Proteomic study on the stability of proteins in bovine, camel, and caprine milk sera after processing

Lina Zhang, Sjef Boeren, Marcel Smits, Toon van Hooijdonk, Jacques Vervoort, Kasper Hettinga

Research output: Contribution to journalArticleAcademicpeer-review

16 Citations (Scopus)

Abstract

Milk proteins have been shown to be very sensitive to processing. This study aims to investigate the changes of the bovine, camel, and caprine milk proteins after freezing, pasteurization (62 °C, 30 min), and spray drying by proteomic techniques, filter-aided sample preparation (FASP) and dimethyl labeling followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). A total of 129, 125, and 74 proteins were quantified in bovine, camel, and caprine milk sera, respectively. The milk serum protein content decreased significantly after freezing, pasteurization, or spray drying, which can be ascribed to the removal of protein aggregates by the pH adjustment and ultracentrifugation during sample preparation. Some of the immune-related proteins were heat-sensitive, such as lactoferrin (LTF), glycosylation-dependent cell adhesion molecule 1 (GLYCAM1), and lactadherin (MFGE8), with losses of approximately 25% to 85% after pasteurization and 85% to 95% after spray drying. α-Lactalbumin (LALBA), osteopontin (SPP1), and whey acidic protein (WAP) were relatively heat stable with losses of 10% to 50% after pasteurization and 25% to 85% after spray drying. The increase of some individual proteins in concentration after freezing may be caused by the proteins originating from damaged milk fat globules and somatic cells. GLYCAM1 decreased significantly after pasteurization in bovine and camel milk but this protein is relatively stable in caprine milk. In conclusion, milk proteins changed differently in concentration after different processing steps, as well as among different species.

LanguageEnglish
Pages104-111
JournalFood Research International
Volume82
DOIs
Publication statusPublished - 2016

Fingerprint

camel milk
Pasteurization
Camelus
Protein Stability
Milk Proteins
goat milk
pasteurization
whey
Proteomics
proteomics
spray drying
Milk
milk proteins
milk
Freezing
Serum
freezing
camels
glycosylation
cell adhesion

Keywords

  • Bovine
  • Camel
  • Caprine
  • Milk serum protein stability
  • Processing
  • Proteomics

Cite this

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title = "Proteomic study on the stability of proteins in bovine, camel, and caprine milk sera after processing",
abstract = "Milk proteins have been shown to be very sensitive to processing. This study aims to investigate the changes of the bovine, camel, and caprine milk proteins after freezing, pasteurization (62 °C, 30 min), and spray drying by proteomic techniques, filter-aided sample preparation (FASP) and dimethyl labeling followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). A total of 129, 125, and 74 proteins were quantified in bovine, camel, and caprine milk sera, respectively. The milk serum protein content decreased significantly after freezing, pasteurization, or spray drying, which can be ascribed to the removal of protein aggregates by the pH adjustment and ultracentrifugation during sample preparation. Some of the immune-related proteins were heat-sensitive, such as lactoferrin (LTF), glycosylation-dependent cell adhesion molecule 1 (GLYCAM1), and lactadherin (MFGE8), with losses of approximately 25{\%} to 85{\%} after pasteurization and 85{\%} to 95{\%} after spray drying. α-Lactalbumin (LALBA), osteopontin (SPP1), and whey acidic protein (WAP) were relatively heat stable with losses of 10{\%} to 50{\%} after pasteurization and 25{\%} to 85{\%} after spray drying. The increase of some individual proteins in concentration after freezing may be caused by the proteins originating from damaged milk fat globules and somatic cells. GLYCAM1 decreased significantly after pasteurization in bovine and camel milk but this protein is relatively stable in caprine milk. In conclusion, milk proteins changed differently in concentration after different processing steps, as well as among different species.",
keywords = "Bovine, Camel, Caprine, Milk serum protein stability, Processing, Proteomics",
author = "Lina Zhang and Sjef Boeren and Marcel Smits and {van Hooijdonk}, Toon and Jacques Vervoort and Kasper Hettinga",
year = "2016",
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journal = "Food Research International",
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Proteomic study on the stability of proteins in bovine, camel, and caprine milk sera after processing. / Zhang, Lina; Boeren, Sjef; Smits, Marcel; van Hooijdonk, Toon; Vervoort, Jacques; Hettinga, Kasper.

In: Food Research International, Vol. 82, 2016, p. 104-111.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Proteomic study on the stability of proteins in bovine, camel, and caprine milk sera after processing

AU - Zhang, Lina

AU - Boeren, Sjef

AU - Smits, Marcel

AU - van Hooijdonk, Toon

AU - Vervoort, Jacques

AU - Hettinga, Kasper

PY - 2016

Y1 - 2016

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AB - Milk proteins have been shown to be very sensitive to processing. This study aims to investigate the changes of the bovine, camel, and caprine milk proteins after freezing, pasteurization (62 °C, 30 min), and spray drying by proteomic techniques, filter-aided sample preparation (FASP) and dimethyl labeling followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). A total of 129, 125, and 74 proteins were quantified in bovine, camel, and caprine milk sera, respectively. The milk serum protein content decreased significantly after freezing, pasteurization, or spray drying, which can be ascribed to the removal of protein aggregates by the pH adjustment and ultracentrifugation during sample preparation. Some of the immune-related proteins were heat-sensitive, such as lactoferrin (LTF), glycosylation-dependent cell adhesion molecule 1 (GLYCAM1), and lactadherin (MFGE8), with losses of approximately 25% to 85% after pasteurization and 85% to 95% after spray drying. α-Lactalbumin (LALBA), osteopontin (SPP1), and whey acidic protein (WAP) were relatively heat stable with losses of 10% to 50% after pasteurization and 25% to 85% after spray drying. The increase of some individual proteins in concentration after freezing may be caused by the proteins originating from damaged milk fat globules and somatic cells. GLYCAM1 decreased significantly after pasteurization in bovine and camel milk but this protein is relatively stable in caprine milk. In conclusion, milk proteins changed differently in concentration after different processing steps, as well as among different species.

KW - Bovine

KW - Camel

KW - Caprine

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KW - Processing

KW - Proteomics

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M3 - Article

VL - 82

SP - 104

EP - 111

JO - Food Research International

T2 - Food Research International

JF - Food Research International

SN - 0963-9969

ER -