TY - JOUR

T1 - Initial proteome analysis of mature barley seeds and malt

AU - Østergaard, Ole

AU - Melchior, Sabrina

AU - Roepstorff, Peter

AU - Svensson, Birte

PY - 2002

Y1 - 2002

N2 - Several barley (Hordeum vulgare) cultivars are used in the production of malt for brewing. The malt quality depends on the cultivar, its growth and storage conditions, and the industrial process. To enhance studies on malt quality, we embarked on a proteome analysis approach for barley seeds and malt. The proteome analysis includes two-dimensional (2-D) gel electrophoresis, mass spectrometry, and bioinformatics for identification of selected proteins. This project initially focused on proteins in major spots in the neutral isoelectric point range (pI 4-7) including selected spots that differ between four barley cultivars. The excellent malting barley cultivar Barke was used as reference. Cultivar differences in the 2-D gel spot patterns are observed both at the seed and the malt level. In seed extracts one of the proteins causing variations has been identified as an alpha-amylase/trypsin inhibitor. In malt extracts multiple forms of the alpha-amylase isozyme 2 have been identified in varying cultivar characteristic spot patterns. The present identification of proteins in major spots from 2-D gels includes 27 different proteins from 42 spots from mature seed extract, while only three specific proteins were identified by analysing 13 different spots from the corresponding malt extract. It is suggested that post-translational processing causes the same protein to occur in different spots.

AB - Several barley (Hordeum vulgare) cultivars are used in the production of malt for brewing. The malt quality depends on the cultivar, its growth and storage conditions, and the industrial process. To enhance studies on malt quality, we embarked on a proteome analysis approach for barley seeds and malt. The proteome analysis includes two-dimensional (2-D) gel electrophoresis, mass spectrometry, and bioinformatics for identification of selected proteins. This project initially focused on proteins in major spots in the neutral isoelectric point range (pI 4-7) including selected spots that differ between four barley cultivars. The excellent malting barley cultivar Barke was used as reference. Cultivar differences in the 2-D gel spot patterns are observed both at the seed and the malt level. In seed extracts one of the proteins causing variations has been identified as an alpha-amylase/trypsin inhibitor. In malt extracts multiple forms of the alpha-amylase isozyme 2 have been identified in varying cultivar characteristic spot patterns. The present identification of proteins in major spots from 2-D gels includes 27 different proteins from 42 spots from mature seed extract, while only three specific proteins were identified by analysing 13 different spots from the corresponding malt extract. It is suggested that post-translational processing causes the same protein to occur in different spots.

KW - Computational Biology/methods

KW - Edible Grain/metabolism

KW - Electrophoresis, Gel, Two-Dimensional/methods

KW - Hordeum/metabolism

KW - Mass Spectrometry/methods

KW - Plant Proteins/analysis

KW - Protein Isoforms

KW - Proteome/chemistry

KW - Silver Staining

KW - Species Specificity

KW - alpha-Amylases/chemistry

U2 - 10.1002/1615-9861(200206)2:6<733::AID-PROT733>3.0.CO;2-E

DO - 10.1002/1615-9861(200206)2:6<733::AID-PROT733>3.0.CO;2-E

M3 - Journal article

C2 - 12112856

VL - 2

SP - 733

EP - 739

JO - Proteomics

JF - Proteomics

SN - 1615-9853

IS - 6

ER -