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SPR based Studies for Pentagalloyl Glucose Binding to α-Amylase

dc.contributor.authorGuerreiro, J. Rafaela L.
dc.contributor.authorSutherland, Duncan S.
dc.contributor.authorFreitas, Victor De
dc.contributor.authorSales, M. Goreti F.
dc.date.accessioned2015-10-19T12:44:49Z
dc.date.available2015-10-19T12:44:49Z
dc.date.issued2012
dc.description.abstractAstringency is an organoleptic property resulting mostly from the interaction of salivary proteins with dietary polyphenols. It is of great importance to consumers but being typically measured by sensorial panels it turns out subjective and expensive. The main goal of the present work is to develop a sensory system to estimate astringency relying on protein/polyphenol interactions. For this purpose, a model protein was immobilized on a sensory gold surface and its subsequent interaction with polyphenols was measured by Surface Plasma Resonance (SPR). α-amylase and pentagalloyl glucose (PGG) were selected as model protein and polyphenol, respectively. To ensure specific binding between these, various surface chemistries were tested. Carboxylic terminated thiol decreased the binding ability of PGG and allowed covalent attachment of α-amylase to the surface. The pH 5 was the optimal condition for α-amylase immobilization on the surface. Further studies focus on Localized SPR sensor and application to wine samples, providing objectivity when compared to a trained panel.pt_PT
dc.identifier.doi10.1016/j.proeng.2012.09.193
dc.identifier.urihttp://hdl.handle.net/10400.22/6745
dc.language.isoengpt_PT
dc.publisherElsevierpt_PT
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S1877705812042567pt_PT
dc.subjectSPRpt_PT
dc.subjectD-Amylasept_PT
dc.subjectPGGpt_PT
dc.subjectastringencypt_PT
dc.titleSPR based Studies for Pentagalloyl Glucose Binding to α-Amylasept_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage501pt_PT
oaire.citation.startPage498pt_PT
oaire.citation.titleProcedia Engineeringpt_PT
oaire.citation.volume47pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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