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. 1991 Feb 15;274(Pt 1):231–236. doi: 10.1042/bj2740231

Purification and characterization of thaumatopain, a cysteine protease from the arils of the plant Thaumatococcus daniellii.

M Cusack 1, A G Stephen 1, R Powls 1, R J Beynon 1
PMCID: PMC1149942  PMID: 2001238

Abstract

Aqueous extracts of the aril of the seed of Thaumatococcus daniellii contain, in addition to the intensely sweet protein thaumatin, a cysteine protease that we have termed thaumatopain. Thaumatopain has been purified by ion-exchange chromatography from arils, and is a monomeric protein of Mr 30,000. The protease strongly resembles papain in proteolytic activity, pH optima, susceptibility to inhibitors of cysteine proteases and in N-terminal sequence. The protease has also been identified in crude aril extracts by affinity labelling with iodo[14C]acetate. Thaumatopain is responsible for the cysteine protease activity previously attributed to thaumatin. Thaumatin is digested by thaumatopain at neutral to alkaline pH values.

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