An improved process for the production of highly purified recombinant thaumatin tagged-variants.
Identifieur interne : 000080 ( Main/Curation ); précédent : 000079; suivant : 000081An improved process for the production of highly purified recombinant thaumatin tagged-variants.
Auteurs : Robert D. Healey [Australie] ; Helene Lebhar [Australie] ; Simon Hornung [Australie] ; Pall Thordarson [Australie] ; Christopher P. Marquis [Australie]Source :
- Food chemistry [ 1873-7072 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Protéines végétales.
- Marantaceae, Pichia, Spectrométrie de masse en tandem, Édulcorants.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plant Proteins.
- Marantaceae, Pichia, Sweetening Agents, Tandem Mass Spectrometry.
Abstract
The sweetest tasting molecule known is the protein thaumatin, first isolated from the katemfe fruit, Thaumatococcus daniellii. Thaumatin is used in the food and beverage industry as a low-calorie sugar substitute. Thaumatin interacts with taste receptors in the oral cavity eliciting a persistent sweet taste and a bitter, liquorice flavor. Recombinant thaumatin was expressed in Pichia pastoris and through a co-expression strategy with a molecular chaperone, yields of one engineered thaumatin variant increased by greater than two-fold. A detailed purification strategy for thaumatin is reported resulting in a homogenous sample recovered at a yield of 42%. The recombinant thaumatins were extensively characterised using size exclusion chromatography for homogeneity, reversed-phase HPLC for purity (99%), peptide digest LC-MS/MS for sequence determination, and circular dichroism and tryptophan fluorescence spectroscopies for conformational characterisation. These new thaumatin variants are amenable for bioconjugation, providing chemical biology tools for thaumatin:taste receptor interaction studies.
DOI: 10.1016/j.foodchem.2017.06.018
PubMed: 28764073
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pubmed:28764073Le document en format XML
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<front><div type="abstract" xml:lang="en">The sweetest tasting molecule known is the protein thaumatin, first isolated from the katemfe fruit, Thaumatococcus daniellii. Thaumatin is used in the food and beverage industry as a low-calorie sugar substitute. Thaumatin interacts with taste receptors in the oral cavity eliciting a persistent sweet taste and a bitter, liquorice flavor. Recombinant thaumatin was expressed in Pichia pastoris and through a co-expression strategy with a molecular chaperone, yields of one engineered thaumatin variant increased by greater than two-fold. A detailed purification strategy for thaumatin is reported resulting in a homogenous sample recovered at a yield of 42%. The recombinant thaumatins were extensively characterised using size exclusion chromatography for homogeneity, reversed-phase HPLC for purity (99%), peptide digest LC-MS/MS for sequence determination, and circular dichroism and tryptophan fluorescence spectroscopies for conformational characterisation. These new thaumatin variants are amenable for bioconjugation, providing chemical biology tools for thaumatin:taste receptor interaction studies.</div>
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<Abstract><AbstractText>The sweetest tasting molecule known is the protein thaumatin, first isolated from the katemfe fruit, Thaumatococcus daniellii. Thaumatin is used in the food and beverage industry as a low-calorie sugar substitute. Thaumatin interacts with taste receptors in the oral cavity eliciting a persistent sweet taste and a bitter, liquorice flavor. Recombinant thaumatin was expressed in Pichia pastoris and through a co-expression strategy with a molecular chaperone, yields of one engineered thaumatin variant increased by greater than two-fold. A detailed purification strategy for thaumatin is reported resulting in a homogenous sample recovered at a yield of 42%. The recombinant thaumatins were extensively characterised using size exclusion chromatography for homogeneity, reversed-phase HPLC for purity (99%), peptide digest LC-MS/MS for sequence determination, and circular dichroism and tryptophan fluorescence spectroscopies for conformational characterisation. These new thaumatin variants are amenable for bioconjugation, providing chemical biology tools for thaumatin:taste receptor interaction studies.</AbstractText>
<CopyrightInformation>Copyright © 2017 Elsevier Ltd. All rights reserved.</CopyrightInformation>
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