Purification and Structural Characterization of LTP1 Polypeptides from Beer
| Autor: | Didier Marion, Daniel Mollé, Jean-Paul Douliez, Sandrine Jégou, Patrick Boivin |
|---|---|
| Přispěvatelé: | ProdInra, Migration, UR 0724 Unité de recherche Biochimie et technologie des protéines, Institut National de la Recherche Agronomique (INRA)-Transformation des Produits Végétaux (T.P.V.)-Unité de recherche Biochimie et technologie des protéines (NANT LBTP), UR 0121 Laboratoire de recherche de Technologie Laitière, Institut National de la Recherche Agronomique (INRA) |
| Rok vydání: | 2000 |
| Předmět: |
Circular dichroism
Alkylation 01 natural sciences Mass Spectrometry symbols.namesake 0404 agricultural biotechnology Glycation [SDV.IDA]Life Sciences [q-bio]/Food engineering Molecule Hexose Amino Acids ComputingMilieux_MISCELLANEOUS Plant Proteins chemistry.chemical_classification business.industry Circular Dichroism 010401 analytical chemistry Beer food and beverages Hordeum 04 agricultural and veterinary sciences General Chemistry Antigens Plant [SDV.IDA] Life Sciences [q-bio]/Food engineering 040401 food science 0104 chemical sciences Maillard reaction chemistry Biochemistry symbols Brewing Hordeum vulgare PROTEINE DE TRANSFERT DE LIPIDE Carrier Proteins Peptides General Agricultural and Biological Sciences business Plant lipid transfer proteins |
| Zdroj: | Journal of Agricultural and Food Chemistry Journal of Agricultural and Food Chemistry, American Chemical Society, 2000, 48, pp.5023-5029 |
| ISSN: | 1520-5118 0021-8561 |
| DOI: | 10.1021/jf000075m |
| Popis: | We report on the purification of lipid transfer proteins (LTP) from barley seeds and beer with the aim of investigating the chemical modifications that occur during the brewing process. In seeds, the well-known LTP of 9 kDa (LTP1) has been found together with a second form named LTPb that displays comparable amino acid composition but was not fully sequenced. These two forms have been recovered in beer with marked chemical modifications including disulfide bond reduction and rearrangement and especially glycation by Maillard reaction. The glycation is heterogeneous with variable amounts of hexose units bound to LTPs. Circular dichroism shows that glycated LTP1 having all their disulfide bridges reduced are totally unfolded. These results provide a first basis for understanding how barley LTPs become foam-promoting agents during the malting and brewing process. |
| Databáze: | OpenAIRE |
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