The identification of a barley haze active protein that influences beer haze stability: Cloning and characterisation of the barley SE protein as a barley trypsin inhibitor of the chloroform/methanol type
Date
2007
Authors
Robinson, L.
Juttner, J.
Milligan, A.
Lahnstein, J.
Eglinton, J.
Evans, D.
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Advisors
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Journal article
Citation
Journal of Cereal Science, 2007; 45(3):343-352
Statement of Responsibility
Louise H. Robinson, Peter Healy, Doug C. Stewart, Jason K. Eglinton, Chris M. Ford and David E. Evans
Conference Name
Abstract
Previous pilot brewing trials have demonstrated that in the absence of a molecular weight (MW) ~12,000 (barley silica eluate (SE) protein), the beer brewed from the malt of these SE −ve varieties formed less haze after accelerated ageing than beers brewed using SE +ve malt varieties. The previously described SE protein was characterised using comparative two-dimensional (2-D) gel electrophoresis immunoblots of barley seed extracts from both SE +ve and SE −ve varieties. The SE protein spot identified was excised and its partial sequence determined, after in-gel cleavage using trypsin and separation of the resulting fragments by reversed-phase high performance liquid chromatography (HPLC). N-terminal sequence analysis of the tryptic peptides from SE +ve and SE −ve varieties identified the SE protein as the barley trypsin inhibitor-CMe precursor (BTI-CMe). The mature BTI-CMe protein is 13.3 kDa and its functional gene is located on chromosome 3H. Cloning of the BTI-CMe protein demonstrated that both SE −ve and SE +ve barley varieties contain a BTI-CMe protein family member that is similar but has a consistently different sequence, primarily in the last 30 amino acid residues of their C-termini.
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Copyright © 2006 Elsevier Ltd All rights reserved.