The pH-dependent thermal and storage stability of glycosylated caseinomacropeptide

Siegert, Nadja; Tolkach, A. M.; Kulozik, Ulrich

doi:10.1016/j.lwt.2012.02.001

Cited by 12 publications

(5 citation statements)

References 34 publications

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“…There were no significant losses in GMP solubility under all conditions tested. Heat stability at mildly acidic and near-neutral pH is in agreement with previous studies, but GMP heat stability has previously been shown to decrease at low pH . This difference could be due to the different heat treatments the authors used, but that remains to be established.…”

Section: Resultssupporting

confidence: 89%

“…Heat stability at mildly acidic and near-neutral pH is in agreement with previous studies, but GMP heat stability has previously been shown to decrease at low pH. 51 This difference could be due to the different heat treatments the authors used, but that remains to be established. At pH 3, there was no significant loss of α-La or β-Lg solubility after LT and HT treatments, which is in agreement with both the solubility state diagram and SDS-PAGE results.…”

Section: ■ Materials and Methodssupporting

confidence: 88%

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Using State Diagrams for Predicting Colloidal Stability of Whey Protein Beverages

Wagoner

Ward²,

Foegeding

2015

J. Agric. Food Chem.

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A method for evaluating aspects of colloidal stability of whey protein beverages after thermal treatment was established. Three state diagrams for beverages (pH 3-7) were developed representing protein solubility, turbidity, and macroscopic state after two ultrahigh-temperature (UHT) treatments. Key transitions of stability in the state diagrams were explored using electrophoresis and chromatography to determine aggregation propensities of β-lactoglobulin, α-lactalbumin, bovine serum albumin, and glycomacropeptide. The state diagrams present an overlapping view of high colloidal stability at pH 3 accompanied by high solubility of individual whey proteins. At pH 5, beverages were characterized by poor solubility, high turbidity, and aggregation/gelation of whey proteins with the exception of glycomacropeptide. Stability increased at pH 6, due to increased solubility of α-lactalbumin. The results indicate that combinations of state diagrams can be used to identify key regions of stability for whey protein containing beverages.

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Section: Resultssupporting

confidence: 89%

Section: ■ Materials and Methodssupporting

confidence: 88%

Using State Diagrams for Predicting Colloidal Stability of Whey Protein Beverages

Wagoner

Ward²,

Foegeding

2015

J. Agric. Food Chem.

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“…1). It is noteworthy that the degree of glycosylation of CMP is affected by the conditions of manufacture, in particular pH and intensity of pre-heat treatment (Siegert, Tolkach, and Kulozik, 2012).Whey protein isolate (WPI) was purchased from Davisco Bipro ® (Davisco Food International, U.S.A.) and contained 91.9% (w/w) protein (Kjeldahl analysis, nitrogen to protein conversation factor of 6.38). The calcium content of the WPI powder was 0.11% (w/w).…”

Section: Methodsmentioning

confidence: 99%

Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.

et al. 2021

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“…Indeed, recently GMP has shown promise as a nutritional therapy in patients with active distal ulcerative colitis [ 68 ]. Moreover, methods for producing GMP based on its glycosylation and the effect of its glycosylation on the peptide’s techno-functional properties have been documented [ 69 , 70 , 71 , 72 , 73 , 74 ]. The fact that some dairy-ingredient companies have already realized the potential of GMP and are promoting this glycopeptide as a premium ingredient isolated from whey makes these findings particularly relevant.…”

Section: Discussionmentioning

confidence: 99%

Glycomacropeptide Reduces Intestinal Epithelial Cell Barrier Dysfunction and Adhesion of Entero-Hemorrhagic and Entero-Pathogenic Escherichia coli in Vitro

Feeney

Ryan

Kilcoyne

et al. 2017

Foods

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In recent years, the potential of glycosylated food components to positively influence health has received considerable attention. Milk is a rich source of biologically active glycoconjugates which are associated with antimicrobial, immunomodulatory, anti-adhesion, anti-inflammatory and prebiotic properties. Glycomacropeptide (GMP) is the C-terminal portion of kappa-casein that is released from whey during cheese-making by the action of chymosin. Many of the biological properties associated with GMP, such as anti-adhesion, have been linked with the carbohydrate portion of the protein. In this study, we investigated the ability of GMP to inhibit the adhesion of a variety of pathogenic Escherichia coli strains to HT-29 and Caco-2 intestinal cell lines, given the importance of E. coli in causing bacterial gastroenteritis. GMP significantly reduced pathogen adhesion, albeit with a high degree of species specificity toward enteropathogenic E. coli (EPEC) strains O125:H32 and O111:H2 and enterohemorrhagic E. coli (EHEC) strain 12900 O157:H7. The anti-adhesive effect resulted from the interaction of GMP with the E. coli cells and was also dependent on GMP concentration. Pre-incubation of intestinal Caco-2 cells with GMP reduced pathogen translocation as represented by a decrease in transepithelial electrical resistance (TEER). Thus, GMP is an effective in-vitro inhibitor of adhesion and epithelial injury caused by E. coli and may have potential as a biofunctional ingredient in foods to improve gastrointestinal health.

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The pH-dependent thermal and storage stability of glycosylated caseinomacropeptide

Cited by 12 publications

References 34 publications

Using State Diagrams for Predicting Colloidal Stability of Whey Protein Beverages

Using State Diagrams for Predicting Colloidal Stability of Whey Protein Beverages

Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.

Glycomacropeptide Reduces Intestinal Epithelial Cell Barrier Dysfunction and Adhesion of Entero-Hemorrhagic and Entero-Pathogenic Escherichia coli in Vitro

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