Different structural behaviors evidenced in thaumatin-like proteins: a spectroscopic study.
作者： F. Secundo , E. Di Stasio , B. Giardina , A. Vitali , F. Perri
DOI: 10.1007/S10930-007-9103-2
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摘要: Three proteins belonging to the thaumatin-like family were compared in this study from a structural point of view: zeamatin, new recently isolated PR-5 Cassia didymobotrya and commercial sweet-thaumatin. The former two possess antifungal activities while thaumatin is well known be natural sweetener. Intrinsic fluorescence studies have evidenced that three behave differently unfolding experiments showing different rigidity. All are more stable at slight acidic buffers, but sweet-thaumatin has major tendency destructurate itself. Similar observations made circular dichroism where dependence relationship pH solvent used confirmed hierarchic scale stability for proteins. These differences should considered significant functional role.
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