Characterization of food proteins by capillary electrophoresis

Chen, Fu-Tai A.; Tusak, Anton

doi:10.1016/0021-9673(94)00700-4

Cited by 33 publications

(14 citation statements)

References 13 publications

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“…Although whey proteins were well resolved using phosphate buffers at pH values between 7 and 9, the presence of urea in the separation buffer was necessary to effectively resolve caseins, as it prevents the formation of aggregates. Chen and Tusak [19] attempted the separation of milk proteins by using a high-ionic strength buffer at high pH (borate buffer at pH about 10.0), to increase the separation efficiency and eliminate the casein aggregates. Under these conditions, b-casein was well separated from a S -casein, but a-La and b-Lg comigrated with as-casein.…”

Section: Separation Of Bovine Milk Proteinsmentioning

confidence: 99%

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Capillary electrophoresis for the analysis of food proteins of animal origin

2001

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In recent years, capillary electrophoresis (CE) has become an analytical technique with many applications in the study of food proteins and peptides. This review describes the existing CE methods of analysis of milk, egg, meat and fish proteins and peptides. The major developments in the application of CE to solve different problems in food technology, such as the assessment of technological processes, quality, and authenticity control of animal foods, are considered. A section dealing with future directions on the analysis of food proteins by CE is also included.

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Section: Separation Of Bovine Milk Proteinsmentioning

confidence: 99%

“…The major egg white proteins were well resolved using an untreated fused-silica capillary and a high salt concentration and high pH borate buffer (300 mM borate buffer at pH 10.0) [19]. Lysozyme migrated ahead of the neutral marker due its high pI, which is 1.0 unit above the buffer pH.…”

Section: Ce Of Egg Proteinsmentioning

confidence: 99%

Capillary electrophoresis for the analysis of food proteins of animal origin

2001

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“…␤-LgB and ␤-LgA were detected in the IFMP 2 and SMP samples. The poorer quality of the protein chromatograms is partly due to the high temperature treatment of the milk (spray drying dehydration at 200 or 250ЊC) [35,36]. Table 1 displays the concentrations of the five major proteins and the seven additives.…”

Section: Commercial Sample Analysismentioning

confidence: 99%

Simultaneous quantification of five proteins and seven additives in dairy products with a heart-cutting two-dimensional liquid chromatography method

Hou

Sun

et al. 2015

J. Sep. Science

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A heart-cutting two-dimensional high-performance liquid chromatography method was developed to simultaneously quantify five major proteins and seven food additives (maltol, ethyl maltol, vanillin, ethyl vanillin, benzoic acid, sorbic acid, and saccharin sodium) in milk and milk powders. In this two-dimensional system, a Venusil XBP-C4 column was selected in the first dimension for protein separation, and a Hypersil ODS-2 C18 column was employed in the second dimension for additive separation; a two-position, six-port switching valve was used to transfer the targets (additives) from the first dimension to the second dimension. Method validation consisted of selectivity, response function, linearity, precision, sensitivity, and recovery. In addition, a conventional one-dimensional high-performance liquid chromatography method was also tested for comparison. The two-dimensional method resulted in significantly improved recovery of the food additives compared to the conventional method (90.6-105.4% and 65.5-86.5%, respectively). Furthermore, this novel method has a simple one-step sample preparation procedure, which shortens the analysis time, resulting in more efficient analysis and less solvent usage.

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“…The result showed that there is 0.360 mg/mL lysozyme (0.360 was equal to 20-fold of the result obtained from the calibration curve of peak area versus concentration, because the proteins from egg white were diluted by buffer before separated), 9.071 mg/mL conalbumin, and 59.068 mg/mL ovalbumin in the egg white. The main constituent of proteins from egg white is ovalbumin (54%), conalbumin (12%), ovomucoid (11%), ovomucin (3.5%), lysozyme (3.4%), ovoinhibitor (1.5%), ovoflavoprotein (0.8%), ovomacroglobulin (0.5%), avidin (0.5%), among smaller fractions of other proteins [46,47]. The content of conalbumin and ovalbumin were similar to our previous work (conalbumin and ovalbumin were 11.511 and 65.383 mg/mL, respectively [33]).…”

Section: Separation Of Proteins From Egg Whitementioning

confidence: 99%

A novel cationic triblock copolymer as noncovalent coating for the separation of proteins by CE

Cao

Zhu

et al. 2011

Electrophoresis

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A novel noncovalent adsorbed coating for CE has been prepared and explored. This coating was based on quaternized poly(2-(dimethylamino)ethyl methacrylate)-block-poly(ethylene oxide)-block-poly(2-(dimethylamino)ethyl methacrylate) (QDED) triblock copolymer which was synthesized by atomic transfer radical polymerization (ATRP) in our laboratory. The polycationic polymer and the negatively charged fused-silica surface attracted each other through electrostatic interactions and hydrogen bonds. It was demonstrated that the coated capillaries provided an electroosmotic flow with reverse direction, and the magnitude of the electroosmotic flow can be modulated by varying the molecular mass of poly(2-(dimethylamino)ethyl methacrylate) (PDMAEMA) block and pH value of the buffer. The effects of the molecular mass of PDMAEMA block in QDED triblock copolymer and pH value of the buffer on the separation of basic proteins were investigated in detail. The triblock copolymer coatings showed higher separation efficiency, better migration time repeatability and would apply to wider range of pH than bare fused-silica capillary when used in separating proteins. Proteins from egg white were also separated through this QDED triblock copolymer-coated capillary. These results demonstrated that the QDED triblock copolymer coatings are suitable for analyzing biosamples.

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Characterization of food proteins by capillary electrophoresis

Cited by 33 publications

References 13 publications

Capillary electrophoresis for the analysis of food proteins of animal origin

Capillary electrophoresis for the analysis of food proteins of animal origin

Simultaneous quantification of five proteins and seven additives in dairy products with a heart-cutting two-dimensional liquid chromatography method

A novel cationic triblock copolymer as noncovalent coating for the separation of proteins by CE

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