Fast analysis of proteins in wines by capillary gel electrophoresis

Rodríguez‐Delgado, Miguel Ángel; Malovaná, Sabina; Montelongo, F. J. García; Cifuentes, Alejandro

doi:10.1007/s00217-002-0514-1

Cited by 15 publications

(4 citation statements)

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“…Peaks at 22 and 26 kDa in SDS‐CGE correspond to bands at 21 and 23 kDa in SDS‐PAGE, respectively, as both mechanisms of protein separation were identical and based on MM size (Rodríguez‐Delgado et al. ). Proteins with similar MM to the 33 kDa band in SDS‐PAGE and 32 kDa peak in SDS‐CGE, which have rarely been reported and characterised in wine protein studies (Hsu and Heatherbell 1987a, Hayasaka et al.…”

Section: Discussionmentioning

confidence: 99%

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Protein concentration and bentonite requirement in Marlborough Sauvignon Blanc wines

Hung

Harrison

Morton

et al. 2013

Australian Journal of Grape and Wine Research

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Background and Aims Protein instability has long been a technical issue in white wine production. The aims of this study were: to examine the variability of wine proteins from a single cultivar within a defined wine region over two vintages; and to investigate the correlation of the content of the total and individual proteins and protein haze with the bentonite dosage required for heat stability. Methods and Results Proteins in Sauvignon Blanc juices and wines from five selected Marlborough, New Zealand, vineyards with two pruning/training regimes (two‐ and four‐cane vertical shoot positioned) were studied over two consecutive vintages. Proteins were quantified and characterised by Coomassie Brilliant Blue assay, sodium dodecyl sulfate polyacrylamide gel electrophoresis and sodium dodecyl sulfate capillary gel electrophoresis (SDS‐CGE). The bentonite requirement for wine protein stability was determined by bentonite fining coupled with a hot/cold test. One vineyard consistently showed the lowest protein concentration and bentonite requirement regardless of pruning treatment and vintage, whereas others varied with pruning treatment and/or vineyard site and/or vintage. Two prevalent juice protein peaks at 22 and 28 kDa in SDS‐CGE corresponded to two main wine protein peaks at 22 and 26 kDa, respectively. The 26 kDa fraction was reduced and became heterogeneous after fermentation, while the 22 kDa fraction remained unaffected. There was a good correlation between bentonite requirement and the 26 kDa fraction (R2 = 0.78). Conclusion The depletion of 26 kDa fraction in wine determined by SDS‐CGE was a good indicator for protein stability by bentonite fining. Significance of the Study These results suggest that the method of protein quantification may have a strong influence on the utility of protein concentration measurement to predict the bentonite requirement of wine.

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Section: Discussionmentioning

confidence: 99%

“…Protein separation by sodium dodecyl sulfate capillary gel electrophoresis (SDS‐CGE) has been demonstrated to take place through the same mechanism as in SDS‐PAGE (Guttman , Rodríguez‐Delgado et al. , Gomis et al. ).…”

Section: Introductionmentioning

confidence: 99%

Protein concentration and bentonite requirement in Marlborough Sauvignon Blanc wines

Hung

Harrison

Morton

et al. 2013

Australian Journal of Grape and Wine Research

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“…Proteins are collected by a centrifugal filter device and denatured with SDS and b-mercaptoethanol. Then they are analyzed by capillary SDS electrophoresis [162]. Variation in berry protein composition was observed in muscadine cultivars as investigated by PAGE and CE-SDS.…”

Section: Proteins In Agricultural Products and Foodmentioning

confidence: 99%

Capillary electrophoresis of proteins 2001–2003

Hutterer

Dolnı́k²

2003

Electrophoresis

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This review article with 244 references describes recent developments in capillary electrophoresis of proteins and covers the two years since the previous review (Dolník, V. Hutterer, K. Electrophoresis 2001, 22, 4163-4178) through Spring 2003. It covers topics related to CE of proteins including modeling of the electrophoretic properties of proteins, sample pretreatment, wall coatings, improving selectivity, detection, special electrophoretic techniques, and applications.

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“…In order to decrease the absorbance of the polymer, Ganzler et al [11] proposed the use of polyethyleneglycol and dextran as sieving mediums. Ready-to-use polymer solutions have recently become commercially available and have been successfully employed by many authors [12][13][14], but preparation of the polymer is simple and much cheaper, as Manabe et al [15] have demonstrated.…”

Section: Introductionmentioning

confidence: 99%

Size‐based separations of proteins by capillary electrophoresis using linear polyacrylamide as a sieving medium: Model studies and analysis of cider proteins

et al. 2003

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Electrophoretic conditions to separate sodium dodecyl sulfate (SDS)-protein complexes according to their relative molecular mass by capillary electrophoresis (CE) using linear polyacrylamide as a sieving matrix were examined. Five purified proteins with relative molecular masses between 14 400 and 66 200 Da were separated on a coated fused-silica capillary with an internal diameter of 100 microm and an effective length of 24 cm (total length, 32.5 cm). Benzoic acid was added to the solution of purified proteins as internal standard; beta-mercaptoethanol was also added as reducing agent. The running buffer composition was 0.05 M tris(hydroxymethyl)aminomethane (Tris), 0.035 M aspartic acid, 0.1% m/v SDS, 4% m/v acrylamide, the resulting pH being 8.0. The applied voltage was 7 kV (reversed voltage polarity) in order to avoid high current intensities. Under optimized conditions, the five proteins were separated in less than 15 min, with a % relative standard deviation (RSD) between 0.2 and 0.4 for migration times in the same day. Good efficiency (values between 150 000 and 40 000 N/m) and resolution (values between 2 and 2.8) were obtained. The inverse of relative migration times was found to correlate with the logarithm of their relative molecular mass. Finally, cider proteins were analyzed and their relative molecular masses were determined. These results were compared with those obtained by SDS-polyacrylamide gel electrophoresis (SDS-PAGE).

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Fast analysis of proteins in wines by capillary gel electrophoresis

Cited by 15 publications

References 0 publications

Protein concentration and bentonite requirement in Marlborough Sauvignon Blanc wines

Protein concentration and bentonite requirement in Marlborough Sauvignon Blanc wines

Capillary electrophoresis of proteins 2001–2003

Size‐based separations of proteins by capillary electrophoresis using linear polyacrylamide as a sieving medium: Model studies and analysis of cider proteins

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