Selected malting parameters of new accessions from the collection of spring barley genetic resources.

The study of plant proteome is important because proteins and glycoproteins are involved in many crucial biological processes that could enhance the agronomical and nutritional value of crops and food products. The analysis of model organisms (e.g., Arabidopsis thaliana) is a popular means to aid in understanding many plant features. Proteomics has the potential to contribute to cereal science, mainly through the description of grain quality by elucidating the ways in which the genes are expressed during grain filling under particular environmental conditions. Since barley grain composition (i.e., its protein and glycoprotein analysis) is important for the brewing industry, human and animal nutrition, plant breeding or cultivar identification, the profiles of glycoproteins released from barley were one of the aims of this paper. This work combines affinity chromatography with 1D gel electrophoresis followed by mass spectrometry for the characterization of modified plant proteins. Lectin chromatography with Concanavalin A (ConA) was integrated to the procedure for the selective isolation of N-glycoproteins. For the verification of the universality of a chosen approach, proteins were extracted by deionized water from two different model plant materials-barley (Hordeum vulgare) and A. thaliana. Our attention was focused on the glycoproteins present in both barley grains and grains after the malting procedure and Arabidopsis seedlings. The proteins retained in an affinity column were separated by SDS-PAGE, excised, digested by trypsin and studied by MALDI-TOF MS. SDS gels revealed the differences between ConA non-bound and bound fractions. The majority of proteins were found in non-bound fractions. Several important glycoproteins were confirmed in studied materials: barley grain (serine carboxypeptidase; alphaamylase inhibitor BMAI-1), barley malt (e.g., b-D-xylosidase) and Arabidopsis (b-D-xylosidase, peroxidase, etc.).

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“…A micromalting method was based on the traditional procedure used in the RIBM [32]. Barley grains were ground to fine flour in a rotating mill.…”

Section: Extraction Of Proteins From Barley Grainsmentioning

confidence: 99%

The Combination of Lectin Affinity Chromatography, Gel Electrophoresis and Mass Spectrometry in the Study of Plant Glycoproteome: Preliminary Insights

2011

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“…Malt was prepared from the same variety by the Research Institute of Brewing and Malting (RIBM, Brno, Czech Republic). A micro‐malting method was based on the traditional procedure used in the RIBM . The protein content of barley grains and malt (determinated by the Kjeldahl method) was 11.50% and 10.95%, respectively.…”

Section: Methodsmentioning

confidence: 99%

Study of quantitative changes of cereal allergenic proteins after food processing

Flodrová

Benkovská

Laštovičková

2014

J. Sci. Food Agric.

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“…All samples (Jersey, Tolar and the KM1910 variety which was registered as "AF Lucius" in 2009) were supplied by the Research Institute of Brewing and Malting (Brno, Czech Republic). Malt was prepared according to the literature 20 . Briefly, the following process was used for laboratory malting.…”

Section: Methodsmentioning

confidence: 99%

Utilization of the Linear Mode of MALDI-TOF Mass Spectrometry in the Study of Glycation During the Malting Process

Laštovičková

Mazanec

Benkovská

et al. 2010

Journal of the Institute of Brewing

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The process of glycation during the malting process was monitored by the linear mode of matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF MS). Watersoluble proteins were investigated and two hulled barley varieties, Jersey and Tolar, were compared to the hulless line KM 1910. The crude extracts of the proteins obtained from the grain, the malt, and aliquots collected every 24 h during the malting process, were mixed with the matrix (2,6-dihydroxyacetophenone) and analyzed by mass spectrometry. The protein composition of the barley changed during the malting process. The protein patterns did not differ significantly between the three varieties of the barley grains. However, significant differences between the malts were evident. Results showed the influence of the malting process on the glycation of certain watersoluble barley proteins, nonspecific lipid transfer protein 1 (LTP1) and protein Z, of which the glycated forms survived the brewing process. These major barley proteins are very important for the formation and stability of beer foam and glycation may prevent their precipitation. Analysis results indicated that slight glycation of the proteins had occurred on the second day of malting. The linear mode of MALDI-TOF mass spectrometry was used as a fast and simple method for monitoring the patterns of low-molecular weight barley proteins with regard to barley variety discrimination. This procedure also enables the selection of barley varieties suitable for the malting industry.

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Selected malting parameters of new accessions from the collection of spring barley genetic resources.

Cited by 10 publications

References 1 publication

The Combination of Lectin Affinity Chromatography, Gel Electrophoresis and Mass Spectrometry in the Study of Plant Glycoproteome: Preliminary Insights

The Combination of Lectin Affinity Chromatography, Gel Electrophoresis and Mass Spectrometry in the Study of Plant Glycoproteome: Preliminary Insights

Study of quantitative changes of cereal allergenic proteins after food processing

Utilization of the Linear Mode of MALDI-TOF Mass Spectrometry in the Study of Glycation During the Malting Process

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