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Immunological characterisation of barley polypeptides in lager foam
Author(s) -
Kauffman Juliet A,
Mills E N Clare,
Brett Gary M,
Fido Roger J,
Tatham Arthur S,
Shewry Peter R,
Onishi Akiko,
Proudlove Michael O,
Morgan Michael R A
Publication year - 1994
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740660312
Subject(s) - hordein , chemistry , trypsin , biochemistry , storage protein , monoclonal antibody , microbiology and biotechnology , prolamin , antibody , chromatography , enzyme , biology , gene , genetics
Eight monoclonal antibodies (mAb) recognising barley polypeptides have been identified from a library developed to wheat prolamins. The specificity or the mAb has been determined using enzyme‐linked immunosorbent assay (ELISA) and immunoblotting. Six were of broad specificity, recognising D, B, C and γ‐hordeins to varying degrees by both techniques. IFRN 0610 preferentially recognised γ‐hordeins by ELISA but was highly specific for this hordein group by immunoblotting. Another mAb, IFRN 0624, bound to a M r ∽ 18000 polypeptide belonging to the CM protein (trypsin/α‐amylase inhibitor) family by immunoblotting. This, or a related protein, was detected by 0624 in all hordein fractions using ELISA. These mAb, together with two others described previously and found to recognise the repeat motif of C hordein, were used in ELISA and immunoblot analysis of Octyl‐Sepharose fractions of lager foam. Hordein polypeptides were found in all foam fractions, indicating that much foam protein originates from the malt. The CM‐like protein was found present in a virtually unmodified form. In contrast, the repeat motif of C hordein was not detected, indicating that it had either been destroyed or masked by other beer constituents. The foam stabilising agent, propylene glycol alginate (PGA), increased the apparent hydrophobicity of hordein fragments suggesting that at least part of the activity of PGA is mediated by interactions with the hordein components of foam.