Advances in Enzyme Research

Volume 4, Issue 1 (March 2016)

ISSN Print: 2328-4846   ISSN Online: 2328-4854

Google-based Impact Factor: 1.67  Citations  

Optima of Trypsin-Catalyzed Hydrolysis and Its Inhibition Determined by SDS-PAGE

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DOI: 10.4236/aer.2016.41001    2,429 Downloads   3,110 Views   Citations

ABSTRACT

SDS-PAGE was applied to determine trypsin activity and inhibition. After the hydrolysis by trypsin to substrate bovine serum albulnin (BSA) under different temperatures and pH, the hydrolysis degree of BSA was conducted using SDS-PAGE. From the quantitative analysis to the electrophoresis bands of BSA and its hydrolysis products in SDS-PAGE pattern, the change of trypsin activity was determined, and then the optimum temperature at 40°C and the optimum pH at pH 8.5 - 8.7 for trypsin activity were obtained. All the target bonds in BSA molecule could be hydrolyzed at the same time by trypsin. The inhibition was due to the binding of inhibitor to trypsin, which made it impossible for trypsin to touch the substrate protein. SDS-PAGE was demonstrated to be also an effect method for assaying the characteristics of trypsin activity and its inhibition.

Cite this paper

Zhou, X. , Wang, T. , Wang, A. and Li, R. (2016) Optima of Trypsin-Catalyzed Hydrolysis and Its Inhibition Determined by SDS-PAGE. Advances in Enzyme Research, 4, 1-6. doi: 10.4236/aer.2016.41001.

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