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    <meta content="van Nierop, S.N.E." name="eprints.creators_name" />
<meta content="Evans, D.E" name="eprints.creators_name" />
<meta content="Axcell, B.C." name="eprints.creators_name" />
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<meta content="The impact of different wort boiling temperatures on the beer foam stabilizing properties of lipid transfer protein 1" name="eprints.title" />
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<meta content="Brewing; wort boiling; beer; foam quality; lipid transfer protein" name="eprints.keywords" />
<meta content="Beer consumers demand satisfactory and consistent foam stability; thus, it is a high priority for brewers.
Beer foam is stabilized by the interaction between certain beer proteins, including lipid transfer protein
1 (LTP1), and isomerized hop R-acids, but destabilized by lipids. In this study it was shown that the
wort boiling temperature during the brewing process was critical in determining the final beer LTP1
content and conformation. LTP1 levels during brewing were measured by an LTP1 ELISA, using
antinative barley LTP1 polyclonal antibodies. It was observed that the higher wort boiling temperatures
(102 °C), resulting from low altitude at sea level, reduced the final beer LTP1 level to 2-3 íg/mL,
whereas the lower wort boiling temperatures (96 °C), resulting from higher altitudes (1800 m),
produced LTP1 levels between 17 and 35 íg/mL. Low levels of LTP1 in combination with elevated
levels of free fatty acids (FFA) resulted in poor foam stability, whereas beer produced with low levels
of LTP1 and FFA had satisfactory foam stability. Previous studies indicated the need for LTP1
denaturing to improve its foam stabilizing properties. However, the results presented here show that
LTP1 denaturation reduces its ability to act as a binding protein for foam-damaging FFA. These
investigations suggest that wort boiling temperature is an important factor in determining the level
and conformation of LTP1, thereby favoring satisfactory beer foam stability." name="eprints.abstract" />
<meta content="2004" name="eprints.date" />
<meta content="published" name="eprints.date_type" />
<meta content="Journal of Agricultural and Food Chemistry" name="eprints.publication" />
<meta content="52" name="eprints.volume" />
<meta content="3120-3129" name="eprints.pagerange" />
<meta content="10.1021/jf035125c" name="eprints.id_number" />
<meta content="TRUE" name="eprints.refereed" />
<meta content="0021-8561" name="eprints.issn" />
<meta content="http://dx.doi.org/10.1021/jf035125c" name="eprints.official_url" />
<meta content="(1) Bamforth, C. W. Perceptions of beer foam. J. Inst. Brew. 2000,
106, 229-238.
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of beer foam, a review. J. Am. Soc. Brew. Chem. 2002, 60, 47-
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(6) Jones, B. L.; Marinac, L. A. Barley LTP1 (PAP1) and LTP2
are inhibitors of green malt cysteine endoproteinases. J. Am. Soc.
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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.
(9) Lusk, L. T.; Goldstein, H.; Ryder, D. Independent role of beer
proteins, melanoidins and polysaccharides in foam formation.
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(10) Sorensen, S. B.; Bech, L. M.; Muldberg, M.; Beenfeldt, T.;
Breddam, K. Barley lipid transfer protein 1 is involved in beer
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(11) Narziss, L. Modern wort boiling. Proc. Inst. Brew. ConV.,
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R. E. Foam negative materials. J. Am. Soc. Brew. Chem. 2001,
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and beer foam brewed with wheat flour. J. Am. Soc. Brew. Chem.
1987, 45, 43-47.
(20) Onishi, A.; Canterranne, E.; Clarke, D. J.; Proudlove, M. O.
Barley lipid binding proteins: their role in beer stabilization.
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(21) Kader, J. C. Lipid transfer proteins in plants. Annu. ReV. Plant
Physiol. Plant Mol. Biol. 1996, 47, 627-654.
(22) 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.
(23) Lusk, L. T.; Goldstein, H.; Watts, K.; Navarro, A.; Ryder, D.
Monitoring barley lipid transfer protein levels in barley, malting
and brewing. Eur. Brew. ConV. Congr. Proc., Budapest 2001,
28, 663-672.
(24) Klopper, W. J. Measurement of foam stability. Brew. Dig. 1977,
52, 51-53.
(25) Venter, P.; Kock, J. L. F.; Kuwa, S.; Botha, A.; Coetzee, D. J.;
Botes, P. J.; Bhatt, R. K.; Schewe, T.; Nigram, S. Production of
3R-hydroxy-polyenoic fatty acids by the yeast Dipodascopsis
uninucleata. Lipids 1997, 32, 1277-1283.
