Sara Junco

Universidad de Oviedo

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Yoana Expósito

Universidad de Oviedo

María Dolores Gutiérrez-Álvarez

Universidad de Oviedo

Domingo Blanco Gomis

Universidad de Oviedo

Domingo Blanco

Universidad de Zaragoza

Cooperative Institutions

Universidad de Oviedo

Servicio Regional de Investigación y Desarrollo Agroalimentario

Universidad de Zaragoza

Centro de Investigación y Tecnología Agroalimentaria de Aragón

Marymount University

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Study of Various Treatments to Isolate Low Levels of Cider Proteins to Be Analyzed by Capillary Sieving Electrophoresis

Journal of Liquid Chromatography &amp Related Technologies (2004)

Domingo Blanco Sara Junco Yoana Expósito María Dolores Gutiérrez-Álvarez

Abstract Four different sample treatments (ethanol precipitation, dialysis, ultrafiltration, and gel filtration) to isolate cider proteins were tested in this work. Purified cider proteins were analyzed by capillary sieving electrophoresis (CSE) using linear polyacrylamide as a sieving medium under optimized conditions; with this technique, separation, and molecular weight determination of proteins are possible. The electropherograms obtained in the protein analysis with each treatment were compared to choose the one that led to the best results. This was found to be ultrafiltration; many peaks were obtained in the electrophoretic profile and their spectra corresponded to a protein. Bradford analysis confirmed this choice. These results were compared with those obtained by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE), the molecular weights of the protein bands agreeing with the molecular weights of the electrophoretic peaks obtained with ultrafiltration.

Ultrafiltration (renal)

Electropherogram

Sodium dodecyl sulfate

Ethanol precipitation

Molecular mass

10.1081/jlc-120034089

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

Electrophoresis (2003)

Domingo Blanco Gomis Sara Junco Yoana Expósito María Dolores Gutiérrez-Álvarez

Abstract 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 μm 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; β‐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).

Molecular mass

Hydroxymethyl

Sodium dodecyl sulfate

Polyacrylamide

10.1002/elps.200390178

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Citations (28)