Effects of calcium chelating agents on the solubility of milk protein concentrate

McCarthy, Noel A.; Power, Orla M.; Wijayanti, Heni; Kelly, Philip M.; Mao, Like; Fenelon, Mark A.

doi:10.1111/1471-0307.12408

Cited by 60 publications

(43 citation statements)

References 28 publications

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“…In addition to chelating calcium, SHMP can crosslink with casein proteins because of its 6 negative charges and homogeneous charge distribution. When SHMP is present in higher concentrations, it also forms calciumcasein phosphate complexes in the presence of calcium (McCarthy et al, 2017) as shown in Figure 1 (mechanism II). Understanding the role of calcium, caseins, and SHMP as a chelator improves our understanding of the changes in the physical and functional properties of high-protein dairy beverages.…”

Section: Resultsmentioning

confidence: 99%

Influence of milk protein concentrates with modified calcium content on enteral dairy beverage formulations: Physicochemical properties

Pandalaneni

Amamcharla

Marella

et al. 2018

Journal of Dairy Science

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Because of their high protein and low lactose content, milk protein concentrates (MPC) are typically used in the formulation of ready-to-drink beverages. Calcium-mediated aggregation of proteins during storage is one of the main reasons for loss of storage stability of these beverages. Control and calcium-reduced MPC [20% calcium-reduced (MPC-20) and 30% calcium-reduced (MPC-30)] were used to evaluate the physicochemical properties in this study. This study was conducted in 2 phases. In phase I, 8% protein solutions were prepared by reconstituting the 3 MPC and adjusting the pH to 7. These solutions were divided into 3 equal parts, 0, 0.15, or 0.25% sodium hexametaphosphate (SHMP) was added, and the solutions were homogenized. In phase II, enteral dairy beverage formulations containing MPC and a mixture of gums, maltodextrin, and sugar were evaluated following the same procedure used in phase I. In both phases, heat stability, apparent viscosity, and particle size were compared before and after heat treatment at 140°C for 15 s. In the absence of SHMP, MPC-20 and MPC-30 exhibited the highest heat coagulation time at 30.9 and 32.8 min, respectively, compared with the control (20.9 min). In phase II, without any addition of SHMP, MPC-20 exhibited the highest heat coagulation time of 9.3 min compared with 7.1 min for control and 6.2 min for MPC-30. An increase in apparent viscosity and a decrease in particle size of reconstituted MPC solutions in phases I and II with an increase in SHMP concentration was attributed to casein micelle dissociation caused by calcium chelation. This study highlights the potential for application of calcium-reduced MPC in dairy-based ready-to-drink and enteral nutrition beverage formulations to improve their heat stability.

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Section: Resultsmentioning

confidence: 99%

Influence of milk protein concentrates with modified calcium content on enteral dairy beverage formulations: Physicochemical properties

Pandalaneni

Amamcharla

Marella

et al. 2018

Journal of Dairy Science

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“…To reduce the concentration of Ca 2+ , calcium-binding salts (CBS) such as salts of phosphoric and citric acids can be added prior to processing to increase heat stability and reduce fouling (Lewis, 2011). The effects of CBS addition on protein structure and heat stability have been studied in various types of milk systems (Vujicic, de Man, & Woodrow, 1968), milk protein concentrate dispersions (McCarthy et al, 2017;Mizuno & Lucey, 2005), milk microfiltration concentrates (Toledo Renhe, Indris, & Corredig, 2018), concentrated micellar casein dispersions (De Kort, Minor, Snoeren, Van Hooijdonk, & Van der Linden, 2011 Furuichi, 1975), individual caseins (Guo, Campbell, Chen, Lenhoff, & Velev, 2003), soymilk (Pathomrungsiyounggul, Lewis, & Grandison, 2010), reconstituted calciumfortified milk powders (Williams, D'Ath, & Augustin, 2005) and whey protein beverages fortified with calcium (Keowmaneechai & McClements, 2002& 2006.…”

Section: Introductionmentioning

confidence: 99%

Influence of calcium-binding salts on heat stability and fouling of whey protein isolate dispersions

Hebishy

Joubran

Murphy

et al. 2019

International Dairy Journal

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The effect of the calcium-binding salts (CBS), trisodium citrate (TSC), tripotassium citrate (TPC) and disodium hydrogen phosphate (DSHP) at concentrations of 1-45 mM on the heat stability and fouling of whey protein isolate (WPI) dispersions (3%, w/v, protein) was investigated. The WPI dispersions were assessed for heat stability in an oil bath at 95 °C for 30 min, viscosity changes during simulated high-temperature short-time (HTST) and fouling

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“…On the contrary, a group of researchers have reported that conjugation of WPI with maltodextrin at 60 °C for 24 h enhanced the protein solubility at pH 3.5–4 (McCarthy et al . ). Interestingly, the system did stabilise when SHMP concentration was increased to 1% w/w.…”

Section: Resultsmentioning

confidence: 97%

“…However, these proteins are prone to denaturation and thus subsequent aggregation upon heating, arising from conformational changes due to alterations in the degree of exposed hydrophobic regions, as well as modification of protein charge (McCarthy et al . ). It is stated that heat treatment at 70–75 °C leads to the formation of small and reversible bonds between protein particles via weak van der Waals interactions while higher temperatures (80–90 °C) strengthen the covalent disulphide bonds.…”

Section: Introductionmentioning

confidence: 97%

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On the heat stability of whey protein: Effect of sodium hexametaphosphate

Rasouli

Abbasi

Azarikia

et al. 2019

Int J of Dairy Tech

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Despite a growing demand for whey protein-based drinks, their instability and lack of solubility during thermal processing is a major challenge for food product formulators. In the present study, the effects of different hydrocolloids and sodium hexametaphosphate (SHMP) on the heat stability, rheological properties, microstructure and sensory characteristics of whey protein concentrate (WPC) dispersions were evaluated. The results indicated that at pH 4, xanthan, k-carrageenan, low methoxyl pectin (LMP) and guar stabilised WPC dispersion without heat treatment, all maintained stability during pasteurisation but not sterilisation. For pH 7, for the same set of hydrocolloids, a similar trend was also observed, albeit at different concentrations. However, by adding optimum ratios of SHMP protein denaturation was retarded, particularly in the case of LMP and i-carrageenan. The highest and lowest apparent viscosities were exhibited by samples containing 0.01% and 0.15% w/w SHMP, respectively. This study highlights the potential capability of SHMP in the prevention of protein denaturation. An exact plausible stability mechanism still needs further more detailed investigation.

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Effects of calcium chelating agents on the solubility of milk protein concentrate

Cited by 60 publications

References 28 publications

Influence of milk protein concentrates with modified calcium content on enteral dairy beverage formulations: Physicochemical properties

Influence of milk protein concentrates with modified calcium content on enteral dairy beverage formulations: Physicochemical properties

Influence of calcium-binding salts on heat stability and fouling of whey protein isolate dispersions

On the heat stability of whey protein: Effect of sodium hexametaphosphate

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