Comparison of capillary electrophoresis and isoelectric focusing for analysis of casein/caseinate addition in processed cheeses

Miralles, Beatriz; Krause, Ingolf; Ramos, Mercedes; Amigo, Lourdes

doi:10.1016/j.idairyj.2005.10.025

Cited by 15 publications

(3 citation statements)

References 13 publications

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“…While both methods showed comparable recovery of isoelectric casein, CIEF provided a significantly better recovery of sodium caseinate than CZE. On the other hand, CZE achieved higher precision of the analysis [127].…”

Section: Dairy Proteinsmentioning

confidence: 97%

Capillary electrophoresis of proteins 2005–2007

Dolnı́k¹

2007

Electrophoresis

152

106

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This review article with 239 references describes recent developments in capillary electrophoresis of proteins, and covers the two years since the previous review (V. Dolník, Electrophoresis 2006, 27, 126-141) through spring 2007. It includes topics related to CE of proteins, such as sample pretreatment, wall coatings, improving separation, various forms of detection, and special electrophoretic techniques including ACE, CIEF, capillary ITP, and CEC. The paper describes applications of CE to analysis of proteins in real-world samples including human body fluids, food and agricultural samples, protein pharmaceuticals and recombinant protein preparations.

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Section: Dairy Proteinsmentioning

confidence: 97%

Capillary electrophoresis of proteins 2005–2007

Dolnı́k¹

2007

Electrophoresis

152

106

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“…Casein is important for the food industry due to its functional properties, and it provides a suitable food structure and consistency, mostly by the ability to emulsify fat and bind water. As casein is released from the gut more slowly due its compact composition, it demonstrates very high leucine deposition, which can last up to 7 h (Dangin et al , ; Miralles et al , ).…”

Section: Introductionmentioning

confidence: 99%

The effect of native and polymerised whey protein isolate addition on surface and microstructural properties of processed cheeses and their meltability determined by Turbiscan

Nastaj

Terpiłowski

Sołowiej

2020

Int J of Food Sci Tech

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The aim of this paper was to investigate the effect of whey protein isolate (WPI) and polymerised whey protein isolate (WPP) addition on physicochemical properties of processed cheese with partial fat replacement. Surface properties were determined by advancing (h a ) and receding (h r ) contact angles, apparent free surface energy (c s ). Roughness measurements, cheese meltability and Turbiscan Stability Index (TSI) were evaluated by Turbiscan. Higher WPP concentrations produced the more hydrophobic surfaces of the samples. Conversely, increase in WPI addition promoted the hydrophilic cheese surfaces. The effect of roughness was much larger for samples containing WPI. The increase in protein addition caused a decrease in meltability and an increase in stability of cheeses. The optical and confocal images have proved that cheeses with WPP demonstrated more packed and denser structure in comparison to samples with WPI.Surface properties of processed cheese M. Nastaj et al.

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“…Several methods are used to analyse the protein fractions, namely, electrophoretic techniques (Carretero et al 1994; Park & Jin, 1998), isoelectric focusing (IEF) (Miralles et al 2006; Criscione et al 2009; Giambra et al 2010) and capillary electrophoresis (De Block et al 2003; Clément et al 2006; Criscione et al 2009). High-performance liquid chromatography (HPLC) by ion-exchange (Andrews et al 1985), hydrophobic interactions (Goheen & Gibbins, 2000; Ferreira et al 2001), gel filtration (Grupta, 1983), reversed phase (Ferreira & Caçote, 2003; Polidori et al 2009) and immunological methods (Haza et al 1996).…”

mentioning

confidence: 99%

Size exclusion and reversed-phase high-performance liquid chromatography/UV for routine control of thermal processing of cows' and donkey milk major proteins

Pinho

Martins

Petisca

et al. 2012

Journal of Dairy Research

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Cows' and donkey milks (raw and thermally processed) and respective whey were analysed for quantification of major proteins. Two different chromatographic approaches, size exclusion (SE-HPLC) and reversed-phase high performance liquid chromatography (RP-HPLC) both coupled to UV detection were used. Usefulness of these methods for routine control of the effect of thermal processing was evaluated. The external standard method was used to calibrate the SE-HPLC and RP-HPLC systems. Concerning quantification of β-lactoglobulin (β-lg), α-lactalbumin (α-la), lysozyme (lys), and total casein (cn), no significant differences between results obtained by SE-HPLC and by RP-HPLC (t-test, P>0·05) were observed for raw milks and whey. Heating of cows' milk promoted aggregation of denatured proteins as observed by SE-HPLC, whereas α-la and β-lg from donkey milk were stable to thermal processing at 100 °C (5 min). Lys was quantified in donkey raw milk and whey however, in thermally processed donkey milk lys was denatured and could not be quantified by HPLC.

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Comparison of capillary electrophoresis and isoelectric focusing for analysis of casein/caseinate addition in processed cheeses

Cited by 15 publications

References 13 publications

Capillary electrophoresis of proteins 2005–2007

Capillary electrophoresis of proteins 2005–2007

The effect of native and polymerised whey protein isolate addition on surface and microstructural properties of processed cheeses and their meltability determined by Turbiscan

Size exclusion and reversed-phase high-performance liquid chromatography/UV for routine control of thermal processing of cows' and donkey milk major proteins

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