Studies on equine milk and comparative studies on equine and bovine milk systems

Show simple item record

dc.contributor.advisor Mulvihill, Daniel M.
dc.contributor.advisor Fox, Patrick F. Uniacke-Lowe, Thérèse 2011-11-24T09:09:13Z 2011-11-24T09:09:13Z 2011-06 2011
dc.identifier.citation Uniacke-Lowe, T., 2011. Studies on equine milk and comparative studies on equine and bovine milk systems. PhD Thesis, University College Cork. en
dc.description.abstract The composition of equine milk differs considerably from that of the milk of the principal dairying species, i.e., the cow, buffalo, goat and sheep. Because equine milk resembles human milk in many respects and is claimed to have special therapeutic properties, it is becoming increasingly popular in Western Europe, where it is produced on large farms in several countries. Equine milk is considered to be highly digestible, rich in essential nutrients and to possess an optimum whey protein:casein ratio, making it very suitable as a substitute for bovine milk in paediatric dietetics. There is some scientific basis for the special nutritional and health-giving properties of equine milk but this study provides a comprehensive analysis of the composition and physico-chemical properties of equine milk which is required to fully exploit its potential in human nutrition. Quantification and distribution of the nitrogenous components and principal salts of equine milk are reported. The effects of the high concentration of ionic calcium, large casein micelles (~ 260 nm), low protein, lack of a sulphydryl group in equine β-lactoglobulin and a very low level of κ-casein on the physico-chemical properties of equine milk are reported. This thesis provides an insight into the stability of equine casein micelles to heat, ethanol, high pressure, rennet or acid. Differences in rennet- and acid-induced coagulation between equine and bovine milk are attributed not only to the low casein content of equine milk but also to differences in the mechanism by which the respective micelles are stabilized. It has been reported that β-casein plays a role in the stabilization of equine casein micelles and proteomic techniques support this view. In this study, equine κ-casein appeared to be resistant to hydrolysis by calf chymosin but equine β-casein was readily hydrolysed. Resolution of equine milk proteins by urea-PAGE showed the multi-phosphorylated isoforms of equine αs- and β-caseins and capillary zone electrophoresis showed 3 to 7 phosphorylated residues in equine β-casein. In vitro digestion of equine β-casein by pepsin and Corolase PP™ did not produce casomorphins BCM-5 or BCM-7, believed to be harmful to human health. Electron microscopy provided very clear, detailed images of equine casein micelles in their native state and when renneted or acidified. Equine milk formed flocs rather then a gel when renneted or acidified which is supported by dynamic oscillatory analysis. The results presented in this thesis will assist in the development of new products from equine milk for human consumption which will retain some of its unique compositional and health-giving properties. en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher University College Cork en
dc.rights © 2011, Thérèse Uniacke-Lowe en
dc.rights.uri en
dc.subject Equine milk en
dc.subject Bovine milk en
dc.subject Physico-chemical properties en
dc.subject Chymosin en
dc.subject Rheology en
dc.subject.lcsh Casein en
dc.subject.lcsh Milk proteins en
dc.subject.lcsh Dairy products--Rheology en
dc.subject.lcsh Milk--Analysis en
dc.title Studies on equine milk and comparative studies on equine and bovine milk systems en
dc.type Doctoral thesis en
dc.type.qualificationlevel Doctoral en
dc.type.qualificationname PhD (Food Chemistry) en
dc.internal.availability Full text available en
dc.description.version Accepted Version en
dc.description.status Not peer reviewed en Food and Nutritional Sciences en

Files in this item

The following license files are associated with this item:

This item appears in the following Collection(s)

Show simple item record

© 2011, Thérèse Uniacke-Lowe Except where otherwise noted, this item's license is described as © 2011, Thérèse Uniacke-Lowe
This website uses cookies. By using this website, you consent to the use of cookies in accordance with the UCC Privacy and Cookies Statement. For more information about cookies and how you can disable them, visit our Privacy and Cookies statement