Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making

Highly concentrated micellar casein concentrate (HC-MCC), a potential ingredient for cheese making, containing ~20% casein with ~70% of serum proteins removed by microfiltration, and diafiltration of skim milk, and then further concentrated by vacuum evaporation. The objectives of this research were...

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Main Author: Lu, Ying
Format: Others
Published: DigitalCommons@USU 2016
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Online Access:https://digitalcommons.usu.edu/etd/5003
https://digitalcommons.usu.edu/cgi/viewcontent.cgi?article=6045&context=etd
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spelling ndltd-UTAHS-oai-digitalcommons.usu.edu-etd-60452019-10-13T05:34:46Z Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making Lu, Ying Highly concentrated micellar casein concentrate (HC-MCC), a potential ingredient for cheese making, containing ~20% casein with ~70% of serum proteins removed by microfiltration, and diafiltration of skim milk, and then further concentrated by vacuum evaporation. The objectives of this research were to investigate solubilization, cold gelation, rennet coagulation properties of recombined HC-MCC and cream for its use in cheese making. In Chapter 3, either mixing thawed HC-MCC in water at high temperature (~50C) or addition of trisodium citrate can achieve complete dispersion and more than 80% solubility of HC-MCC in water (3% protein). Overnight storage helps to fully disperse HC-MCC, but only reaches ~30% of solubility at 20C. Cold-gelation of HCMCC is thermally reversible and reducing protein levels in HC-MCC can decrease its CGT. The HC-MCC with less than 16% of protein does not gel at 5C. We propose that cold-gelation of HC-MCC occurs when the kinetic energy of the casein micelles is sufficiently reduced to inhibit their mobility in relation to adjacent casein micelles. In Chapter 4, the recombined concentrated milk (RCM) by mixing thawed frozen HC-MCC and cream with 12% casein at pH 6.6 does not gel until cooled below 12°C. Addition of either sodium citrate or high levels of calcium increased CGT, although low levels of calcium did not impact CGT. Cold gelation of RCM was thermally reversible, even when citrate was added to partially chelate calcium. We propose that cold gelation of RCM occurs when protein strands that have been partially released from the casein micelles entangle, restrict their mobility and form a fine stranded gel network. The RCM at a casein level of 12% (wt/wt) has potential for use in cheese making. In Chapter 5, reducing rennet level can increase coagulation time of RCM (11% casein) without impact on curd firmness or firming rate. Decreased coagulation temperature helps to increase coagulation time and decrease curd firmness rate, but also increases the initial viscosity of RCM. Pre-acidified RCM has no advantage in increasing coagulation time, decreasing curd firmness or firming rate. Microstructure of RCM and its coagulum indicates that the increased curd firmness probably results from the highly inter-linked and longer protein strands in RCM curd. Reducing rennet level can be applied to slow down rennet coagulation of RCM (11% casein) in cheese making. 2016-05-01T07:00:00Z text application/pdf https://digitalcommons.usu.edu/etd/5003 https://digitalcommons.usu.edu/cgi/viewcontent.cgi?article=6045&context=etd Copyright 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 Andrew Wesolek (andrew.wesolek@usu.edu). All Graduate Theses and Dissertations DigitalCommons@USU casein micelle coagulation gelation microfiltration microstructure rheology Food Science
collection NDLTD
format Others
sources NDLTD
topic casein micelle
coagulation
gelation
microfiltration
microstructure
rheology
Food Science
spellingShingle casein micelle
coagulation
gelation
microfiltration
microstructure
rheology
Food Science
Lu, Ying
Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making
description Highly concentrated micellar casein concentrate (HC-MCC), a potential ingredient for cheese making, containing ~20% casein with ~70% of serum proteins removed by microfiltration, and diafiltration of skim milk, and then further concentrated by vacuum evaporation. The objectives of this research were to investigate solubilization, cold gelation, rennet coagulation properties of recombined HC-MCC and cream for its use in cheese making. In Chapter 3, either mixing thawed HC-MCC in water at high temperature (~50C) or addition of trisodium citrate can achieve complete dispersion and more than 80% solubility of HC-MCC in water (3% protein). Overnight storage helps to fully disperse HC-MCC, but only reaches ~30% of solubility at 20C. Cold-gelation of HCMCC is thermally reversible and reducing protein levels in HC-MCC can decrease its CGT. The HC-MCC with less than 16% of protein does not gel at 5C. We propose that cold-gelation of HC-MCC occurs when the kinetic energy of the casein micelles is sufficiently reduced to inhibit their mobility in relation to adjacent casein micelles. In Chapter 4, the recombined concentrated milk (RCM) by mixing thawed frozen HC-MCC and cream with 12% casein at pH 6.6 does not gel until cooled below 12°C. Addition of either sodium citrate or high levels of calcium increased CGT, although low levels of calcium did not impact CGT. Cold gelation of RCM was thermally reversible, even when citrate was added to partially chelate calcium. We propose that cold gelation of RCM occurs when protein strands that have been partially released from the casein micelles entangle, restrict their mobility and form a fine stranded gel network. The RCM at a casein level of 12% (wt/wt) has potential for use in cheese making. In Chapter 5, reducing rennet level can increase coagulation time of RCM (11% casein) without impact on curd firmness or firming rate. Decreased coagulation temperature helps to increase coagulation time and decrease curd firmness rate, but also increases the initial viscosity of RCM. Pre-acidified RCM has no advantage in increasing coagulation time, decreasing curd firmness or firming rate. Microstructure of RCM and its coagulum indicates that the increased curd firmness probably results from the highly inter-linked and longer protein strands in RCM curd. Reducing rennet level can be applied to slow down rennet coagulation of RCM (11% casein) in cheese making.
author Lu, Ying
author_facet Lu, Ying
author_sort Lu, Ying
title Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making
title_short Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making
title_full Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making
title_fullStr Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making
title_full_unstemmed Investigation of Solubilization, Cold Gelation, and Rennet Coagulation Properties of Highly Concentrated Micellar Casein Concentrate for Use in Cheese Making
title_sort investigation of solubilization, cold gelation, and rennet coagulation properties of highly concentrated micellar casein concentrate for use in cheese making
publisher DigitalCommons@USU
publishDate 2016
url https://digitalcommons.usu.edu/etd/5003
https://digitalcommons.usu.edu/cgi/viewcontent.cgi?article=6045&context=etd
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