Return to search

Enzymic Milk Coagulation: Casein Micelle Aggregation and Curd Formation

Enzymic milk coagulation was monitored by measuring changes in curd firmness and apparent absorbance of undiluted milk. Detection of coagulation, visually or rheologically, occurred after the milk changes from a system of aggregating particles to an extended space network. This change was observed as a shoulder in apparent absorbance plots and coagulation time was defined as the critical point in the aggregation process analogously to non-linear condensation polymerization reactions. It corresponds to the inflexion point during the period when apparent absorbance was rapidly increasing and can be calculated by fitting curd firmness data to an exponential equation.
Addition of calcium chloride to milk reduced coagulation time with a minimum occurring at .05M calcium. Also, curd firmness increased with a maximum at .02M calcium. It appears that calcium affects all stages of coagulation: proteolysis, micelle aggregation, and gelation. When bulk culture media was added to milk, the pH of the media had a greater effect on coagulation time than did presence of phosphate in the media.
Non-specific proteolytic activity of milk coagulants affects the initial rate of curd firming but not the maximum firmness. The more proteolytic the enzyme the slower the curd firming rate. This can be used to rapidly assay for pepsin content of bovine rennets.

Identiferoai:union.ndltd.org:UTAHS/oai:digitalcommons.usu.edu:etd-6369
Date01 May 1983
CreatorsMcMahon, Donald J.
PublisherDigitalCommons@USU
Source SetsUtah State University
Detected LanguageEnglish
Typetext
Formatapplication/pdf
SourceAll Graduate Theses and Dissertations
RightsCopyright for this work is held by the author. Transmission or reproduction of materials protected by copyright beyond that allowed by fair use requires the written permission of the copyright owners. Works not in the public domain cannot be commercially exploited without permission of the copyright owner. Responsibility for any use rests exclusively with the user. For more information contact digitalcommons@usu.edu.

Page generated in 0.0027 seconds