Interaction between lactoferrin and casein micelles in skimmed milk

Croguennec, Thomas; Li, Na; Phelebon, Laure; Garnier-Lambrouin, Fabienne; Gésan-Guiziou, Geneviève

doi:10.1016/j.idairyj.2012.06.003

Cited by 33 publications

(12 citation statements)

References 33 publications

(43 reference statements)

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“…[ 3 , 5 ]. Native LPO and LF are positively charged and hence bind partially to the negatively charged casein micelles in BRM, leading to a lower recovery yield in MF permeate as compared to native IgG, despite the former having a lower molecular mass of 70–80 and 78 kDa, as compared to that of 146–163 kDa for the IgG [ 35 , 36 ]. Therefore, considering the production efficiency as well as the recovery yield of major and minor serum proteins, a 100 nm ceramic membrane was selected for subsequent experiments.…”

Section: Resultsmentioning

confidence: 99%

Transmission of Major and Minor Serum Proteins during Microfiltration of Skim Milk: Effects of Pore Diameters, Concentration Factors and Processing Stages

Liu

et al. 2021

Foods

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Effects of pore diameters (100, 50, and 20 nm), concentration factors (1–8) and processing stages (1–5) on the transmission of major serum proteins (β-lactoglobulin and α-lactalbumin) and minor serum proteins (immunoglobulin (Ig) G, IgA, IgM, lactoferrin (LF), lactoperoxidase (LPO), xanthine oxidase (XO)) during ceramic microfiltration (MF) of skim milk were studied. Holstein skim milk was microfiltered at a temperature of 50 °C, a transmembrane pressure of 110 kPa and a crossflow velocity of 6.7 m/s, using a tubular single stainless steel module that consisted of three ceramic tubes, each with 19 channels (3.5 mm inner diameter) and a length of 0.5 m. For MF with 100 nm and 50 nm pore diameters, the recovery yield of major serum proteins in permeate was 44.3% and 44.1%, while the recovery yield of minor serum proteins was slightly less by 0%–8% than 50 nm MF. MF with 20 nm pore diameters showed a markedly lower (by 12%–45%) recovery yield for both major and minor serum proteins, corresponding with its lower membrane flux. Flux sharply decreased with an increasing concentration factor (CF) up to four, and thereafter remained almost unchanged. Compared to the decrease (88%) of flux, the transmission of major and minor serum proteins was decreased by 4%–15% from CF = one to CF = eight. With increasing processing stages, the flux gradually increased, and the recovery yield of both major and minor proteins in the permeate gradually decreased and reached a considerably low value at stage five. After four stages of MF with 100 nm pore diameter and a CF of four for each stage, the cumulative recovery yield of major serum proteins, IgG, IgA, IgM, LF, LPO, and XO reached 95.7%, 90.8%, 68.5%, 34.1%, 15.3%, 39.1% and 81.2% respectively.

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Section: Resultsmentioning

confidence: 99%

Transmission of Major and Minor Serum Proteins during Microfiltration of Skim Milk: Effects of Pore Diameters, Concentration Factors and Processing Stages

Liu

et al. 2021

Foods

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“…One of these attraction forces was related to its high isoelectric point (pI = 7.8-8.9) so acquiring a positive net charge at natural milk pH (6.8) that enable it to form a loose electrostatic interaction with the negatively charged protein molecules e. g. casein micelle (pI = 4.6). [6,8] unlike all other published techniques this study was targeted to counteract this attraction force by using simplest vacuum driven downstream purification which is manually packed using SP-Sepharose. [9][10][11] upon using skimmed milk samples, lactoferrin was found to be readily adsorbed to cation exchange resin (e. g. SP-Sepharose), and consequently released in a purified single fraction through salt gradient addition.…”

Section: Introductionmentioning

confidence: 99%

“…A distinctive characteristic of lactoferrin is its ability to interact with caseins, [5,6] whey proteins, and milk fat globules at natural milk pH [7] thus hiders its direct determination in presence of these interfering molecules. One of these attraction forces was related to its high isoelectric point (pI=7.8–8.9) so acquiring a positive net charge at natural milk pH (6.8) that enable it to form a loose electrostatic interaction with the negatively charged protein molecules e. g. casein micelle (pI=4.6) [6,8] . unlike all other published techniques this study was targeted to counteract this attraction force by using simplest vacuum driven downstream purification which is manually packed using SP‐Sepharose [9–11] .…”

Section: Introductionmentioning

confidence: 99%

Quality Assessment of Lactoferrin in some Marketed Nutraceuticals Derived from Milk using Validated Analytical Methods

Mohamed¹,

Al‐Ghobashy

Fouad³

et al. 2020

ChemistrySelect

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In recent years, lactoferrin has received great attention for its nutritional and immunological uses. As minor element its inclusion in milk with other milk proteins hindered its direct determination. So downstream purification of lactoferrin from skimmed milk was optimized using vacuum driven approach. The purity of lactoferrin was monitored using gel electrophoresis along with validated RP‐HPLC and SE‐HPLC assays. Factors affecting lactoferrin during milk processing, handling and storage were also investigated. These methods were applicable on various products in Egyptian market to withdraw our attention towards careful monitoring during in‐process quality control which showed deleterious reactions affecting of the milk proteins during processing causing significant denaturation so as to track concentration, purity and stability of lactoferrin.

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“…Moreover, Lf can interact with the negatively charged proteins. In milk, about half of the Lf is combined with negatively charged casein micelles through electrostatic attraction (Croguennec, Li, Phelebon, Garnier-Lambrouin, & Gésan-Guiziou, 2012), higher levels of which is bound to smaller casein micelles, indicating that Lf is mainly bonded to the surface κ-casein layer (Anema & De Kruif, 2013). After adding Lf to milk, the attachment of Lf on the surface of casein micelles initially increased the size and turbidity of casein micelles, followed by the disintegration of casein micelles (Anema & De Kruif, 2012a).…”

Section: Introductionmentioning

confidence: 99%

Formation of lactoferrin/sodium caseinate complexes and their adsorption behaviour at the air/water interface

Zhao

2017

Food Chemistry

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This research investigated the complexation behaviour between lactoferrin (Lf) and sodium caseinate (NaCas) before and after heat treatment. The results showed that heating facilitated their interaction and different complexes were formed at different Lf/NaCas ratios. The presence of low concentrations of NaCas resulted in the rapid precipitation of Lf, while no precipitation was observed at the NaCas concentrations higher than Lf/NaCas ratio of 2:1. The formed complexes at the ratio of 2:1 have an average diameter of 194±9.0nm and they exhibited a great capacity in lowering the air/water interfacial tension. Further increase of NaCas concentration to ratios of 1:1 and 1:2 resulted in the formation of smaller complexes with average diameters of 60±2.5nm. The complexes formed at these two ratios showed similar adsorption behaviour at the air/water interface and they exhibited lower capacity in decreasing the interfacial tension than the ratio of 2:1.

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Interaction between lactoferrin and casein micelles in skimmed milk

Cited by 33 publications

References 33 publications

Transmission of Major and Minor Serum Proteins during Microfiltration of Skim Milk: Effects of Pore Diameters, Concentration Factors and Processing Stages

Transmission of Major and Minor Serum Proteins during Microfiltration of Skim Milk: Effects of Pore Diameters, Concentration Factors and Processing Stages

Quality Assessment of Lactoferrin in some Marketed Nutraceuticals Derived from Milk using Validated Analytical Methods

Formation of lactoferrin/sodium caseinate complexes and their adsorption behaviour at the air/water interface

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