Casein glycomacropeptide pH-dependent self-assembly and cold gelation

Farı́as, Marta E.; Martínez, María Julia; Pilosof, Ana M.R.

doi:10.1016/j.idairyj.2009.09.002

Cited by 73 publications

(104 citation statements)

References 30 publications

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“…In a recent work (Farías et al, 2010) we showed that CMP at pH below 4.5 undergoes a time-dependent self-assembly at room temperature which leads with time to the formation of opaque gels. The minimum CMP concentration for this cold-gelation depended on pH.…”

Section: Cmp Gelationmentioning

confidence: 96%

“…At room temperature, CMP undergoes a pH-dependent self-assembly at pH < 4.5 forming different self-assembled structures that depending on CMP concentration can form gels. Self-assembled structures are almost pH-reversible, but dimers appear to be resistant to pH changes once formed (Farías et al, 2010). CMP self-assembly would include a first stage of hydrophobic self-assembly to form dimers which further interact trough electrostatic bonds to form gels with time.…”

Section: Size Distribution Of Particles At Ph 35mentioning

confidence: 99%

“…A further increase of temperature slightly reduced the time for gelation. According to the model proposed to explain CMP self-assembly and the formation of a network-like structure (gel) at room temperature (Farías et al, 2010), it would involve a first step of hydrophobic self-assembly to form dimers which further interact trough electrostatic bonds to form gels with time. Temperature increases the potential for hydrophobic interactions (Bryant & McClements, 1998) increasing the rate of the first step involving hydrophobic bonds between CMP monomers, thus increasing the overall gelation rate.…”

Section: Cmp Gelationmentioning

confidence: 99%

“…Burton and Skudder (1987) reported the gelation of a 9.3% (w/w) CMP solution at pH 4.5 and 20 C. However, Wang (2007) reported that CMP was also able to form a gel only at pH < 4.0. In a recent paper, we described the pH-driven cold gelation of CMP and proposed a model to explain it (Farías, Martinez, & Pilosof, 2010). As a result of the spontaneous pH-driven self-assembly of CMP at room temperature, the solutions at pH below 4.5 gelled with time.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The dynamics of heat gelation of casein glycomacropeptide – β-lactoglobulin mixtures as affected by interactions in the aqueous phase

Martínez

Farı́as

Pilosof

2010

International Dairy Journal

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Section: Cmp Gelationmentioning

confidence: 96%

Section: Size Distribution Of Particles At Ph 35mentioning

confidence: 99%

Section: Cmp Gelationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The dynamics of heat gelation of casein glycomacropeptide – β-lactoglobulin mixtures as affected by interactions in the aqueous phase

Martínez

Farı́as

Pilosof

2010

International Dairy Journal

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“…With glycomacropeptide, the monomer molecules of glycomacropeptide are able to self-assemble at gastric pH (pH 4) because of hydrophobic interaction (Farías, Martinez, & Pilosof, 2010) that prohibits its accessibility to pepsin in stomach phase. However, at intestinal phase (pH 7), most of the hydrophobic domains of glycomacropeptide become strong negative charge density due to deprotonation of amino acids (Glu and Asp) that makes glycomacropeptide molecules turn into strong negative shields preventing then self-association (Sharma, Rajput, & Mann, 2013).…”

Section: Protein Digestion Determined By Sds-pagementioning

confidence: 99%

Digestibility and structural changes of ingredients in infant formulae during the gastrointestinal digestion

Nguyen¹

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Although mothers' milk is the ideal food for babies, infant formula has become an alternative when breastfeeding is not possible or inadequate for babies. To design a proper formula for babies, it is essential to understand the digestibility of macronutrients and their bio-accessibility in the infant gastrointestinal tract. Because in vivo gastrointestinal studies on human infants are restricted by ethical constraint, cost issues, and intensive resource, in vitro models could be a better replacement.In vitro models offer advantages with low cost, easy sampling accessibility and no ethical issues. This thesis aims to assess the digestibility of each ingredient proteins, lipids, and carbohydrates in infant formulation then compare with mothers' milk. A static bench-top in vitro model for infant digestion was set up with infant gastric pH (4.0-4.5) and the activity of simulated digestive enzymes suitable for human infants with 60 minutes of gastric phase and 120 minutes of intestinal phase.Popular protein sources of caseins, whey, and soy proteins were employed in infant formulations.The in vitro digestion of these proteins in infant formulations was studied in the presence of enzyme proteases only (without lipolytic enzymes). Obtained results showed around 20% of caseins and no components of whey were hydrolysed after 60 minutes in the simulated stomach. In the simulated intestinal phase, 8% of α-lactalbumin was hydrolysed while caseins and β-lactoglobulin were completely digested immediately and 30 minutes respectively after addition of intestinal digestive proteases. Overall, soy proteins indicated lower level of hydrolysis than dairy proteins during in vitro infant digestion as observed by SDS-PAGE. The soy protein fractions glycinin and β-conglycinin were partially hydrolysed during the gastrointestinal phase. The observed pH drop confirms that caseins are easily digested in the intestinal phase compared to whey and soy protein. Gastric digestion resulted in a decrease of the particle size of protein aggregates, but no fat coalescence was observed during both gastric and intestinal digestion in the given conditions.The in vitro digestion of hydrolysed and non-hydrolysed dairy (casein and whey proteins) was studied under conditions without lipolytic enzymes. Results show hydrolysed proteins were completely digested in the small intestine while non-hydrolysed proteins (caseins, α-lactalbumin, β-lactoglobulin, conglycinin, glycinin) were only partially digested in the simulated gastrointestinal tract. Although observed pH-drop for non-hydrolysed protein formulations was lower, significantly higher levels of ninhydrin-reactive amino nitrogen in hydrolysed proteins suggested higher digestibility of hydrolysed proteins than their non-hydrolysed counterparts. Only formulations containing caseins showed a decrease in particle size of protein aggregates during gastric digestion. No fat globule coalescence was observed during both gastric and intestinal digestions in the given conditions. Lipid digestion of infa...

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Biological Roles and Production Technologies Associated with Bovine Glycomacropeptide

Feeney

Joshi

Hickey

2018

Novel Proteins for Food, Pharmaceuticals and Agriculture

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Casein glycomacropeptide pH-dependent self-assembly and cold gelation

Cited by 73 publications

References 30 publications

The dynamics of heat gelation of casein glycomacropeptide – β-lactoglobulin mixtures as affected by interactions in the aqueous phase

The dynamics of heat gelation of casein glycomacropeptide – β-lactoglobulin mixtures as affected by interactions in the aqueous phase

Digestibility and structural changes of ingredients in infant formulae during the gastrointestinal digestion

Biological Roles and Production Technologies Associated with Bovine Glycomacropeptide

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