Influence of calcium and sodium chloride on caseinomacropeptide self-assembly and flow behaviour at neutral pH

Loria, Karina G.; Pilosof, Ana M.R.; Farı́as, Marta E.

doi:10.1016/j.lwt.2018.09.029

Cited by 7 publications

(3 citation statements)

References 24 publications

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“…A previous study (Loria et al ., 2018) found that, in the absence of salts, CMP mainly presented a monomeric form at pH 7.0. However, if salt is added, the hydrophobic associations of CMP are promoted due to screening of electric charges.…”

Section: Resultsmentioning

confidence: 99%

Rheological and microstructural characterisation of heat-induced whey protein isolate gels affected by the addition of caseinomacropeptide

Guedes

Freitas

Franco

et al. 2022

Journal of Dairy Research

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Caseinomacropeptide (CMP) is derived from the chymosin cleavage of κ-casein during cheese production. This study developed gels from CMPs, which were isolated by different ultrafiltration systems, and whey protein isolate (WPI), and studied their rheological and ultrastructural characteristics. The 30% WPI gel showed high elastic modulus (G′) values and stronger structure than the other samples with CMP. Another gel, with 50% protein, 30% WPI and 20% CMP sample isolated from the 30 kDa retentate, had a weaker structure and lower G′ value. The third gel, with 30% WPI and 20% CMP sample from the 5 kDa retentate derived from the 30 kDa retentate, presented intermediate structural strength. Despite the increase in protein concentration from the addition of CMP, there was a decrease in the strength of the gel network. Different CMP isolation processes also contributed to differences in the microscopic analysis of gel structures with the same protein content.

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Section: Resultsmentioning

confidence: 99%

Rheological and microstructural characterisation of heat-induced whey protein isolate gels affected by the addition of caseinomacropeptide

Guedes

Freitas

Franco

et al. 2022

Journal of Dairy Research

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“…The total nitrogen content of solutions and the respective powders was determined using Kjeldahl method [25]. The nitrogen to protein conversion factors used for MCC and GMP were 6.38 and 7.07, respectively [23]. The total solids content of solutions and powder samples were determined using oven drying (103.5 • C for 5 h) [26].…”

Section: Compositional Analysis Of Protein Solutions and Powdersmentioning

confidence: 99%

“…Likewise, the formation of protein aggregates in solutions of sodium caseinate or denatured β-lactoglobulin was reported to be suppressed by the presence of GMP [18,21,22], providing evidence of electrostatic repulsion induced by GMP for preventing protein-protein interactions. GMP shows the tendency to self-associate at neutral pH in pure water in the presence of calcium (>1.2 mmol/g GMP) through hydrophobic interaction [23], as the negative charge of sialic acid is screened by ionic calcium (Ca 2+ ) at neutral pH [24]. Consequently, it is hypothesized that GMP would enhance dissolution properties of high-protein dairy powders due to its highly hydrophilic nature; more specifically, incorporation of GMP in MCC solution at neutral pH would modulate electrostatic interactions between casein micelles, with consequent improvement of rehydration properties of subsequent high protein, casein-dominant powders.…”

Section: Introductionmentioning

confidence: 99%

Influence of Glycomacropeptide on Rehydration Characteristics of Micellar Casein Concentrate Powder

Panthi

Bot

O’Mahony

2021

Foods

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Glycomacropeptide (GMP) shows potential for enhancing the rehydration properties of high-protein dairy powders due to its hydrophilic nature. This study involved formulating micellar casein concentrate (MCC) solutions (8.6% final protein content) with 0, 10, and 20% GMP as a percentage of total protein, and investigated the physicochemical and rehydration properties of the resultant freeze-dried powders (P-MCC-0G, P-MCC-10G, and P-MCC-20G, respectively). The surface charges of caseins in the control MCC and 10 or 20% GMP blended solutions were −25.8, −29.6, and −31.5 mV, respectively. Tablets prepared from P-MCC-10G or P-MCC-20G powders displayed enhanced wettability with contact angle values of 80.6° and 79.5°, respectively, compared with 85.5° for P-MCC-0G. Moreover, blending of GMP with MCC resulted in faster disintegration of powder particles during rehydration (i.e., dispersibility) compared to P-MCC-0G. Faster and more extensive release of caseins from powder particles into solution was evident with the increasing proportion of GMP, with the majority of GMP released within the first 15 min of rehydration. The results of this study will contribute to further development of formulation science for achieving enhanced solubility characteristics of high-protein dairy powder ingredients, such as MCC.

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Effect of dialysate type on ultrasound-assisted self-assembly Zein nanocomplexes: Fabrication, characterization, and physicochemical stability

Zhou

Zhao²,

Chen³

et al. 2022

Food Research International

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Influence of calcium and sodium chloride on caseinomacropeptide self-assembly and flow behaviour at neutral pH

Cited by 7 publications

References 24 publications

Rheological and microstructural characterisation of heat-induced whey protein isolate gels affected by the addition of caseinomacropeptide

Rheological and microstructural characterisation of heat-induced whey protein isolate gels affected by the addition of caseinomacropeptide

Influence of Glycomacropeptide on Rehydration Characteristics of Micellar Casein Concentrate Powder

Effect of dialysate type on ultrasound-assisted self-assembly Zein nanocomplexes: Fabrication, characterization, and physicochemical stability

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