Characterization of casein lactosylation by capillary electrophoresis and mass spectrometry

Steffan, W.; Balzer, Hartmut H.; Lippert, Frank; Sambor, B. C.; Bradbury, Allan G. W.; Henle, Thomas

doi:10.1007/s00217-005-0177-9

Cited by 11 publications

(9 citation statements)

References 10 publications

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“…The formation of lactosylated b-casein A1 and A2 during heating of processed cheese was found to correlate with the furosine content. This indicated CZE of casein could be used to monitor early Mailard reaction in dairy products [133].…”

Section: Dairy Proteinsmentioning

confidence: 98%

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: 98%

Capillary electrophoresis of proteins 2005–2007

Dolnı́k¹

2007

Electrophoresis

152

106

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“…These reactions occur naturally or are induced especially during heat treatment or storage (Siciliano et al 2000;Le et al 2013). Glycation can be followed by evaluation of the number of the free amino groups of lysyl residues and more precisely by mass spectrometry (Steffan et al 2006;Siciliano et al 2013). Courthaudon et al (1989) reported that glycation of casein with glucose, fructose, galactose, mannose, maltose, or lactose improved their solubility especially close to their isoelectric point (but it remained unchanged at neutral and alkaline pH and decreased at low pH values).…”

Section: Reaction With Sugarsmentioning

confidence: 99%

Modifications of structures and functions of caseins: a scientific and technological challenge

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

264

133

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Casein molecules are used in food industry as ingredients. They can be used as isolated forms and under micellar form consisting in an association of different casein molecules and calcium phosphate. In this review, after a brief reminder of the main characteristics of casein molecules and casein micelles, the modifications of caseins induced by physical, chemical, and enzymatic actions are reported. The resulting new physicochemical properties (mineral and casein compositions, charge, hydrophobicity, aggregation state, and morphology) and techno-functionalities (heat stability, viscosity, gelation, emulsifying, and foaming properties) are described and discussed with a special attention paid to the results obtained in our laboratory since several decades.

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“…This is in line with Steffan et al . (), who found a linear correlation between unmodified β‐CN and furosine in processed cheese, although only a singly lactosylated β‐CN was detected (Steffan et al . ).…”

Section: Resultsmentioning

confidence: 99%

“…(), who found a linear correlation between unmodified β‐CN and furosine in processed cheese, although only a singly lactosylated β‐CN was detected (Steffan et al . ). For the higher lactosylated proteins such as α S1 ‐CN 8 P and β‐lg, the best correlations were achieved with an exponential fit resulting in R 2 = 0.93 and R 2 = 0.95, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…A quantitative correlation in wet milk systems with furosine concentration could only be achieved for a singly lactosylated β‐CN in processed cheese (Steffan et al . ). In dry milk systems, a quantitative relationship between furosine concentration and lactosylated peptides originating from whey proteins was established for milk powder (Le et al .…”

Section: Introductionmentioning

confidence: 97%

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Protein lactosylation in UHT milk during storage measured by Liquid Chromatography–Mass Spectrometry and quantification of furosine

Rauh

Johansen

Bakman

et al. 2015

Int J of Dairy Tech

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The initial stage of the Maillard reaction, protein lactosylation, occurs during heat treatment of milk and continues during subsequent storage. We compared the initial lactosylation as well as the rate of lactosylation of milk proteins during storage in UHT milk subjected to direct or indirect heat treatment using liquid chromatography (LC) coupled with electrospray injection mass spectrometry (ESI-MS). Furosine content was used as an overall marker to allow for a quantitative correlation of lactosylation measured by LC-ESI-MS in the UHT milks. Protein lactosylation increased during the storage period of 6 months at 20°C. Both the initial extent and the rate of lactosylation positively correlated with the number of lysine residues in the different proteins. An exponential or linear correlation with furosine concentration could be established for major and minor lactosylated proteins, respectively.

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Characterization of casein lactosylation by capillary electrophoresis and mass spectrometry

Cited by 11 publications

References 10 publications

Capillary electrophoresis of proteins 2005–2007

Capillary electrophoresis of proteins 2005–2007

Modifications of structures and functions of caseins: a scientific and technological challenge

Protein lactosylation in UHT milk during storage measured by Liquid Chromatography–Mass Spectrometry and quantification of furosine

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