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Volumn 52, Issue 10, 2004, Pages 3120-3129

Impact of Different Wort Boiling Temperatures on the Beer Foam Stabilizing Properties of Lipid Transfer Protein 1

Author keywords

Beer; Brewing; Foam quality; Lipid transfer protein; Wort boiling

Indexed keywords

FATTY ACID; LIPID TRANSFER PROTEIN; POLYCLONAL ANTIBODY;

EID: 2442617221     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf035125c     Document Type: Article
Times cited : (81)

References (39)
  • 1
    • 0034338122 scopus 로고    scopus 로고
    • Perceptions of beer foam
    • Bamforth, C. W. Perceptions of beer foam. J. Inst. Brew. 2000, 106, 229-238.
    • (2000) J. Inst. Brew. , vol.106 , pp. 229-238
    • Bamforth, C.W.1
  • 3
    • 2442479244 scopus 로고    scopus 로고
    • Aspen Publishers: Gaithersberg, MD
    • Lewis, M. J.; Young, T. W. Brewing; Aspen Publishers: Gaithersberg, MD, 2001.
    • (2001) Brewing
    • Lewis, M.J.1    Young, T.W.2
  • 4
    • 0036097175 scopus 로고    scopus 로고
    • Do not be fobbed off, the substance of beer foam, a review
    • Evans, D. E.; Sheehan, M. C. Do not be fobbed off, the substance of beer foam, a review. J. Am Soc. Brew. Chem. 2002, 60, 47-57.
    • (2002) J. Am Soc. Brew. Chem. , vol.60 , pp. 47-57
    • Evans, D.E.1    Sheehan, M.C.2
  • 5
    • 0002580242 scopus 로고
    • Origin of dominant beer protein immunochemical identity with β-amylase-associated protein from barley
    • Hejgaard, J. Origin of dominant beer protein immunochemical identity with β-amylase-associated protein from barley. J. Inst. Brew. 1977, 83, 94-96.
    • (1977) J. Inst. Brew. , vol.83 , pp. 94-96
    • Hejgaard, J.1
  • 6
    • 0006094488 scopus 로고
    • Barley LTP1 (PAP1) and LTP2 are inhibitors of green malt cysteine endoproteinases
    • Jones, B. L.; Marinac, L. A. Barley LTP1 (PAP1) and LTP2 are inhibitors of green malt cysteine endoproteinases. J. Am. Soc. Brew. Chem. 1995, 53, 194-195.
    • (1995) J. Am. Soc. Brew. Chem. , vol.53 , pp. 194-195
    • Jones, B.L.1    Marinac, L.A.2
  • 7
    • 84979400255 scopus 로고
    • Antigenic beer macromolecules, an experimental survey of purification methods
    • Kaersgaard, P.; Hejgaard, J. Antigenic beer macromolecules, an experimental survey of purification methods. J. Inst. Brew. 1979, 85, 103-111.
    • (1979) J. Inst. Brew. , vol.85 , pp. 103-111
    • Kaersgaard, P.1    Hejgaard, J.2
  • 8
    • 0001686333 scopus 로고
    • Throughout the brewing process barley lipid transfer protein 1 (LTP1) is transformed into a more foam-promoting form
    • Bech, L. M.; Vaag, P.; Heinemann, B.; Breddam, K. Throughout the brewing process barley lipid transfer protein 1 (LTP1) is transformed into a more foam-promoting form. Eur. Brew. Conv. Congr. Proc., Brussels 1995, 25, 561-568.
    • (1995) Eur. Brew. Conv. Congr. Proc., Brussels , vol.25 , pp. 561-568
    • Bech, L.M.1    Vaag, P.2    Heinemann, B.3    Breddam, K.4
  • 9
    • 0002633282 scopus 로고
    • Independent role of beer proteins, melanoidins and polysaccharides in foam formation
    • Lusk, L. T.; Goldstein, H.; Ryder, D. Independent role of beer proteins, melanoidins and polysaccharides in foam formation. J. Am. Soc. Brew. Chem. 1995, 53, 93-103.
    • (1995) J. Am. Soc. Brew. Chem. , vol.53 , pp. 93-103
    • Lusk, L.T.1    Goldstein, H.2    Ryder, D.3
  • 13
    • 84978587158 scopus 로고
    • The effects of lipids and related materials on beer foam
