Stability of milk protein concentrate suspensions to in-container sterilisation heating conditions

Crowley, Shane V.; Boudin, Marion; Chen, Biye; Gazi, Inge; Huppertz, Thom; Kelly, Alan L.; O’Mahony, James A.

doi:10.1016/j.idairyj.2015.05.009

Cited by 35 publications

(35 citation statements)

References 10 publications

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“…Hence, calcium ion activity alone could not be the dominating factor explaining the differences between the UHT stability of these samples. Similar results on ionic calcium and heat stability behavior of milk protein concentrate suspensions (MPC80) was reported by Crowley et al (2015) .…”

Section: A C C E P T E D Accepted Manuscriptsupporting

confidence: 87%

Comparison of ultra high temperature (UHT) stability of high protein milk dispersions prepared from milk protein concentrate (MPC) and conventional low heat skimmed milk powder (SMP)

Singh

Prakash

2019

Journal of Food Engineering

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Section: A C C E P T E D Accepted Manuscriptsupporting

confidence: 87%

Comparison of ultra high temperature (UHT) stability of high protein milk dispersions prepared from milk protein concentrate (MPC) and conventional low heat skimmed milk powder (SMP)

Singh

Prakash

2019

Journal of Food Engineering

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“…The highest soluble casein to whey protein ratio is observed when milk is heated at pH 6.4 and then concentrated, while heat treatments at pH 6.7 and 7.0 result in higher ratio of whey protein to soluble casein (Krishnakutti Nair et al, 2013). In reconstituted MPC, κ-CN dissociation decreases with increasing protein content and increases with pH (Crowley et al, 2015a).…”

Section: Heat Stability In Concentrated Systemsmentioning

confidence: 95%

“…Spray-dried MPC powders obtained after membrane filtration range in protein concentration from 35 to more than 85 g per 100 g of solids, with a corresponding decrease in the amount of lactose and minerals, depending on the extent of concentration and DF. The solubility of the MPC powders differs substantially, depending on processing conditions, protein concentration, ionic composition (Crowley et al, 2015a).…”

Section: Concentration Of Milkmentioning

confidence: 99%

“…With the utilization of MPC as ingredients in dairy products, interest has increased in understanding the effect of protein concentration on the bulk properties of milk concentrates, isolates, or casein micelle suspensions and their properties during reconstitution (Karlsson et al, 2005;Crowley et al, 2015a;Gazi and Huppertz, 2015). Regardless of the mode of concentration, the viscosity of casein micelle suspensions increases with concentration, with a dramatic change from a Newtonian to a non-Newtonian behavior (Karlsson et al, 2007;Dahbi et al, 2010;Krishnakutti Nair et al, 2014).…”

Section: Colloidal Properties Of Casein Micelles In Concentrated Milkmentioning

confidence: 99%

“…Excessive calcium activity has been attributed as a problem in heat stability of MPC with high protein concentration (Crowley et al, 2015a). Recently, calcium-depleted MPC have been suggested as possible value added for ready to drink and enteral formulations (Eshpari et al, 2014;Marella et al, 2015;Pandalaneni et al, 2018); however, it is important to also control the reconstitution conditions, as this will further modify the ionic balance (Eshpari et al, 2014(Eshpari et al, , 2015Lin et al, 2018;Liu et al, 2019).…”

Section: Heat Stability In Concentrated Systemsmentioning

confidence: 99%

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Invited review: Understanding the behavior of caseins in milk concentrates

Corredig

Nair²,

Liu

et al. 2019

Journal of Dairy Science

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The colloidal properties of the casein micelles play a major role in the structural properties of milk protein concentrates. Because of their great technological importance, the structural-functional relationships of casein micelles have been studied for decades in skim milk; however, novel ingredients are now available with higher protein concentrations and varying in composition. The colloidal behavior of caseins in these systems is not fully understood. Concentrates prepared with membrane technologies, and subjected to pre-or postmodifications that affect their technological functionality, have become increasingly widespread. This has created large opportunities for innovation and generation of value-added ingredients. The manner in which caseins interact with themselves and the other components in these concentrates will affect the structure of the final matrix. During concentration by filtration, the interparticle distance between the micelles decreases considerably, increasing their spatial correlation and decreasing their diffusivity. Rearrangements occur due to changes in environmental conditions, such as ionic composition, osmotic stress, shear, pH, or heating temperature. This will have important consequences on bulk viscosity of the concentrates, as well as on the mode of formation of structures' building blocks. This paper aims at highlighting some of the important factors affecting the colloidal structure of casein micelles, their destabilization and network formation, namely, processing history, volume fraction, composition of the serum phase, and ionic equilibrium. Understanding these factors will lead to a better quality control of dairy ingredients and to the development of a new generation of ingredients with targeted functionality.

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Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

Dumpler

Wohlschläger

Kulozik

2016

Dairy Sci. & Technol.

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Heat treatment of concentrated milk systems for preservation and long shelf life or at least a sufficient removal of food pathogens prior to spray drying is a crucial step due to the decreasing stability of these systems toward heat compared to unconcentrated milk. Heat-induced coagulation is observed when temperature-time combinations for the achievement of certain microbial inactivation effects are higher than the heat and colloidal stability of the concentrated milk system allows. In this work, the effects of direct steam injection on the stability of casein micelles in concentrated skim milk (CSM) of 18, 23, and 27% total non-fat solids, heat-treated by direct steam injection (DSI), were investigated. Quantitative differential centrifugation for the separation of aggregates, casein micelles, dissociated submicellar particles, and soluble proteins and subsequent analysis of caseins and whey proteins within these fractions by RP-HPLC were applied. Quantitative separation was monitored by particle size measurements. The dissociation of κ-casein as well as an increase in casein micelle hydrodynamic radius were observed to increase with increasing total solid content of CSM, heat treatment time, and temperature. Heat-induced dissociation of β-Lg-κcasein complexes at a critical level of 30-35% was found to induce severe coagulation of κ-casein-depleted calcium-sensitive casein micelles in CSM heated by DSI. Dissociated and aggregated proteins were found to be present as distinct colloidal particle classes differing in size from casein micelles.

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Stability of milk protein concentrate suspensions to in-container sterilisation heating conditions

Cited by 35 publications

References 10 publications

Comparison of ultra high temperature (UHT) stability of high protein milk dispersions prepared from milk protein concentrate (MPC) and conventional low heat skimmed milk powder (SMP)

Comparison of ultra high temperature (UHT) stability of high protein milk dispersions prepared from milk protein concentrate (MPC) and conventional low heat skimmed milk powder (SMP)

Invited review: Understanding the behavior of caseins in milk concentrates

Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

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