Food proteins as potential carriers for phenolics

M.C. Bohin

Research output: Thesisinternal PhD, WUAcademic

Abstract

The development of phenolic-rich functional foods is often limited by the off-tastes of phenolics that might be counteracted by sequestering these compounds using a carrier, thereby preventing them to interact with bitter taste receptors and salivary proteins. A range of common animal food proteins were tested for binding of phenolics. It appeared that a proline-rich open protein structure, as in β-casein, favored binding of phenolics. Globular proteins other than bovine serum albumin showed poor potential for use as carrier. No appropriate carriers for monomeric phenolics were found. β-Casein and Na-caseinate were shown to have good bitter-masking potential for EGCG, as measured by a maximal reduction in bitter receptor activation of ~93% measured in vitro. This effective reduction in bitter receptor activation was confirmed by a sensory test. This illustrates the validity of using food proteins with good binding properties as carriers for phenolics.

Different methodologies for probing the interaction between proteins and phenolics were developed: (i) ultrafiltration followed by UV quantification of unbound phenolics in the retentate, (ii) fluorescence quenching, and (iii) ultrafiltration followed by mass spectrometric quantification of unbound phenolics in the retentate. The latter method offered the opportunity to analyze preferential binding to protein of individual phenolics present in a complex mixture. With these methods, it was established that, with respect to phenolics, conformation and flexibility were important drivers of protein-phenolic interaction, besides degree of polymerization and galloylation. With respect to relatively proline-poor unstructured proteins such as α-casein and β-casein, it appeared that there should be other factors, besides proline density, explaining the interaction with phenolics.

Original languageEnglish
QualificationDoctor of Philosophy
Awarding Institution
  • Wageningen University
Supervisors/Advisors
  • Gruppen, Harry, Promotor
  • Vincken, Jean-Paul, Co-promotor
Award date25 Oct 2013
Place of PublicationS.l.
Publisher
Print ISBNs9789461736765
Publication statusPublished - 2013

Fingerprint

protein sources
casein
proline
proteins
ultrafiltration
receptors
binding properties
food animals
protein structure
bovine serum albumin
polymerization
functional foods
methodology
fluorescence
testing

Keywords

  • proteins
  • phenolic compounds
  • casein
  • caseinates
  • bitterness
  • interactions

Cite this

Bohin, M. C. (2013). Food proteins as potential carriers for phenolics. S.l.: s.n.
Bohin, M.C.. / Food proteins as potential carriers for phenolics. S.l. : s.n., 2013. 140 p.
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abstract = "The development of phenolic-rich functional foods is often limited by the off-tastes of phenolics that might be counteracted by sequestering these compounds using a carrier, thereby preventing them to interact with bitter taste receptors and salivary proteins. A range of common animal food proteins were tested for binding of phenolics. It appeared that a proline-rich open protein structure, as in β-casein, favored binding of phenolics. Globular proteins other than bovine serum albumin showed poor potential for use as carrier. No appropriate carriers for monomeric phenolics were found. β-Casein and Na-caseinate were shown to have good bitter-masking potential for EGCG, as measured by a maximal reduction in bitter receptor activation of ~93{\%} measured in vitro. This effective reduction in bitter receptor activation was confirmed by a sensory test. This illustrates the validity of using food proteins with good binding properties as carriers for phenolics. Different methodologies for probing the interaction between proteins and phenolics were developed: (i) ultrafiltration followed by UV quantification of unbound phenolics in the retentate, (ii) fluorescence quenching, and (iii) ultrafiltration followed by mass spectrometric quantification of unbound phenolics in the retentate. The latter method offered the opportunity to analyze preferential binding to protein of individual phenolics present in a complex mixture. With these methods, it was established that, with respect to phenolics, conformation and flexibility were important drivers of protein-phenolic interaction, besides degree of polymerization and galloylation. With respect to relatively proline-poor unstructured proteins such as α-casein and β-casein, it appeared that there should be other factors, besides proline density, explaining the interaction with phenolics.",
keywords = "eiwitten, fenolverbindingen, case{\"i}ne, case{\"i}naten, bitterheid, interacties, proteins, phenolic compounds, casein, caseinates, bitterness, interactions",
author = "M.C. Bohin",
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year = "2013",
language = "English",
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}

Bohin, MC 2013, 'Food proteins as potential carriers for phenolics', Doctor of Philosophy, Wageningen University, S.l..

