Bovine β-casein: Isolation, properties and functionality. A review

Atamer, Zeynep; Post, A. E.; Schubert, Thomas; Holder, Aline; Boom, R.M.; Hinrichs, Jörg

doi:10.1016/j.idairyj.2016.11.010

Cited by 79 publications

(37 citation statements)

References 90 publications

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“…Skim milk is used for the extraction of casein. This can be done by applying a purely physical process or a combination of physical and biochemical processes [13]. Examples of the applied methods are namely: (i) precipitation by rennet (rennet-casein) [25], by mineral acids such as hydrochloric or sulphuric acid (mineral acid-casein) [16] or using a lactic starter (lactic acid-casein) [15] and (ii) separation using a membrane filtration process such as microfiltration [26].…”

Section: Resultsmentioning

confidence: 99%

“…In this study, for the production of casein, a cross-flow membrane filtration process was used to obtain micellar casein concentrate. In comparison to other chemical and thermal processes applied for the separation of the individual fractions [13], no modification of the casein micelles occurs and the functional characteristics of the casein protein does not change [27]. Therefore, caseins obtained by using this method can be considered as "native".…”

Section: Resultsmentioning

confidence: 99%

“…Since the beginning of 1950s, several methods, either at small or large scale, have been developed for the isolation of casein fractions, especially β-casein [13]. Some of the pioneering work involves ion-exchange chromatography [14], electrophoresis [15], selective precipitation [16], gel chromatography [17] and liquid chromatography [18].…”

Section: Introductionmentioning

confidence: 99%

“…Some of the pioneering work involves ion-exchange chromatography [14], electrophoresis [15], selective precipitation [16], gel chromatography [17] and liquid chromatography [18]. The processes for the isolation of the fractions use mainly selective solubility and precipitation as well as cross flow membrane filtration (microfiltration and ultrafiltration) [13]. Considerable progress has been made in isolating and purifying β-casein.…”

Section: Introductionmentioning

confidence: 99%

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2017

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Abstract:The fractions of caseins (αs-, β-and κ-) are widely used in food applications due to their physiochemical properties as well as their bio-and techno-functional properties. Especially, β-casein fraction is a precursor having a variety of bioactive peptides such as antihypertensive and opioid. Different methods have been established in isolating and purifying the casein fractions, particularly on β-casein isolation. However, the obtained yield for each fraction still requires further improvement. The aim of this study was to increase the yield and purity of the fractions by constructing a set of experiments on technical scale and determining the main process parameters. Based on our previous studies on laboratory scale, a method for the technical scale isolation of casein fractions from micellar casein powder was developed. A comparable yield and purity values for β-casein were obtained.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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2017

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“…Extraction of β-casein involves three consecutive steps: separation of whole casein from milk, and isolation of β-casein; micelle disruption by acidification, chelation or cooling, and purification; washing, precipitation and separation [100]. …”

Section: Casein Delivery Particlesmentioning

confidence: 99%

Potential of Casein as a Carrier for Biologically Active Agents

2017

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Casein is the collective name for a family of milk proteins. In bovine milk, casein comprises four peptides: αS1, αS2, β, and κ, differing in their amino acid, phosphorus and carbohydrate content but similar in their amphiphilic character. Hydrophilic and hydrophobic regions of casein show block distribution in the protein chain. Casein peptides carry negative charge on their surface as a result of phosphorylation and tend to bind nanoclusters of amorphous calcium phosphate. Due to these properties, in suitable conditions, casein molecules agglomerate into spherical micelles. The high content of casein in milk (2.75 %) has made it one of the most popular proteins. Novel research techniques have improved understanding of its properties, opening up new applications. However, casein is not just a dietary protein. Its properties promise new and unexpected applications in science and the pharmaceutical and functional food industries. One example is an encapsulation of health-related substances in casein matrices. This review discusses gelation, coacervation, self-assembly and reassembly of casein peptides as means of encapsulation. We highlight information on encapsulation of health-related substances such as drugs and dietary supplements inside casein micro- and nanoparticles.

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