Application of immunological methods to differentiate between foam-positive and haze-active proteins originating from malt
Date
2003
Authors
Evans, D.
Robinson, L.
Sheehan, M.
Tolhurst, R.
Hill, A.
Skerritt, J.
Barr, A.
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Journal of the American Society of Brewing Chemists, 2003; 61(2):55-62
Statement of Responsibility
Conference Name
Abstract
Beer foam and storage haze stability are of critical importance to brewers because they are among the first characteristics by which a consumer judges the quality of his or her beer. Key malt-derived, foam-positive proteins, including protein Z4, lipid transfer protein 1 (LTP1), and some members of the hordein storage protein family, interact principally with hop acids to stabilize foam. Silica-mediated beer stabilization procedures remove haze-active protein with high levels of proline (>30%) and glutamine (>30%), suggestive of a hordein origin, without reducing foam stability. Polyclonal antibodies to protein fractions of enriched beer foam proteins and proteins extracted from silica used for beer stabilization were developed. The antibodies were found to measure different malt-derived proteins. The antibodies were subsequently used to select foam-positive and haze-active hordein-recognizing monoclonal antibodies, which enabled the development of enzyme-linked immunosorbent assays (ELISAs). The ELISAs and immunochemical procedures were applied to predict beer foam and haze quality from malt used to brew beer by using pilot- (50 L) and small-scale (0.6-0.8 L) brewing procedures. It is anticipated that the immunochemical methods may be applied to select and manipulate malt for brewing to improve beer foam stability while reducing the likelihood of storage haze formation.