Characterisation of protein-polyphenol interactions in beer during forced aging

Research output: Contribution to journalJournal articlepeer-review

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Characterisation of protein-polyphenol interactions in beer during forced aging. / Jongberg, Sisse; Andersen, Mogens L.; Lund, Marianne N.

In: Journal of the Institute of Brewing, Vol. 126, No. 4, 2020, p. 371-381.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Jongberg, S, Andersen, ML & Lund, MN 2020, 'Characterisation of protein-polyphenol interactions in beer during forced aging', Journal of the Institute of Brewing, vol. 126, no. 4, pp. 371-381. https://doi.org/10.1002/jib.623

APA

Jongberg, S., Andersen, M. L., & Lund, M. N. (2020). Characterisation of protein-polyphenol interactions in beer during forced aging. Journal of the Institute of Brewing, 126(4), 371-381. https://doi.org/10.1002/jib.623

Vancouver

Jongberg S, Andersen ML, Lund MN. Characterisation of protein-polyphenol interactions in beer during forced aging. Journal of the Institute of Brewing. 2020;126(4):371-381. https://doi.org/10.1002/jib.623

Author

Jongberg, Sisse ; Andersen, Mogens L. ; Lund, Marianne N. / Characterisation of protein-polyphenol interactions in beer during forced aging. In: Journal of the Institute of Brewing. 2020 ; Vol. 126, No. 4. pp. 371-381.

Bibtex

@article{05029336130944b8b4ae00e014082d66,
title = "Characterisation of protein-polyphenol interactions in beer during forced aging",
abstract = "Proteins and proteinaceous material were extracted by acetone precipitation of beer that had undergone forced aging through 0 (control), 5 (medium) or 10 (high) heat/chill cycles (60 degrees C 48h/0 degrees C 24h). Size exclusion chromatography analysis of the crude beer extract showed that forced ageing led to a significant increase in binding of phenolic compounds to Protein Z and especially to lipid transfer protein 1 (LTP1). Protein-polyphenol conjugates were also present in high molecular weight (> 100 kDa) and low molecular weight fractions (<5 kDa), but these conjugates were already present in the fresh beer and were not affected by the forced aging. Treatment of the crude beer extract with sulphite (2 M) dissociated the protein-polyphenol bindings in LTP1 and Protein Z that had been generated during medium forced aging. Identification and quantification of the free, the non-covalently, and the covalently bound phenolic compounds were performed by UHPLC after extraction by methanol, acetic acid, and sulphite, respectively. The amounts of vanillic acid and caffeic acid decreased in the free polyphenol fraction, indicating binding to proteins during forced aging. Epicatechin and quercetin-3-O-glucoside were found to be non-covalently bound during forced aging. Finally, gallic acid, epicatechin, protocatechuic acid, and astragalin were found to be covalently bound already in the fresh beer. (c) 2020 The Institute of Brewing & Distilling",
keywords = "Haze, polyphenols, sulphite, covalent binding, GREEN TEA, HAZE, STABILITY, OXIDATION, QUINONES, KINETICS, EXTRACT, QUALITY, BINDING, ACIDS",
author = "Sisse Jongberg and Andersen, {Mogens L.} and Lund, {Marianne N.}",
year = "2020",
doi = "10.1002/jib.623",
language = "English",
volume = "126",
pages = "371--381",
journal = "Journal of the Federated Institutes of Brewing",
issn = "0046-9750",
publisher = "Wiley-Blackwell",
number = "4",

}

RIS

TY - JOUR

T1 - Characterisation of protein-polyphenol interactions in beer during forced aging

AU - Jongberg, Sisse

AU - Andersen, Mogens L.

AU - Lund, Marianne N.

PY - 2020

Y1 - 2020

N2 - Proteins and proteinaceous material were extracted by acetone precipitation of beer that had undergone forced aging through 0 (control), 5 (medium) or 10 (high) heat/chill cycles (60 degrees C 48h/0 degrees C 24h). Size exclusion chromatography analysis of the crude beer extract showed that forced ageing led to a significant increase in binding of phenolic compounds to Protein Z and especially to lipid transfer protein 1 (LTP1). Protein-polyphenol conjugates were also present in high molecular weight (> 100 kDa) and low molecular weight fractions (<5 kDa), but these conjugates were already present in the fresh beer and were not affected by the forced aging. Treatment of the crude beer extract with sulphite (2 M) dissociated the protein-polyphenol bindings in LTP1 and Protein Z that had been generated during medium forced aging. Identification and quantification of the free, the non-covalently, and the covalently bound phenolic compounds were performed by UHPLC after extraction by methanol, acetic acid, and sulphite, respectively. The amounts of vanillic acid and caffeic acid decreased in the free polyphenol fraction, indicating binding to proteins during forced aging. Epicatechin and quercetin-3-O-glucoside were found to be non-covalently bound during forced aging. Finally, gallic acid, epicatechin, protocatechuic acid, and astragalin were found to be covalently bound already in the fresh beer. (c) 2020 The Institute of Brewing & Distilling

AB - Proteins and proteinaceous material were extracted by acetone precipitation of beer that had undergone forced aging through 0 (control), 5 (medium) or 10 (high) heat/chill cycles (60 degrees C 48h/0 degrees C 24h). Size exclusion chromatography analysis of the crude beer extract showed that forced ageing led to a significant increase in binding of phenolic compounds to Protein Z and especially to lipid transfer protein 1 (LTP1). Protein-polyphenol conjugates were also present in high molecular weight (> 100 kDa) and low molecular weight fractions (<5 kDa), but these conjugates were already present in the fresh beer and were not affected by the forced aging. Treatment of the crude beer extract with sulphite (2 M) dissociated the protein-polyphenol bindings in LTP1 and Protein Z that had been generated during medium forced aging. Identification and quantification of the free, the non-covalently, and the covalently bound phenolic compounds were performed by UHPLC after extraction by methanol, acetic acid, and sulphite, respectively. The amounts of vanillic acid and caffeic acid decreased in the free polyphenol fraction, indicating binding to proteins during forced aging. Epicatechin and quercetin-3-O-glucoside were found to be non-covalently bound during forced aging. Finally, gallic acid, epicatechin, protocatechuic acid, and astragalin were found to be covalently bound already in the fresh beer. (c) 2020 The Institute of Brewing & Distilling

KW - Haze

KW - polyphenols

KW - sulphite

KW - covalent binding

KW - GREEN TEA

KW - HAZE

KW - STABILITY

KW - OXIDATION

KW - QUINONES

KW - KINETICS

KW - EXTRACT

KW - QUALITY

KW - BINDING

KW - ACIDS

U2 - 10.1002/jib.623

DO - 10.1002/jib.623

M3 - Journal article

VL - 126

SP - 371

EP - 381

JO - Journal of the Federated Institutes of Brewing

JF - Journal of the Federated Institutes of Brewing

SN - 0046-9750

IS - 4

ER -

ID: 248598565