The influence of barley malt protein modification on beer foam stability and their relationship to the Barley Dimeric α-Amylase Inhibitor-1 (BDAI-1) as a possible foam-promoting protein

Yoshihiro Okada, Takashi Ilmure, Kiyoshi Takoi, Takafumi Kaneko, Makoto Kihara, Katsuhiro Hayashi, Kazutoshi Ito, Kazuhiro Sato, Kazuyoshi Takeda

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

The foam stability of beer is one of the important key factors in evaluating the quality of beer. The purpose of this study was to investigate the relationship between the level of malt modification (degradation of protein, starch, and so on) and the beer foam stability. This was achieved by examining foam-promoting proteins using two-dimensional gel electrophoresis (2DE). We found that the foam stability of beer samples brewed from the barley malts of cultivars B and C decreased as the level of malt modification increased; however, the foam stability of cultivar A did not change. To identify the property providing the increased foam stability of cultivar A, we analyzed beer proteins using 2DE. We analyzed three fractions that could contain beer foam-promoting proteins, namely, beer whole proteins, salt-precipitated proteins, and the proteins concentrated from beer foam. As a result, we found that in cultivar A, some protein spots did not change in any of these three protein fractions even when the level of malt modification increased, although the corresponding protein spots in cultivars B and C decreased. We analyzed these protein spots by peptide mass finger printing using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. As a result, all of these spots were identified as barley dimeric α-amylase inhibitor-1 (BDAI-1). These results suggest that BDAI-1 is an important contributor to beer foam stability.

Original languageEnglish
Pages (from-to)1458-1464
Number of pages7
JournalJournal of Agricultural and Food Chemistry
Volume56
Issue number4
DOIs
Publication statusPublished - Feb 27 2008

Fingerprint

Beer
malt
Hordeum
Amylases
foams
beers
amylases
Foams
barley
Proteins
proteins
cultivars
Printing
matrix-assisted laser desorption-ionization mass spectrometry
two-dimensional gel electrophoresis
Electrophoresis, Gel, Two-Dimensional
protein degradation
Starch
Electrophoresis
Proteolysis

Keywords

  • Barley malt cultivar
  • Beer foam stability
  • Beer protein
  • Malt modification
  • Two-dimensional gel electrophoresis

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)

Cite this

The influence of barley malt protein modification on beer foam stability and their relationship to the Barley Dimeric α-Amylase Inhibitor-1 (BDAI-1) as a possible foam-promoting protein. / Okada, Yoshihiro; Ilmure, Takashi; Takoi, Kiyoshi; Kaneko, Takafumi; Kihara, Makoto; Hayashi, Katsuhiro; Ito, Kazutoshi; Sato, Kazuhiro; Takeda, Kazuyoshi.

In: Journal of Agricultural and Food Chemistry, Vol. 56, No. 4, 27.02.2008, p. 1458-1464.

Research output: Contribution to journalArticle

Okada, Yoshihiro ; Ilmure, Takashi ; Takoi, Kiyoshi ; Kaneko, Takafumi ; Kihara, Makoto ; Hayashi, Katsuhiro ; Ito, Kazutoshi ; Sato, Kazuhiro ; Takeda, Kazuyoshi. / The influence of barley malt protein modification on beer foam stability and their relationship to the Barley Dimeric α-Amylase Inhibitor-1 (BDAI-1) as a possible foam-promoting protein. In: Journal of Agricultural and Food Chemistry. 2008 ; Vol. 56, No. 4. pp. 1458-1464.
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AB - The foam stability of beer is one of the important key factors in evaluating the quality of beer. The purpose of this study was to investigate the relationship between the level of malt modification (degradation of protein, starch, and so on) and the beer foam stability. This was achieved by examining foam-promoting proteins using two-dimensional gel electrophoresis (2DE). We found that the foam stability of beer samples brewed from the barley malts of cultivars B and C decreased as the level of malt modification increased; however, the foam stability of cultivar A did not change. To identify the property providing the increased foam stability of cultivar A, we analyzed beer proteins using 2DE. We analyzed three fractions that could contain beer foam-promoting proteins, namely, beer whole proteins, salt-precipitated proteins, and the proteins concentrated from beer foam. As a result, we found that in cultivar A, some protein spots did not change in any of these three protein fractions even when the level of malt modification increased, although the corresponding protein spots in cultivars B and C decreased. We analyzed these protein spots by peptide mass finger printing using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. As a result, all of these spots were identified as barley dimeric α-amylase inhibitor-1 (BDAI-1). These results suggest that BDAI-1 is an important contributor to beer foam stability.

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