Origin and Evolution of the Major Constituents of Milk

Oftedal, Olav T.

doi:10.1007/978-1-4614-4714-6_1

Cited by 19 publications

(24 citation statements)

References 193 publications

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“…This subject is considered to be outside the scope of this book and the interested reader is referred to Mepham et al (1992), Martin et al (2013a, b), Oftedal 2013 andSingh et al (2014). Such knowledge permits the genetic engineering of milk proteins with respect to the transfer of genes from one species to another, the over-expression of a particular desirable protein(s), the elimination of certain undesirable proteins, changing the amino acid sequence by point mutations to modify the functional properties of the protein or transfer of a milk protein gene to a plant or microbial host.…”

Section: Structure and Expression Of Milk Protein Genesmentioning

confidence: 98%

Milk Proteins

Fox¹,

Uniacke‐Lowe²,

McSweeney³

et al. 2015

Dairy Chemistry and Biochemistry

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Section: Structure and Expression Of Milk Protein Genesmentioning

confidence: 98%

Milk Proteins

Fox¹,

Uniacke‐Lowe²,

McSweeney³

et al. 2015

Dairy Chemistry and Biochemistry

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“…Bear milk contains little lactose but a high level of total sugars (mainly OSs) −1.7 and 28.6 g/kg, respectively (Oftedal 2013). Bear milk contains little lactose but a high level of total sugars (mainly OSs) −1.7 and 28.6 g/kg, respectively (Oftedal 2013).…”

Section: Oligosaccharidesmentioning

confidence: 99%

“…This subject is considered to be outside the scope of this book and the interested reader is referred to Mepham et al (1992), Martin et al (2013a, b), Oftedal 2013 andSingh et al (2014). This subject is considered to be outside the scope of this book and the interested reader is referred to Mepham et al (1992), Martin et al (2013a, b), Oftedal 2013 andSingh et al (2014).…”

Section: Structure and Expression Of Milk Protein Genesmentioning

confidence: 99%

Dairy Chemistry and Biochemistry

Fox¹,

Uniacke‐Lowe²,

McSweeney³

et al. 2015

568

570

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“…This hypothesis is supported by the fact that milk is supersaturated with calcium, and phospho-serine residues are conserved in mammalian species (Oftedal, 2013). …”

Section: Introductionmentioning

confidence: 98%

The association of low-molecular-weight hydrophobic compounds with native casein micelles in bovine milk

Cheema

Mohan

Campagna

et al. 2015

Journal of Dairy Science

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The agreed biological function of the casein micelles in milk is to carry minerals (calcium, magnesium, and phosphorus) from mother to young along with amino acids for growth and development. Recently, native and modified casein micelles were used as encapsulating and delivery agents for various hydrophobic low-molecular-weight probes. The ability of modified casein micelles to bind certain probes may derive from the binding affinity of native casein micelles. Hence, a study with milk from single cows was conducted to further elucidate the association of hydrophobic molecules into native casein micelles and further understand their biological function. Hydrophobic and hydrophilic extraction followed by ultraperformance liquid chromatography-high resolution mass spectrometry analysis were performed over protein fractions obtained from size exclusion fractionation of raw skim milk. Hydrophobic compounds, including phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylethanolamine, and sphingomyelin, showed strong association exclusively to casein micelles as compared with whey proteins, whereas hydrophilic compounds did not display any preference for their association among milk proteins. Further analysis using liquid chromatography-tandem mass spectrometry detected 42 compounds associated solely with the casein-micelles fraction. Mass fragments in tandem mass spectrometry identified 4 of these compounds as phosphatidylcholine with fatty acid composition of 16:0/18:1, 14:0/16:0, 16:0/16:0, and 18:1/18:0. These results support that transporting low-molecular-weight hydrophobic molecules is also a biological function of the casein micelles in milk.

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Origin and Evolution of the Major Constituents of Milk

Cited by 19 publications

References 193 publications

Milk Proteins

Milk Proteins

Dairy Chemistry and Biochemistry

The association of low-molecular-weight hydrophobic compounds with native casein micelles in bovine milk

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