    • Roberts, R. T.; Keeney, P. J.; Wainwright, T. The effects of lipids and related materials on beer foam. J. Inst. Brew. 1978, 84, 9-12.
    • (1978) J. Inst. Brew. , vol.84 , pp. 9-12
    • Roberts, R.T.1    Keeney, P.J.2    Wainwright, T.3
  • 15
    • 2442433285 scopus 로고    scopus 로고
    • Negative influences on foam
    • Gromus, J. Negative influences on foam. Eur. Brew. Conv. Monograph 1998, No. 27, 69-83.
    • (1998) Eur. Brew. Conv. Monograph , vol.27 , pp. 69-83
    • Gromus, J.1
  • 16
    • 84979376459 scopus 로고
    • The foaming properties of beer
    • Bamforth, C. W. The foaming properties of beer. J. Inst. Brew. 1985, 91, 370-383.
    • (1985) J. Inst. Brew. , vol.91 , pp. 370-383
    • Bamforth, C.W.1
  • 17
    • 2442424951 scopus 로고
    • Foam evaluation: I. Primary cling; secondary cling; foam strength
    • Glenister, P. R.; Segal, E. Foam evaluation: I. primary cling; secondary cling; foam strength. Proc. Am. Soc. Brew. Chem. 1964, 55-63.
    • (1964) Proc. Am. Soc. Brew. Chem. , pp. 55-63
    • Glenister, P.R.1    Segal, E.2
  • 18
    • 84987288529 scopus 로고
    • The protection of beer foam against lipid-induced destabilization
    • Clarke, D. C.; Wilde, P. J.; Marion, D. The protection of beer foam against lipid-induced destabilization. J. Inst. Brew. 1994, 100, 23-25.
    • (1994) J. Inst. Brew. , vol.100 , pp. 23-25
    • Clarke, D.C.1    Wilde, P.J.2    Marion, D.3
  • 19
    • 0001827293 scopus 로고
    • Lipid-protein interactions in beer and beer foam brewed with wheat flour
    • Morris, K. S.; Hough, J. S. Lipid-protein interactions in beer and beer foam brewed with wheat flour. J. Am. Soc. Brew. Chem. 1987, 45, 43-47.
    • (1987) J. Am. Soc. Brew. Chem. , vol.45 , pp. 43-47
    • Morris, K.S.1    Hough, J.S.2
  • 22
    • 0033450812 scopus 로고    scopus 로고
    • The impact of malt derived proteins on beer foam quality. Part I. The effect of germination and kilning on the level of protein Z4, protein Z7 and LTP1
    • Evans, D. E.; Hejgaard, J. The impact of malt derived proteins on beer foam quality. Part I. The effect of germination and kilning on the level of protein Z4, protein Z7 and LTP1. J. Inst. Brew. 1999, 105, 159-169.
    • (1999) J. Inst. Brew. , vol.105 , pp. 159-169
    • Evans, D.E.1    Hejgaard, J.2
  • 24
    • 0002109254 scopus 로고
    • Measurement of foam stability
    • Klopper, W. J. Measurement of foam stability. Brew. Dig. 1977, 52, 51-53.
    • (1977) Brew. Dig. , vol.52 , pp. 51-53
    • Klopper, W.J.1
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 2442485457 scopus 로고
    • Some aspects of the technology of wort boiling today
    • Narziss, L.; Miedaner, H.; Scheider, S. Some aspects of the technology of wort boiling today. Brauwelt Int. 1992, 4, 346-355.
    • (1992) Brauwelt Int. , vol.4 , pp. 346-355
    • Narziss, L.1    Miedaner, H.2    Scheider, S.3
  • 29
    • 2442491721 scopus 로고    scopus 로고
    • Wort boiling today-boiling systems with low thermal stress in combination with volatile stripping
    • Willaert, R. G.; Baron, G. V. Wort boiling today-boiling systems with low thermal stress in combination with volatile stripping. J. Brew. Biotechnol. 2001, 26, 217-230.
    • (2001) J. Brew. Biotechnol. , vol.26 , pp. 217-230
    • Willaert, R.G.1    Baron, G.V.2
  • 30
    • 0034773958 scopus 로고    scopus 로고
    • Evidence of the glycation and denaturation of LTP1 during the malting and brewing process
    • Jegou, S.; Douliez, J.-P.; Molle, D.; Boivin, P.; Marion, D. Evidence of the glycation and denaturation of LTP1 during the malting and brewing process. J. Agric. Food Chem. 2001, 49, 4942-4949.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4942-4949
