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

Rauh, Valentin; Johansen, Lene Buhelt; Bakman, Mette; Ipsen, Richard; Paulsson, Marie; Larsen, Lotte Bach; Hammershøj, Marianne

doi:10.1111/1471-0307.12265

Cited by 37 publications

(24 citation statements)

References 18 publications

(55 reference statements)

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“…Siciliano, Mazzeo, Arena, Renzone, and Scaloni (2013) and Siciliano, Rega, Amoresano, and Pucci (2000) reported that the extent of lactosylation accounts for 30% and 70% of the protein in UHT and powdered milk respectively. In a recent study, UHT milk stored up to 6 months at 20 °C showed that the extent and the rate of lactosylation correlated with the number of Lys residues in the different proteins, and a linear correlation with furosine was observed (Rauh et al, 2015); furosine is formed from lactulosyl-lysine by acidic digestion during analysis. Theoretically, lactose can attach to any site of lysine in milk proteins and affect their functional and nutritional properties.…”

Section: Lactosylationmentioning

confidence: 95%

Proteomics of major bovine milk proteins: Novel insights

Deeth

Larsen

2017

International Dairy Journal

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Milk proteomics covers the identification, characterisation and quantification of milk proteins. Its applications vary from the basic composition of milk proteins to their post-translational modifications (PTMs), occurring naturally or via processing and storage. Through the combination of liquid chromatography or two-dimensional gel electrophoresis with advanced mass spectrometry, milk proteomics has revealed PTMs that affect milk protein structural and functional properties. This review discusses detection by proteomics-based methods with special emphasis on natural and process induced PTMs in the major bovine milk proteins. The review covers the importance of milk proteomics in determining PTMs, especially those formed by heat treatment and during storage, and highlights some breakthroughs in PTM studies. Furthermore, aspects and applications of quantitative proteomics on milk proteins and bioinformatics are covered. ___________________________________________________________________________________ 1998). Milk from other species have been included in other reviews (Cunsolo, Muccilli, Saletti & Foti, 2011; El-Salam, 2014) and will not be included here. Overall, bovine milk proteins and related peptides can be classified into four different groups: caseins (α S1-, α S2-, βand κ-caseins), serum proteins [αlactalbumin (α-La), β-lactoglobulin (β-Lg), bovine serum albumin (BSA), immunoglobulins (Igs) and a range of other minor whey proteins], proteose peptones (low molecular weight peptides derived from caseins and well as proteose peptone component 3, called PP3) and membrane [mostly milk fat globule membrane (MFGM)] proteins (Table 1).

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Section: Lactosylationmentioning

confidence: 95%

Proteomics of major bovine milk proteins: Novel insights

Deeth

Larsen

2017

International Dairy Journal

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“…The dilution of the sample with guanidine buffer gave a better resolution of individual proteins compared to dissolution of milk samples in urea buffer as used by Rauh et al (2014), Bonizzi et al (2009), and Visser et al (1991). In the case of whey proteins, higher heat intensity leads to a pre-peak formation due to non-enzymatic glycosylation of whey proteins with lactose as described by Rauh et al (2015). By using this method, we could quantitatively follow the heatinduced aggregation process of individual caseins at heated different temperatures and heat holding times at constant non-fat total solid content of 27% as presented in Fig.…”

Section: Heat-induced Aggregation Of Caseins In Concentrated Skim Milkmentioning

confidence: 99%

Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

Dumpler

Wohlschläger

Kulozik

2016

Dairy Sci. & Technol.

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Heat treatment of concentrated milk systems for preservation and long shelf life or at least a sufficient removal of food pathogens prior to spray drying is a crucial step due to the decreasing stability of these systems toward heat compared to unconcentrated milk. Heat-induced coagulation is observed when temperature-time combinations for the achievement of certain microbial inactivation effects are higher than the heat and colloidal stability of the concentrated milk system allows. In this work, the effects of direct steam injection on the stability of casein micelles in concentrated skim milk (CSM) of 18, 23, and 27% total non-fat solids, heat-treated by direct steam injection (DSI), were investigated. Quantitative differential centrifugation for the separation of aggregates, casein micelles, dissociated submicellar particles, and soluble proteins and subsequent analysis of caseins and whey proteins within these fractions by RP-HPLC were applied. Quantitative separation was monitored by particle size measurements. The dissociation of κ-casein as well as an increase in casein micelle hydrodynamic radius were observed to increase with increasing total solid content of CSM, heat treatment time, and temperature. Heat-induced dissociation of β-Lg-κcasein complexes at a critical level of 30-35% was found to induce severe coagulation of κ-casein-depleted calcium-sensitive casein micelles in CSM heated by DSI. Dissociated and aggregated proteins were found to be present as distinct colloidal particle classes differing in size from casein micelles.

