MS based proteomic approaches for analysis of barley malt

Laštovičková, Markéta; Bobáľová, Janette

doi:10.1016/j.jcs.2012.07.013

Cited by 13 publications

(9 citation statements)

References 119 publications

(107 reference statements)

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“…SDS gels displayed noticeable changes in the band intensities between both wheat/couscous and barley/malt pairs. This result was in accordance with our expectation and data that has already been published . The protein band intensities of couscous seemed to be generally lower than those in wheat grains.…”

Section: Resultssupporting

confidence: 94%

Study of quantitative changes of cereal allergenic proteins after food processing

Flodrová

Benkovská

Laštovičková

2014

J. Sci. Food Agric.

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Section: Resultssupporting

confidence: 94%

Study of quantitative changes of cereal allergenic proteins after food processing

Flodrová

Benkovská

Laštovičková

2014

J. Sci. Food Agric.

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“…Water-soluble proteins from barley grain and malt and from 7-day-old seedlings of Arabidopsis were obtained by an optimized extraction procedure [34]. Obtained extracts were subjected to the separation on an affinity column with immobilized lectin.…”

Section: Resultsmentioning

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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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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“…Methods of extracting and identifying the low‐salt soluble fraction consisting of enzymes and enzyme inhibitors from barley seeds and malt have been developed . Less than 200 protein spots in germinating barley or malt obtained by micromalting have been identified in previous studies and prediction of the relationship between metabolic proteins and malt quality is stranded. While the biochemistry of malting and brewing has been the subject of extensive study, knowledge of specific molecular processes catalyzed and regulated by metabolic proteins is limited.…”

Section: Introductionmentioning

confidence: 99%

Temporal Analyses of Barley Malting Stages Using Shotgun Proteomics

Mahalingam

2018

Proteomics

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Malt derived from barley malting is an essential raw material for beer brewing. In this study, we performed the first dynamic proteome survey during barley malting using a gel-free proteomics approach. This entailed in-solution tryptic digestion of precipitated proteins and analysis of peptides by nanoliquid chromatography coupled with tandem mass spectrometry. A total of 1418 proteins were identified from the five malting stages: Steep, 1, 3, 5 days after germination, and end of Kiln. About 900 proteins identified in this analysis were uncharacterized or predicted proteins. Integrating information from Uniprot90, Uniprot50, Pfam, Interpro databases and gene ontologies from EnsemblPlants, 796 of the predicted and uncharacterized proteins were provided functional annotations. Nearly 63% of the identified proteins were present during all the five time points suggesting a coordinated activation of major metabolic pathways during malting. GO enrichment analysis showed over-representation of proteins associated with translation, carbohydrate metabolism, and stress response. Analysis of variance of the spectral counts of proteins present in all the five malting stages identified 205 proteins with significant differences in their abundance. Proteins associated with carbohydrate metabolism especially enzyme activity regulation provide novel targets for malting barley breeding and for predicting malting quality.

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MS based proteomic approaches for analysis of barley malt

Cited by 13 publications

References 119 publications

Study of quantitative changes of cereal allergenic proteins after food processing

Study of quantitative changes of cereal allergenic proteins after food processing

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

Temporal Analyses of Barley Malting Stages Using Shotgun Proteomics

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