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Probing heat‐stable water‐soluble proteins from barley to malt and beer
Author(s) -
Perrocheau Ludivine,
Rogniaux Hélène,
Boivin Patrick,
Marion Didier
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200401153
Subject(s) - brewing , plant lipid transfer proteins , maillard reaction , chemistry , proteomics , storage protein , mashing , biochemistry , protease , food science , gel electrophoresis , chymotrypsin , glutenin , amylase , chromatography , trypsin , enzyme , protein subunit , fermentation , gene
Proteins determine the quality of barley in malting and brewing end‐uses. In this regard, water‐soluble barley proteins play a major role in the formation, stability, and texture of head foams. Our objective was to survey the barley seed proteins that could be involved in the foaming properties of beer. Therefore, two‐dimensional (2‐D) electrophoresis and mass spectrometry were combined to highlight the barley proteins that could resist the heating treatments occurring during malting and brewing processes. As expected, from barley to malt and to beer, most of the heat‐stable proteins are disulfide‐rich proteins, implicated in the defense of plants against their bio‐aggressors, e.g. , serpin‐like chymotrypsin inhibitors (protein Z), amylase and amylase‐protease inhibitors, and lipid transfer proteins (LTP1 and LTP2). For LTP1s, the complex pattern displayed in 2‐D electrophoresis could be related to some chemical modifications already described elsewhere, such as acylation or glycation through Maillard reactions, which occur on malting. Our proteomics approach allowed the identification of the numerous proteins present in beer in addition to the major ones already described. The involvement of these proteins in the quality of beer foam can now be evaluated.