Natural variation in casein composition of milk

Research output: Thesisinternal PhD, WU

Abstract

Bovine milk contains 3-4 % protein and almost 80% of the milk protein fraction consist of four caseins; αs1-casein, β-casein, αs2-casein and κ-casein. Most of the caseins in milk are assembled in casein micelles, which consist of several thousands of individual casein molecules and salts. The unique structure of casein micelles allows the delivery of large amounts of calcium and phosphate to the neonate. Considerable natural variation in casein content and composition exists between milk samples from individual cows, however the impact of these variations on casein micelle structure and technological properties of dairy products are largely unknown. This study showed that the expression of caseins and their post-translational modification as well as inclusion of calcium in casein micelles are well-balanced processes. Analysis of the genetic background of phosphorylation of αs1-casein with eight or nine phosphate groupsshowed that αs1-casein phosphorylation was regulated by a different set of genes. Also, variation in αs1-casein phosphorylation resulted in changes in the core of casein micelles and was associated with a difference in degradation efficiency by chymosin in milk gels. Another post-translational modification, glycosylation of κ-casein, resulted in changes in the surface of casein micelles. Natural variation in αs1-CN phosphorylationand glycosylation of κ-casein are both relevant factors to consider for optimization of dairy products and the design of future breeding strategies.

Original languageEnglish
QualificationDoctor of Philosophy
Awarding Institution
  • Wageningen University
Supervisors/Advisors
  • van Hooijdonk, Toon, Promotor
  • Huppertz, T., Co-promotor, External person
  • van Valenberg, Hein, Co-promotor
Award date23 May 2014
Place of PublicationWageningen
Publisher
Print ISBNs9789461739445
Publication statusPublished - 2014

Fingerprint

milk composition
casein
micelles
milk
phosphorylation
post-translational modification
glycosylation
dairy products
phosphates
calcium
chymosin
dairy protein

Keywords

  • milk
  • casein
  • milk composition
  • variation

Cite this

Bijl, E. (2014). Natural variation in casein composition of milk. Wageningen: Wageningen University.
Bijl, E.. / Natural variation in casein composition of milk. Wageningen : Wageningen University, 2014. 145 p.
@phdthesis{7f69927734724b759f8bcc9a5e000935,
title = "Natural variation in casein composition of milk",
abstract = "Bovine milk contains 3-4 {\%} protein and almost 80{\%} of the milk protein fraction consist of four caseins; αs1-casein, β-casein, αs2-casein and κ-casein. Most of the caseins in milk are assembled in casein micelles, which consist of several thousands of individual casein molecules and salts. The unique structure of casein micelles allows the delivery of large amounts of calcium and phosphate to the neonate. Considerable natural variation in casein content and composition exists between milk samples from individual cows, however the impact of these variations on casein micelle structure and technological properties of dairy products are largely unknown. This study showed that the expression of caseins and their post-translational modification as well as inclusion of calcium in casein micelles are well-balanced processes. Analysis of the genetic background of phosphorylation of αs1-casein with eight or nine phosphate groupsshowed that αs1-casein phosphorylation was regulated by a different set of genes. Also, variation in αs1-casein phosphorylation resulted in changes in the core of casein micelles and was associated with a difference in degradation efficiency by chymosin in milk gels. Another post-translational modification, glycosylation of κ-casein, resulted in changes in the surface of casein micelles. Natural variation in αs1-CN phosphorylationand glycosylation of κ-casein are both relevant factors to consider for optimization of dairy products and the design of future breeding strategies.",
keywords = "melk, case{\"i}ne, melksamenstelling, variatie, milk, casein, milk composition, variation",
author = "E. Bijl",
note = "WU thesis 5749",
year = "2014",
language = "English",
isbn = "9789461739445",
publisher = "Wageningen University",
school = "Wageningen University",

}

Bijl, E 2014, 'Natural variation in casein composition of milk', Doctor of Philosophy, Wageningen University, Wageningen.

Natural variation in casein composition of milk. / Bijl, E.

Wageningen : Wageningen University, 2014. 145 p.

Research output: Thesisinternal PhD, WU

TY - THES

T1 - Natural variation in casein composition of milk

AU - Bijl, E.

N1 - WU thesis 5749

PY - 2014

Y1 - 2014

N2 - Bovine milk contains 3-4 % protein and almost 80% of the milk protein fraction consist of four caseins; αs1-casein, β-casein, αs2-casein and κ-casein. Most of the caseins in milk are assembled in casein micelles, which consist of several thousands of individual casein molecules and salts. The unique structure of casein micelles allows the delivery of large amounts of calcium and phosphate to the neonate. Considerable natural variation in casein content and composition exists between milk samples from individual cows, however the impact of these variations on casein micelle structure and technological properties of dairy products are largely unknown. This study showed that the expression of caseins and their post-translational modification as well as inclusion of calcium in casein micelles are well-balanced processes. Analysis of the genetic background of phosphorylation of αs1-casein with eight or nine phosphate groupsshowed that αs1-casein phosphorylation was regulated by a different set of genes. Also, variation in αs1-casein phosphorylation resulted in changes in the core of casein micelles and was associated with a difference in degradation efficiency by chymosin in milk gels. Another post-translational modification, glycosylation of κ-casein, resulted in changes in the surface of casein micelles. Natural variation in αs1-CN phosphorylationand glycosylation of κ-casein are both relevant factors to consider for optimization of dairy products and the design of future breeding strategies.

AB - Bovine milk contains 3-4 % protein and almost 80% of the milk protein fraction consist of four caseins; αs1-casein, β-casein, αs2-casein and κ-casein. Most of the caseins in milk are assembled in casein micelles, which consist of several thousands of individual casein molecules and salts. The unique structure of casein micelles allows the delivery of large amounts of calcium and phosphate to the neonate. Considerable natural variation in casein content and composition exists between milk samples from individual cows, however the impact of these variations on casein micelle structure and technological properties of dairy products are largely unknown. This study showed that the expression of caseins and their post-translational modification as well as inclusion of calcium in casein micelles are well-balanced processes. Analysis of the genetic background of phosphorylation of αs1-casein with eight or nine phosphate groupsshowed that αs1-casein phosphorylation was regulated by a different set of genes. Also, variation in αs1-casein phosphorylation resulted in changes in the core of casein micelles and was associated with a difference in degradation efficiency by chymosin in milk gels. Another post-translational modification, glycosylation of κ-casein, resulted in changes in the surface of casein micelles. Natural variation in αs1-CN phosphorylationand glycosylation of κ-casein are both relevant factors to consider for optimization of dairy products and the design of future breeding strategies.

KW - melk

KW - caseïne

KW - melksamenstelling

KW - variatie

KW - milk

KW - casein

KW - milk composition

KW - variation

M3 - internal PhD, WU

SN - 9789461739445

PB - Wageningen University

CY - Wageningen

ER -

Bijl E. Natural variation in casein composition of milk. Wageningen: Wageningen University, 2014. 145 p.