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“…Molecular weight of proteins in concentrated milk was determined by liquid chromatographyelectrospray ionization time-of-flight mass spectrometry (LC-ESI-TOF-MS) (Agilent Technologies, Santa Clara, CA, USA). Sample preparation was performed according to the protocol, mentioned by Rauh et al, 2015 [73]. Briefly, 200 µL of concentrated milk was treated with 20 µL of 0.5 M DTT, 1 mL of 100 mM trisodium citrate, and 6 M urea at temperature 30 • C for 1 h in a thermostat.…”

Section: Understanding Of Molecular Weight Of Proteins In Concentratementioning

confidence: 99%

“…It may explain by the fact that the electrophoretic mobility of caseins in electrophoresis gel is lower than expected from their molar mass [108]. It may be justified by the fact that phosphorylation [109] and lactosylation of caseins [73] change the migration of casein molecules in electrophoresis gel. However, in SDS-PAGE, several protein aggregates were present, they were absent in mass-spectrum.…”

Section: Molecular Weight Of Different Proteins In Concentrated Milk mentioning

confidence: 99%

Production of Liquid Milk Protein Concentrate with Antioxidant Capacity, Angiotensin Converting Enzyme Inhibitory Activity, Antibacterial Activity, and Hypoallergenic Property by Membrane Filtration and Enzymatic Modification of Proteins

et al. 2020

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Liquid milk protein concentrate with different beneficial values was prepared by membrane filtration and enzymatic modification of proteins in a sequential way. In the first step, milk protein concentrate was produced from ultra-heat-treated skimmed milk by removing milk serum as permeate. A tubular ceramic-made membrane with filtration area 5 × 10−3 m2 and pore size 5 nm, placed in a cross-flow membrane house, was adopted. Superior operational strategy in filtration process was herein: trans-membrane pressure 3 bar, retention flow rate 100 L·h−1, and implementation of a static turbulence promoter within the tubular membrane. Milk with concentrated proteins from retentate side was treated with the different concentrations of trypsin, ranging from 0.008–0.064 g·L−1 in individual batch-mode operations at temperature 40 °C for 10 min. Subsequently, inactivation of trypsin in reaction was done at a temperature of 70 °C for 30 min of incubation. Antioxidant capacity in enzyme-treated liquid milk protein concentrate was measured with the Ferric reducing ability of plasma assay. The reduction of angiotensin converting enzyme activity by enzyme-treated liquid milk protein concentrate was measured with substrate (Abz-FRK(Dnp)-P) and recombinant angiotensin converting enzyme. The antibacterial activity of enzyme-treated liquid milk protein concentrate towards Bacillus cereus and Staphylococcus aureus was tested. Antioxidant capacity, anti-angiotensin converting enzyme activity, and antibacterial activity were increased with the increase of trypsin concentration in proteolytic reaction. Immune-reactive proteins in enzyme-treated liquid milk protein concentrate were identified with clinically proved milk positive pooled human serum and peroxidase-labelled anti-human Immunoglobulin E. The reduction of allergenicity in milk protein concentrate was enzyme dose-dependent.

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

Cited by 37 publications

References 18 publications

Proteomics of major bovine milk proteins: Novel insights

Proteomics of major bovine milk proteins: Novel insights

Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

Production of Liquid Milk Protein Concentrate with Antioxidant Capacity, Angiotensin Converting Enzyme Inhibitory Activity, Antibacterial Activity, and Hypoallergenic Property by Membrane Filtration and Enzymatic Modification of Proteins

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