level of secondary structure but the beta-trypsin isoform undergoes a major rearrangement. The use of until 60% (v/v) ethanol showed that beta-trypsin presents a denaturation process 17% more cooperative. The organic solvent causes redistribution in the supramolecular arrangement of both isoforms: all concentrations used induced the beta-trypsin molecules to rearrange into agglomerates. The alpha-trypsin rearranges into agglomerates up to 60% (v/v) of ethanol and aggregates at 80% (v/v) of ethanol. Both isoforms keep the enzymatic activity up to 60% (v/v) of ethanol. (c) 2021 Elsevier B.V. All rights reserved.

Automated summary

The study compared the enzymatic, structural, and energetic properties of bovine beta- and alpha-trypsin isoforms in aqueous-organic media, showing that the changes induced on the structure and activity of the same trypsin isoform occur at different concentrations. Better activity results were found for beta-trypsin in ethanolic media, with activity about 60% higher than alpha-trypsin.