(26) Laemmli, U. K. Cleavage of structural proteins during the
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(27) Lide, D. R. Handbook of Chemistry and Physics, 71st ed.; CPD
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355.
(29) 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.
(30) 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.
(31) Jegou, S.; Douliez, J.-P.; Molle, D.; Boivin, P.; Marion, D.
Purification and characterization of LTP polypeptide from beer.
J. Agric. Food Chem. 2000, 48, 5023-5029.
(32) 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.
(33) 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.
(34) Chowdhury, S. K.; Katta, V.; Chait, B. T. Probing conformational
changes in proteins by mass spectrometry. J. Am. Chem. Soc.
1990, 112, 9012-9013.
(35) 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.
(36) Gumerov, D. R.; Dobo, A.; Kaltashov, I. A. Protein-ion chargestate
distributions in electrospray ionization mass spectrometry:
3128 J. Agric. Food Chem., Vol. 52, No. 10, 2004 Van Nierop et al.
distinguishing conformational contributions from masking effects.
Eur. J. Mass Spectrom. 2002, 8, 123-125.
(37) Simmons, D. A.; Konermann, L. Characterization of transient
protein folding intermediates during myoglobin reconstitution
by time-resolved electrospray mass spectrometry with on-line
isotopic pulse labeling. Biochemistry 2002, 41, 1906-1914.
(38) Winston, R. L.; Fitzgerald, M. C. Mass spectrometry as a readout
of protein structure and function. Mass Spectrom. ReV. 1997,
16, 165-179.
(39) Heinemann, B.; Andersen, K. V.; Nielsen, P. R.; Bech, L. M.;
Poulsen, F. M. Structure in solution of a four-helix lipid binding
protein. Protein Sci. 1996, 5, 13-23.
R" name="eprints.referencetext" />
<meta content="van Nierop, S.N.E. and Evans, D.E and Axcell, B.C. and Cantrell, I.C. and Rautenbach, M. (2004) The impact of different wort boiling temperatures on the beer foam stabilizing properties of lipid transfer protein 1. Journal of Agricultural and Food Chemistry, 52 . pp. 3120-3129. ISSN 0021-8561" name="eprints.citation" />
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<meta content="van Nierop, S.N.E." name="DC.creator" />
<meta content="Evans, D.E" name="DC.creator" />
<meta content="Axcell, B.C." name="DC.creator" />
<meta content="Cantrell, I.C." name="DC.creator" />
<meta content="Rautenbach, M." name="DC.creator" />
<meta content="300000 Agricultural, Veterinary and Environmental Sciences" name="DC.subject" />
<meta content="Beer consumers demand satisfactory and consistent foam stability; thus, it is a high priority for brewers.
Beer foam is stabilized by the interaction between certain beer proteins, including lipid transfer protein
1 (LTP1), and isomerized hop R-acids, but destabilized by lipids. In this study it was shown that the
wort boiling temperature during the brewing process was critical in determining the final beer LTP1
content and conformation. LTP1 levels during brewing were measured by an LTP1 ELISA, using
antinative barley LTP1 polyclonal antibodies. It was observed that the higher wort boiling temperatures
(102 °C), resulting from low altitude at sea level, reduced the final beer LTP1 level to 2-3 íg/mL,
whereas the lower wort boiling temperatures (96 °C), resulting from higher altitudes (1800 m),
produced LTP1 levels between 17 and 35 íg/mL. Low levels of LTP1 in combination with elevated
levels of free fatty acids (FFA) resulted in poor foam stability, whereas beer produced with low levels
of LTP1 and FFA had satisfactory foam stability. Previous studies indicated the need for LTP1
denaturing to improve its foam stabilizing properties. However, the results presented here show that
LTP1 denaturation reduces its ability to act as a binding protein for foam-damaging FFA. These
investigations suggest that wort boiling temperature is an important factor in determining the level
and conformation of LTP1, thereby favoring satisfactory beer foam stability." name="DC.description" />
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    <h1 class="ep_tm_pagetitle">The impact of different wort boiling temperatures on the beer foam stabilizing properties of lipid transfer protein 1</h1>
