Absolute Quantitation of β-Lactoglobulin by Protein Liquid Chromatography−Mass Spectrometry and Its Application to Different Milk Products

Czerwenka, Christoph; Maier, Irene; Potocnik, Natascha; Pittner, Fritz; Lindner, Wolfgang

doi:10.1021/ac062367d

Cited by 53 publications

(37 citation statements)

References 24 publications

(40 reference statements)

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“…With a similar approach, internal standard β-Lg was used to quantify non-bovine β-Lg in different milk-derived products [120]. The use of "bottom-up" methods, such as SILAC, ICAT, and iTRAQ, for quantitative analysis in proteomics has progressively increased [121,122].…”

Section: Allergen Quantification Methodsmentioning

confidence: 99%

Allergenicity of Milk Proteins

Caira¹,

Pizzano²,

Picariello³

et al. 2012

Milk Protein

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Section: Allergen Quantification Methodsmentioning

confidence: 99%

Allergenicity of Milk Proteins

Caira¹,

Pizzano²,

Picariello³

et al. 2012

Milk Protein

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“…Several calibration dependencies for determination of the percentage of bovine milk in either ovine or caprine milk samples should be utilized, using the coupling of LC and MS [2,[37][38][39][40][41]. The tested linear dependences of the percentage of addition of bovine milk to ovine, and/or caprine milk are specified in Table 3.…”

Section: Quantitative Analysis Of Milk Mixturesmentioning

confidence: 99%

Capillary electrophoresis‐mass spectrometry – a fast and reliable tool for the monitoring of milk adulteration

et al. 2008

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The development of a rapid, simple and accurate analytical method aimed at the detection and quantification of bovine milk in either ovine or caprine milk samples by means of CE-MS analyses of whey proteins with high-ionic strength and presence of acidic running buffer is described. The high-ionic strength buffer was used in order to minimize the problems with the adsorption of the proteins onto the fused-silica capillary wall. The acidic running electrolyte, pH 1.9, was used to support the production of positive ions in electrospray. Highly linear dependences of the ratio of the sum of non-bovine beta-lactoglobulins (ovine or caprine) to the total beta-lactoglobulins in milk mixture (bovine plus ovine or bovine plus caprine) vs. the volume percentage of added bovine milk in ovine (or caprine) milk were obtained. This technique allowed the fast and reliable evaluation of milk adulteration. The amount of bovine milk added into the "non-bovine" ones can be well within the concentration range of 5-95%.

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“…Recently, a reliable LC–MS or LC–MS/MS method has been developed for microlevel determination of α‐lactalbumin and β‐lactoglobulin in dairy products. Quantification of whey proteins using this technique could be achieved by measuring the intact protein (at protein level) or signature peptides after protein digestion (at peptide level) . Bovine β‐lactoglobulin in dairy products was quantified at protein level by LC–MS using β‐lactoglobulins from caprine and bubaline as the internal standard (IS) .…”

Section: Introductionmentioning

confidence: 99%

A combined tryptic peptide and winged peptide internal standard approach for the determination of α‐lactalbumin in dairy products by ultra high performance liquid chromatography with tandem mass spectrometry

Lai

Zhang

Chen

et al. 2015

J of Separation Science

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A robust ultra high performance liquid chromatography with tandem mass spectrometry method at peptide level was established for measuring α-lactalbumin in various dairy products. An isotope-labeled winged peptide (VKKILDKVG*INYW*LAHKALCSEKL) with extra amino acids of the sequence of signature peptide concatenated at each end as the internal standard was spiked in samples to participate in the whole tryptic digestion process. The peptide VG*INYW*LAHK that resulted from the isotope-labeled winged peptide was used as the final isotopically labeled internal standard of the α-lactalbumin signature peptide (VGINYWLAHK) during the quantitative analysis. The contents of α-lactalbumin in samples were calculated based on the equimolar relationship between the α-lactalbumin protein and signature peptide. The optimized molar ratio of trypsin to protein (1:60) and enzymatic digestion time (5 h) could not only improve the digestion efficiency and reduce the cost, but also minimize the period of sample pretreatment. Considering the robustness of the current method using the isotopically labeled internal standard and acceptable measurement cost, its application may promote the development of nutrient investigation and quality control of α-lactalbumin in dairy products. This protein analysis method might provide a new reference strategy for food analysis and quantitative protein analysis.

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Absolute Quantitation of β-Lactoglobulin by Protein Liquid Chromatography−Mass Spectrometry and Its Application to Different Milk Products

Cited by 53 publications

References 24 publications

Allergenicity of Milk Proteins

Allergenicity of Milk Proteins

Capillary electrophoresis‐mass spectrometry – a fast and reliable tool for the monitoring of milk adulteration

A combined tryptic peptide and winged peptide internal standard approach for the determination of α‐lactalbumin in dairy products by ultra high performance liquid chromatography with tandem mass spectrometry

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