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GrainGenes Reference Report: TPJ-19-473

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Reference	TPJ-19-473
Title	Some thaumatin-like proteins hydrolyse polymeric beta-1,3-glucans
Journal	The Plant Journal
Year	1999
Volume	19
Pages	473-480
Author	Grenier J Potvin C Trudel J Asselin A
Abstract	Thaumatin and 12 purified thaumatin-like (TL) proteins were surveyed for their capacity to hydrolyse beta-1,3-glucans by using an in-gel glucanase assay Six TL proteins identified by N-terminal amino acid microsequencing were found to be active on carboxymethyl(CM)-pachyman: a barley leaf stress-related permatin, two tomato fruit osmotins, a cherry fruit and two tobacco stigma proteins TL enzymes ranged in specific activity from 0.07 to 89 nkat mg(-1) with CM-pachyman as substrate Hydrolytic activities were not restricted to TL proteins strongly binding to water-insoluble beta-1,3-glucans since the two osmotins were active without tight binding to pachyman Some TL proteins hydrolysed crude fungal walls and one barley TL enzyme even lysed fungal spores No activity was observed on laminarin in the in-gel hydrolase assay. Thin-layer chromatography revealed that the six enzymes acted as endo-beta-1,3-glucanases leading to the formation of various oligoglucosides. Thus far, the TL enzymes (EC 3.2..1.x) appeared different from the well-known beta-1,3-glucanases (EC 3.2.1.39). No activity was found with thaumatin, zeamatin, tobacco leaf PR-R protein and four stress-related TL proteins from barley and pea. This is the first demonstration that diverse TL proteins are enzymatically active. The functions of some TL proteins must be reassessed because they display endo-beta-1,3-glucanase activity on polymeric beta-1,3-glucans.
Keyword	[ Hide all but 1 of 19 ] amino acid sequence beta-glucan beta-glucanase enzyme activity fruits hordeum vulgare hydrolysis leaves lycopersicon-esculentum nicotiana tabacum o-glycoside-hydrolases pisum sativum plant pathogenic-fungi plant proteins prunus-avium saccharomyces cerevisiae stigma substrate zea mays

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