Comparison of physicochemical properties of recombinant buckwheat trypsin inhibitor (rBTI) and soybean trypsin inhibitor (SBTI).

Protein Expr Purif

Department of Food Science and Agricultural Chemistry, McGill University (Macdonald Campus), Ste-Anne-de-Bellevue, Québec, H9X 3V9, Canada. Electronic address:

Published: July 2020

The inhibitory activities of buckwheat trypsin inhibitor (rBTI) towards trypsin were compared with soybean trypsin inhibitor (SBTI) in terms of their sensitivities to temperature, pH, salt ions and organic solvents. Both rBTI and SBTI were stable over a broad pH range of 2.0-12.0. rBTI exhibited higher thermal stability than SBTI. The inhibitory activity of rBTI was decreased by Zinc ions (Zn), KSCN, vitamin C and urea, while that of SBTI remained unchanged. However, HO, Mg and Cu ions had no significant effects on the inhibitory activities of rBTI and SBTI. Acetonitrile enhanced the inhibitory activity of rBTI, but had no effect on SBTI, while dimethylacetamide (DMAC) increased the inhibitory effect of both rBTI and SBTI. On the contrary, the inhibitory activities of rBTI and SBTI were reduced by isopropyl alcohol and methanol. The inhibition constants K of rBTI and SBTI were calculated to be 7.41 × 10 M and 6.52 × 10 M, respectively.

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http://dx.doi.org/10.1016/j.pep.2020.105614DOI Listing

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Comparison of physicochemical properties of recombinant buckwheat trypsin inhibitor (rBTI) and soybean trypsin inhibitor (SBTI).

Protein Expr Purif

July 2020

Department of Food Science and Agricultural Chemistry, McGill University (Macdonald Campus), Ste-Anne-de-Bellevue, Québec, H9X 3V9, Canada. Electronic address:

The inhibitory activities of buckwheat trypsin inhibitor (rBTI) towards trypsin were compared with soybean trypsin inhibitor (SBTI) in terms of their sensitivities to temperature, pH, salt ions and organic solvents. Both rBTI and SBTI were stable over a broad pH range of 2.0-12.

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