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Article

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

Citation
Cusack M, Stephen AG, Powls R & Beynon R (1991) Purification and characterization of thaumatopain, a cysteine protease from the arils of the plant Thaumatococcus daniellii. Biochemical Journal, 274 (1), pp. 231-236. https://doi.org/10.1042/bj2740231

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 M(r) 30000. 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.

Journal
Biochemical Journal: Volume 274, Issue 1

StatusPublished
Author(s)Cusack, Maggie; Stephen, Andrew G; Powls, Roy; Beynon, Robert
Publication date28/02/1991
Publication date online15/02/1991
URLhttp://hdl.handle.net/1893/24985
PublisherPortland Press
ISSN0264-6021
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