    <p style="margin-bottom: 1em" class="not_ep_block"><span class="person_name">van Nierop, S.N.E.</span> and <span class="person_name">Evans, D.E</span> and <span class="person_name">Axcell, B.C.</span> and <span class="person_name">Cantrell, I.C.</span> and <span class="person_name">Rautenbach, M.</span> (2004) <xhtml:em>The impact of different wort boiling temperatures on the beer foam stabilizing properties of lipid transfer protein 1.</xhtml:em> Journal of Agricultural and Food Chemistry, 52 . pp. 3120-3129. ISSN 0021-8561</p><p style="margin-bottom: 1em" class="not_ep_block"></p><table style="margin-bottom: 1em" class="not_ep_block"><tr><td valign="top" style="text-align:center"><a href="http://eprints.utas.edu.au/2315/1/_vanNierop_JAFC-04.pdf"><img alt="[img]" src="http://eprints.utas.edu.au/style/images/fileicons/application_pdf.png" class="ep_doc_icon" border="0" /></a></td><td valign="top"><a href="http://eprints.utas.edu.au/2315/1/_vanNierop_JAFC-04.pdf"><span class="ep_document_citation">PDF</span></a> - Full text restricted - Requires a PDF viewer<br />187Kb</td><td><form method="get" accept-charset="utf-8" action="http://eprints.utas.edu.au/cgi/request_doc"><input accept-charset="utf-8" value="2965" name="docid" type="hidden" /><div class=""><input value="Request a copy" name="_action_null" class="ep_form_action_button" onclick="return EPJS_button_pushed( '_action_null' )" type="submit" /> </div></form></td></tr></table><p style="margin-bottom: 1em" class="not_ep_block">Official URL: <a href="http://dx.doi.org/10.1021/jf035125c">http://dx.doi.org/10.1021/jf035125c</a></p><div class="not_ep_block"><h2>Abstract</h2><p style="padding-bottom: 16px; text-align: left; margin: 1em auto 0em auto">Beer consumers demand satisfactory and consistent foam stability; thus, it is a high priority for brewers.&#13;
Beer foam is stabilized by the interaction between certain beer proteins, including lipid transfer protein&#13;
1 (LTP1), and isomerized hop R-acids, but destabilized by lipids. In this study it was shown that the&#13;
wort boiling temperature during the brewing process was critical in determining the final beer LTP1&#13;
content and conformation. LTP1 levels during brewing were measured by an LTP1 ELISA, using&#13;
antinative barley LTP1 polyclonal antibodies. It was observed that the higher wort boiling temperatures&#13;
(102 °C), resulting from low altitude at sea level, reduced the final beer LTP1 level to 2-3 íg/mL,&#13;
whereas the lower wort boiling temperatures (96 °C), resulting from higher altitudes (1800 m),&#13;
produced LTP1 levels between 17 and 35 íg/mL. Low levels of LTP1 in combination with elevated&#13;
levels of free fatty acids (FFA) resulted in poor foam stability, whereas beer produced with low levels&#13;
of LTP1 and FFA had satisfactory foam stability. Previous studies indicated the need for LTP1&#13;
denaturing to improve its foam stabilizing properties. However, the results presented here show that&#13;
LTP1 denaturation reduces its ability to act as a binding protein for foam-damaging FFA. These&#13;
investigations suggest that wort boiling temperature is an important factor in determining the level&#13;
and conformation of LTP1, thereby favoring satisfactory beer foam stability.</p></div><table style="margin-bottom: 1em" cellpadding="3" class="not_ep_block" border="0"><tr><th valign="top" class="ep_row">Item Type:</th><td valign="top" class="ep_row">Article</td></tr><tr><th valign="top" class="ep_row">Keywords:</th><td valign="top" class="ep_row">Brewing; wort boiling; beer; foam quality; lipid transfer protein</td></tr><tr><th valign="top" class="ep_row">Subjects:</th><td valign="top" class="ep_row"><a href="http://eprints.utas.edu.au/view/subjects/300000.html">300000 Agricultural, Veterinary and Environmental Sciences</a></td></tr><tr><th valign="top" class="ep_row">ID Code:</th><td valign="top" class="ep_row">2315</td></tr><tr><th valign="top" class="ep_row">Deposited By:</th><td valign="top" class="ep_row"><span class="ep_name_citation"><span class="person_name">Dr Evan Evans</span></span></td></tr><tr><th valign="top" class="ep_row">Deposited On:</th><td valign="top" class="ep_row">24 Oct 2007 12:00</td></tr><tr><th valign="top" class="ep_row">Last Modified:</th><td valign="top" class="ep_row">09 Jan 2008 02:30</td></tr><tr><th valign="top" class="ep_row">ePrint Statistics:</th><td valign="top" class="ep_row"><a target="ePrintStats" href="/es/index.php?action=show_detail_eprint;id=2315;">View statistics for this ePrint</a></td></tr></table><p align="right">Repository Staff Only: <a href="http://eprints.utas.edu.au/cgi/users/home?screen=EPrint::View&amp;eprintid=2315">item control page</a></p>
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