    • Jegou, S.1    Douliez, J.-P.2    Molle, D.3    Boivin, P.4    Marion, D.5
  • 32
    • 0035823634 scopus 로고    scopus 로고
    • Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-transcriptional modification
    • Lindorff-Larsen, K.; Lerche, M. H.; Poulsen, F. M.; Roepsstoff, P.; Winther, J. R. Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-transcriptional modification. J. Biol. Chem. 2001, 276, 33547-33553.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33547-33553
    • Lindorff-Larsen, K.1    Lerche, M.H.2    Poulsen, F.M.3    Roepsstoff, P.4    Winther, J.R.5
  • 33
    • 84979424803 scopus 로고
    • The fractionation of polypeptides from barley and beer by hydrophobic interaction chromatography: The influence of their hydrophobicity on foam stability
    • Slack, P. T.; Bamforth, C. W. The fractionation of polypeptides from barley and beer by hydrophobic interaction chromatography: the influence of their hydrophobicity on foam stability. J. Inst. Brew. 1983, 89, 397-401.
    • (1983) J. Inst. Brew. , vol.89 , pp. 397-401
    • Slack, P.T.1    Bamforth, C.W.2
  • 34
    • 0025674590 scopus 로고
    • Probing conformational changes in proteins by mass spectrometry
    • Chowdhury, S. K.; Katta, V.; Chait, B. T. Probing conformational changes in proteins by mass spectrometry. J. Am. Chem. Soc. 1990, 112, 9012-9013.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9012-9013
    • Chowdhury, S.K.1    Katta, V.2    Chait, B.T.3
  • 35
    • 0036177471 scopus 로고    scopus 로고
    • Detecting equilibrium cytochrome c folding intermediates by electrospray ionization mass spectrometry: Two partially folded forms populate the molten-globule state
    • Grandori, R. Detecting equilibrium cytochrome c folding intermediates by electrospray ionization mass spectrometry: two partially folded forms populate the molten-globule state. Protein Sci. 2002, 11, 453-458.
    • (2002) Protein Sci. , vol.11 , pp. 453-458
    • Grandori, R.1
  • 36
    • 0036335091 scopus 로고    scopus 로고
    • Protein-ion charge-state distributions in electrospray ionization mass spectrometry: Distinguishing conformational contributions from masking effects
    • Gumerov, D. R.; Dobo, A.; Kaltashov, I. A. Protein-ion charge-state distributions in electrospray ionization mass spectrometry: distinguishing conformational contributions from masking effects. Eur. J. Mass Spectrom. 2002, 8, 123-125.
    • (2002) Eur. J. Mass Spectrom. , vol.8 , pp. 123-125
    • Gumerov, D.R.1    Dobo, A.2    Kaltashov, I.A.3
  • 37
    • 0037065802 scopus 로고    scopus 로고
    • Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospmy mass spectrometry with on-line isotopic pulse labeling
    • Simmons, D. A.; Konermann, L. Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospmy mass spectrometry with on-line isotopic pulse labeling. Biochemistry 2002, 41, 1906-1914.
    • (2002) Biochemistry , vol.41 , pp. 1906-1914
    • Simmons, D.A.1    Konermann, L.2
  • 38
    • 0031173707 scopus 로고    scopus 로고
    • Mass spectrometry as a readout of protein structure and function
    • Winston, R. L.; Fitzgerald, M. C. Mass spectrometry as a readout of protein structure and function. Mass Spectrom. Rev. 1997, 16, 165-179.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 165-179
    • Winston, R.L.1    Fitzgerald, M.C.2


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