Food proteins as potential carriers for phenolics. / Bohin, M.C.

S.l. : s.n., 2013. 140 p.

Research output: Thesisinternal PhD, WUAcademic

TY - THES

T1 - Food proteins as potential carriers for phenolics

AU - Bohin, M.C.

N1 - WU thesis 5586

PY - 2013

Y1 - 2013

N2 - The development of phenolic-rich functional foods is often limited by the off-tastes of phenolics that might be counteracted by sequestering these compounds using a carrier, thereby preventing them to interact with bitter taste receptors and salivary proteins. A range of common animal food proteins were tested for binding of phenolics. It appeared that a proline-rich open protein structure, as in β-casein, favored binding of phenolics. Globular proteins other than bovine serum albumin showed poor potential for use as carrier. No appropriate carriers for monomeric phenolics were found. β-Casein and Na-caseinate were shown to have good bitter-masking potential for EGCG, as measured by a maximal reduction in bitter receptor activation of ~93% measured in vitro. This effective reduction in bitter receptor activation was confirmed by a sensory test. This illustrates the validity of using food proteins with good binding properties as carriers for phenolics. Different methodologies for probing the interaction between proteins and phenolics were developed: (i) ultrafiltration followed by UV quantification of unbound phenolics in the retentate, (ii) fluorescence quenching, and (iii) ultrafiltration followed by mass spectrometric quantification of unbound phenolics in the retentate. The latter method offered the opportunity to analyze preferential binding to protein of individual phenolics present in a complex mixture. With these methods, it was established that, with respect to phenolics, conformation and flexibility were important drivers of protein-phenolic interaction, besides degree of polymerization and galloylation. With respect to relatively proline-poor unstructured proteins such as α-casein and β-casein, it appeared that there should be other factors, besides proline density, explaining the interaction with phenolics.

AB - The development of phenolic-rich functional foods is often limited by the off-tastes of phenolics that might be counteracted by sequestering these compounds using a carrier, thereby preventing them to interact with bitter taste receptors and salivary proteins. A range of common animal food proteins were tested for binding of phenolics. It appeared that a proline-rich open protein structure, as in β-casein, favored binding of phenolics. Globular proteins other than bovine serum albumin showed poor potential for use as carrier. No appropriate carriers for monomeric phenolics were found. β-Casein and Na-caseinate were shown to have good bitter-masking potential for EGCG, as measured by a maximal reduction in bitter receptor activation of ~93% measured in vitro. This effective reduction in bitter receptor activation was confirmed by a sensory test. This illustrates the validity of using food proteins with good binding properties as carriers for phenolics. Different methodologies for probing the interaction between proteins and phenolics were developed: (i) ultrafiltration followed by UV quantification of unbound phenolics in the retentate, (ii) fluorescence quenching, and (iii) ultrafiltration followed by mass spectrometric quantification of unbound phenolics in the retentate. The latter method offered the opportunity to analyze preferential binding to protein of individual phenolics present in a complex mixture. With these methods, it was established that, with respect to phenolics, conformation and flexibility were important drivers of protein-phenolic interaction, besides degree of polymerization and galloylation. With respect to relatively proline-poor unstructured proteins such as α-casein and β-casein, it appeared that there should be other factors, besides proline density, explaining the interaction with phenolics.

KW - eiwitten

KW - fenolverbindingen

KW - caseïne

KW - caseïnaten

KW - bitterheid

KW - interacties

KW - proteins

KW - phenolic compounds

KW - casein

KW - caseinates

KW - bitterness

KW - interactions

M3 - internal PhD, WU

SN - 9789461736765

PB - s.n.

CY - S.l.

ER -

Bohin MC. Food proteins as potential carriers for phenolics. S.l.: s.n., 2013. 140 p.