Purification and structural characterization of LTP1 polypeptides from beer.
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.
Jégou
S
S
Unité de Biochimie et Technologie des Protéines, INRA, BP 71627, 44316 Nantes Cedex 03, France.
Douliez
J P
JP
Mollé
D
D
Boivin
P
P
Marion
D
D
D000478:Alkylation; D000596:Amino Acids / Q000032:analysis; D052179:Antigens, Plant; D001515:Beer / Q000032:analysis*; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002942:Circular Dichroism; D001467:Hordeum / Q000737:chemistry; D013058:Mass Spectrometry; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins
D000596:Amino Acids; D052179:Antigens, Plant; D002352:Carrier Proteins; D010455:Peptides; D010940:Plant Proteins; C511920:lipid transfer proteins, plant