Proteomic comparison of equine and bovine milks on renneting.
Abstract: Rennet-induced coagulation of bovine milk is a complex mechanism in which chymosin specifically hydrolyzes κ-casein, the protein responsible for the stability of the casein micelle. In equine milk, this mechanism is still unclear, and the protein targets of chymosin are unknown. To reveal the proteins involved, the rennetability of equine milk by calf chymosin was examined using gel-free and gel-based proteomic analysis and compared to bovine milk. RP-HPLC analysis of bovine and equine milks showed the release of several peptides following chymosin incubation. The hydrolyses of equine and bovine casein by chymosin were different, and the major peptides produced from equine milk were identified by mass spectrometry as fragments of β-casein. Using two-dimensional electrophoresis, equine β-casein was confirmed as the main target of calf chymosin over 24 h at 30 °C and pH 6.5. The gel-based analysis of equine milk discriminated between the different individual proteins and provided information on the range of isoforms of each protein as a result of post-translational modifications, as well as positively identified for the first time several isoforms of κ-casein. In comparison to bovine milk, κ-casein isoforms in equine milk were not involved in chymosin-induced coagulation. The intensity of equine β-casein spots decreased following chymosin addition, but at a slower rate than bovine κ-casein.
Publication Date: 2013-03-05 PubMed ID: 23414207DOI: 10.1021/jf3045846Google Scholar: Lookup
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- Comparative Study
- Journal Article
Summary
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This research aims to compare the process of rennet-induced coagulation between equine and bovine milks. The main finding is that in equine milk, unlike in bovine milk, β-casein, not κ-casein protein, is the main target of calf chymosin.
Renneting Process in Milk
- The study examines the process of rennet-induced coagulation of milk, a phenomenon crucial to cheese production. In bovine milk, the protein called κ-casein is responsible for the stability of casein micelle, which is a complex formed by protein particles in milk. Chymosin, an enzyme, specifically hydrolyzes or breaks the bond of κ-casein, leading to the coagulation of milk.
- However, in equine milk, the protein targets for chymosin are not yet clearly identified, hence the study aims to decipher this.
Proteomic Analysis
- Both gel-based and gel-free proteomic analysis were utilized in this study. Proteomic analysis is a technique used for studying proteins present in a sample, their composition, structure and behavior.
- Equine milk was analysed by calf chymosin, and it was compared to the process in bovine milk.
- RP-HPLC (Reverse-Phase High Performance Liquid Chromatography) analysis was conducted on both bovine and equine milks, which revealed the release of several peptides following chymosin incubation. Peptides are smaller parts of the protein which are formed by breaking the protein molecule.
- It was found that the process of hydrolysis or breaking down of casein by chymosin is different in equine and bovine milk.
Key Findings
- Using mass spectrometry and other analytical methods, it was identified that the major peptides produced from the equine milk were fragments of β-casein, making it the main target of calf chymosin. This differs from bovine milk where κ-casein is the main target.
- Findings also reveal that unlike bovine milk, κ-casein isoforms in equine milk were not involved in chymosin-induced coagulation, and the coagulation process seemed to progress at a slower rate in equine milk.
- The changes and presence of several isoforms of κ-casein in equine milk were recorded for the first time as a result of this research.
Cite This Article
APA
Uniacke-Lowe T, Chevalier F, Hem S, Fox PF, Mulvihill DM.
(2013).
Proteomic comparison of equine and bovine milks on renneting.
J Agric Food Chem, 61(11), 2839-2850.
https://doi.org/10.1021/jf3045846 Publication
Researcher Affiliations
- School of Food and Nutritional Sciences, University College , Cork, Ireland.
MeSH Terms
- Animals
- Biocatalysis
- Caseins / chemistry
- Cattle
- Chromatography, High Pressure Liquid
- Chymosin / chemistry
- Electrophoresis, Gel, Two-Dimensional
- Horses
- Milk / chemistry
- Milk Proteins / chemistry
- Proteomics
Citations
This article has been cited 4 times.- Faccia M, D'Alessandro AG, Summer A, Hailu Y. Milk Products from Minor Dairy Species: A Review.. Animals (Basel) 2020 Jul 24;10(8).
- Faccia M, Gambacorta G, Martemucci G, Difonzo G, D'Alessandro AG. Chemical-Sensory Traits of Fresh Cheese Made by Enzymatic Coagulation of Donkey Milk.. Foods 2019 Dec 23;9(1).
- Gu J, Li Q, Chen B, Xu C, Zheng H, Zhou Y, Peng Z, Hu Z, Wang B. Species identification of Bombyx mori and Antheraea pernyi silk via immunology and proteomics.. Sci Rep 2019 Jun 28;9(1):9381.
- Brinkmann J, Koudelka T, Keppler JK, Tholey A, Schwarz K, Thaller G, Tetens J. Characterization of an Equine α-S2-Casein Variant Due to a 1.3 kb Deletion Spanning Two Coding Exons.. PLoS One 2015;10(10):e0139700.
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