Determination of lactoferrin in bovine milk, colostrum and infant formulas by optical biosensor analysis

Indyk, Harvey E.; Filonzi, Enríco L.

doi:10.1016/j.idairyj.2004.09.003

Cited by 65 publications

(51 citation statements)

References 40 publications

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“…The same results of LF content in cows' milk were reported by Zimecki and Kruzel [36]. Different factors may contribute to variation of LF concentration such as different animal health status, level of BSA, lactation stage as well as daily milk production, some studies reported a big variation of LF content in milk among individual cows, for example from 0.06-1.0 mgmL -1 LF [28,49].…”

Section: Lf Concentration In Liquid Wheysupporting

confidence: 75%

The Influence of Heat Treatment in Liquid Whey at Various pH on Immunoglobulin G and Lactoferrin from Yak and Cows’ Colostrum/Milk

Xiaoyun¹,

Lin²

2015

J Food Process Technol

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Yak milk is gaining popularity yearly, as a source of nutritious, immune, less likely to cause allergies than cows' milk and a means of generating income, though ranked behind bovine milk in China. The main objective of the research was to compare the Immunoglobulin G (IgG) and Lactoferrin (LF) concentrations of liquid whey from Yak and dairy Cows' colostrum or milk. Thereafter, the thermal stability of liquid whey was evaluated by measuring the concentration change in IgG and LF using an ELISA technique, as influenced by temperature and pH after centrifugation.IgG and LF concentrations in liquid whey from colostrums both in yak and cow were significantly higher (p<0.05) compared to milk. IgG did not differ significantly (p>0.05) between yak and cow's milk, as well as between yak and cow's colostrum. Also, LF content was not significant different between yak and cow milk. However, LF concentration was significantly higher in cows' colostrum than in yak. With reference to IgG content, yak breed observed to produce high quality colostrum for all samples tested compared to cows.The extent of IgG and LF denaturation confirmed to increase with increased protein concentration, temperature and pH change near to pI. Colostral IgG and LF were more denatured compared to milk in both yak and dairy cows. There was significant (p<0.05) influence of pH changes resulted in either partial or complete denaturation or increased tendency to aggregate, which was removed during centrifugation. Liquid whey less affected at lower pH and at mild heat temperatures.

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Section: Lf Concentration In Liquid Wheysupporting

confidence: 75%

The Influence of Heat Treatment in Liquid Whey at Various pH on Immunoglobulin G and Lactoferrin from Yak and Cows’ Colostrum/Milk

Xiaoyun¹,

Lin²

2015

J Food Process Technol

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“…Several authors have reported an increased concentration of lactoferrin in colostrum (Pakkanen and Aalto 1997;Hahn et al 1998;Zhang et al 2002Zhang et al , 2011Sobczuk-Szul et al 2013). Reiter (1978) reported that the concentration of lactoferrin in colostrum is 30-fold higher than that in milk, while Indyk and Filonzi (2005) observed a 100-fold higher concentration of lactoferrin in colostrum than in milk. It should be noted that, in addition to stage of lactation, lactoferrin concentration is significantly correlated with SCC, level of BSA and volume of milk produced (Cheng et al 2008).…”

Section: Proteinmentioning

confidence: 99%

Composition and properties of bovine colostrum: a review

McGrath

Fox

McSweeney

et al. 2015

Dairy Sci. & Technol.

299

263

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Colostrum is the initial milk secreted by mammals following parturition, the composition and physicochemical properties of which are highly dynamic and variable. The composition and physicochemical properties of colostrum during the initial postpartum period has not been systematically reviewed for many years, although the topic remains of interest both to milk producers and processors. In this article, the current understanding of the composition of colostrum, i.e. carbohydrates, proteins, growth factors, enzymes, enzyme inhibitors, nucleotides and nucleosides, cytokines, fats, vitamins and minerals, is reviewed. In addition, the physicochemical properties, i.e. pH and buffering capacity, colour, density and specific gravity, osmotic pressure, somatic cell count, properties of casein micelles, ethanol stability and rennet coagulation properties are discussed, as well as the effects of heat-treating colostrum.

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“…An XK16 water-jacketed chromatography column (GE Healthcare), connected to an For column breakthrough studies, lactoferrin concentrations were determined using an optical biosensor analysis as described by Indyk and Filzoni [35], using a surface plasmon resonance technique (SPR) on a Biacore 3000 instrument (Biacore , Uppsala, Sweden). Raw whole milk samples were centrifuged at 4800 g (Min-Spin, Ependorf, Hamburg, Germany) for 2 minutes to remove fat and filtered using a 5 µm filter (Sartorious AG, Goettingen, Germany) before serial dilutions (to 2000x) were made in 500 mM HBS-EP buffer (10 mM HEPES, pH 7.4 with 3 mM EDTA and 0.005% (v/v) surfactant P20).…”

Section: Raw Milk Was Obtained From Greenfield Dairy Farm Site (Dexcementioning

confidence: 99%

Capture of lactoferrin and lactoperoxidase from raw whole milk by cation exchange chromatography

Fee

Chand

2006

Separation and Purification Technology

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The production of high-value dairy proteins such as lactoferrin and lactoperoxidase normally requires extensive pre-treatments of milk to remove fat and caseins by centrifugation, precipitation, Ca 2+ chelation and/or filtration. Similarly, fat and caseins are normally removed prior to capture of recombinant proteins from the milk of transgenic animals. Such pre-treatments can result in significant loss of protein yield and/or activity. In this paper we demonstrate that it is possible to pass significant quantities of raw, untreated milk through a 5 cm high chromatography column packed with SP Sepharose Big Beads™ (GE Healthcare, Uppsala, Sweden) without exceeding the maximum allowable backpressure, provided that the processing temperature is kept nominally around milking temperature (35 to 37 o C).Results show that more than 100 column volumes of raw milk could be loaded at 300 cm/hr before breakthrough of lactoperoxidase occurred. The dynamic capacity for adsorbing lactoferrin and lactoperoxidase simultaneously under these conditions was approximately 48.6 mg/mL of resin. Minor leakage (4.6% of the feed concentration) of lactoferrin occurred throughout the loading process but major breakthrough occurred only after approximately 100 column volumes was loaded.

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Determination of lactoferrin in bovine milk, colostrum and infant formulas by optical biosensor analysis

Cited by 65 publications

References 40 publications

The Influence of Heat Treatment in Liquid Whey at Various pH on Immunoglobulin G and Lactoferrin from Yak and Cows’ Colostrum/Milk

The Influence of Heat Treatment in Liquid Whey at Various pH on Immunoglobulin G and Lactoferrin from Yak and Cows’ Colostrum/Milk

Composition and properties of bovine colostrum: a review

Capture of lactoferrin and lactoperoxidase from raw whole milk by cation exchange chromatography

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