PMID: 6988215Mar 1, 1980Paper

Enzymatic properties of the sweet-tasting proteins thaumatin and monellin after partial reduction

European Journal of Biochemistry
H van der Wel, W J Bel

Abstract

After partial reduction of disulfide bonds in the thaumatins, the sweet-tasting proteins from the fruits of Thaumatococcus danielii Benth, a rapid autodigestion was demonstrated. In the presence of suitable substrates, the reduced thaumatins showed protease, amidase and esterase activity. Thiol-blocking reagents like mercury(II) chloride inhibited the enzymatic activity. Of the thaumatins b, c, I, II and III (with increasing isoelectric points), thaumatin I showed the lowest enzymatic activity. In this series, the enzymatic activity increased from thaumatin I to thaumatin III as well as from thaumatin I to thaumatin b. Acetylation of the epsilon-amino group of lysine residues in the thaumatins by acetic anhydride, causing a decrease in basicity, led to an increase in enzymatic activity, which is correlated with the number of acetyl groups introduced. Comparison of the amino acid sequence of thaumatin I with that of cysteine proteases of plant origin showed no similarities. Moreover, the thaumatins lack histidine, one of the amino acids in the active site of the cysteine proteases. Monellin, the sweet-tasting protein from the fruits of Dioscoreophyllum cumminsii Diels, is not enzymatically active. However, when monellin with ace...Continue Reading

References

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Citations

Jan 1, 1992·Critical Reviews in Food Science and Nutrition·Y Kurihara
Nov 20, 2002·Molecular Plant-microbe Interactions : MPMI·Reza ZareiePeter J Murphy
Oct 1, 1984·European Journal of Biochemistry·H van der WelF J van der Ouderaa
Dec 5, 1992·Journal of Molecular Biology·C M OgataS H Kim
Apr 5, 1990·Nature·R Beynon, M Cusack
Apr 5, 2020·Genes·Magdalena Ewa PawełkowiczWojciech Pląder
Jul 30, 2009·The Journal of Organic Chemistry·Preeti SejwalYan-Yeung Luk

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