Post-translational Modifications of Caseins

Bijl, Etske; Holland, John W.; Boland, Mike

doi:10.1016/b978-0-12-405171-3.00005-2

Cited by 13 publications

(5 citation statements)

References 126 publications

(103 reference statements)

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“…One of the most problems in producing acidic milk drinks is their two‐phase production and maintenance due to their low viscosity, low pH, and their effect on protein deposition (Azarikia & Abbasi, 2010 ). Basically, the stability of casein micelles at the natural pH of milk is due to the position of kappa‐caseins on the casein micelle surface, which prevents the micelles from approaching each other by forming hair layers on their surface and spatial and electrostatic repulsion mechanisms (Holland & Boland, 2014 ; Manguy & Shields, 2019 ).…”

Section: Resultsmentioning

confidence: 99%

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Investigation of rheological, physicochemical, and sensorial properties of traditional low‐fat Doogh formulated

Rahmati,

Mahjoorian,

Fazeli

et al. 2023

Food Science & Nutrition

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Doogh is a fermented beverage made from yoghurt with water and salt. Similarly, drinks based on yoghurt are available in different countries with varying degrees of dilution, fat content, rheological properties, and taste. In this project, the use of mathematical calculations in describing rheological parameters from traditional low‐fat Doogh enriched with Caspian Sea (Huso huso) gelatin (0.4 w/v %), xanthan hydrocolloids (0.4 w/v %), and their mixture at a ratio of 0.2:0.2 w/v % studied. Also, serum isolation, pH, and sensory evaluation of samples were investigated. Also, the relationship between apparent viscosity and temperature of Doogh samples using the Arrhenius equation was studied. The sensory evaluation revealed that the overall acceptance scores of the samples containing gelatin, xanthan, mix, and control were 4.31, 4.33, 4.58, and 4.12, respectively. The study on serum separation value showed control sample (45.07) and mix sample (0.84) at the end of 30 days. On the first day, the pH of the Doogh samples decreased with the addition of hydrocolloids, and this trend was time dependent. pH reduction was higher in Doogh with gelatin than in other samples. Mathematical calculations showed that the low‐fat Doogh is a non‐Newtonian type and shear‐thinning (Pseudoplastic) fluid. The activation energy was calculated between 11.65 and 19.15 kJ/mol. According to the obtained results, it concluded that the use of two hydrocolloid compounds improved the physicochemical and sensory characteristics of the low‐fat Doogh samples. Also, the Ostwald‐de Waele mathematical model had a high correlation with the rheological behavior of the samples.

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Section: Resultsmentioning

confidence: 99%

“…Basically, the stability of casein micelles at the natural pH of milk is due to the position of kappa-caseins on the casein micelle surface, which prevents the micelles from approaching each other by forming hair layers on their surface and spatial and electrostatic repulsion mechanisms (Holland & Boland, 2014;Manguy & Shields, 2019).…”

Section: Ta B L Ementioning

confidence: 99%

Investigation of rheological, physicochemical, and sensorial properties of traditional low‐fat Doogh formulated

Rahmati,

Mahjoorian,

Fazeli

et al. 2023

Food Science & Nutrition

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“…The crude enzymatic extract of P. camemberti 0798400075 produced in the rst 24 hrs of fermentation was used to analyze the coagulant activity at 40 ºC at different times, and the results are presented in Table 1, each analysis was performed in triplicate with the control (medium without the enzyme). The coagulant activity determines the level of coagulation that caiseinase performs in milk casein micelles, which are constituted by four types of caseins called αS1, αS2, β and κ-caseins, joined through hydrophobic and electrostatic interactions, and mainly by calcium phosphate salts (Holland and Boland 2014). The κ-casein fraction, which is located on the surface of the micelle, is the only major component of casein that remains soluble in the presence of Ca 2+ ions at the concentrations found in milk.…”

Section: Determination Of Clotting Activitymentioning

confidence: 99%

New Protease Produced by Solid State Fermentation of Penicillium camemberti 0798400075 Using Coffee Hull Applied in Milk Coagulation

Melo,

Silva,

Tavares

et al. 2023

Preprint

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The milk clotting proteases have the specificity of hydrolyzing the k-casein fraction of milk casein micelles. In this study, the biochemical characterization and coagulation potential of a new milk coagulant derived from the enzymatic extract of Penicillium camemberti 0798400075 through solid state fermentation (SSF) using coffee husks are investigated. The caseinase produced showed low proteolytic activity (0.076 U/mL) and high coagulant activity (8 ACL/mL and 10 ACL/mL) for powdered and whole UHT milk, respectively, and reached optimal temperature at 50 ºC and optimal pH at 7, remained with 80% of its activity at 40 ºC, showed greater affinity for acidic conditions, containing more than 60% of its activity at pH 5.0 and exhibited an increase in its activity in the presence of Mg2+ ions. The new coagulant showed potential to be used as a substitute for rennet in the coagulation process of milk caseins.

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“…They form a colloidal complex (micelles) with calcium phosphate as well as small amounts of other minerals. A key element affecting micelle formation and stability is the presence of PTMs, such as phosphorylation in α S1 CN, α S2 CN i βCN and glycosylation in κCN [9]. The main protein in bovine milk is βCN [10].…”

Section: Introductionmentioning

confidence: 99%

Identification of post-translational modifications of milk and whey proteins with different structures

Rodzik

Railean-Plugaru

Pomastowski³

et al. 2023

Preprint

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Post-translational modifications (PTMs) regulate cellular processes, and any disruption of PTMs leads to abnormal activity of biological processes, and therefore diseases. The main goal of the present research was focused on developing a rapid analytical method for identifying PTMs in milk (β-casein) and whey (β-lactoglobulin) proteins that differ by structure and composition; the chosen proteins are considered the richest source of nutrients and functional components. The classical in-gel protein digestion method and protein digestion in a microreactor (μ-IMER) method has been performed. In addition, ZipTip pipette tipscontaining C18 reverse phase media were used for both methods to concentrate and purify peptide samples; they also aimed to determine the effect of such a prepared sample on the improvement or deterioration of the sequence coverage result. As support for the preparation of the microreactor, a monolithic copolymer synthesized from GMA and EDMA was used. Subsequently, surface modifications were carried out to attach the enzyme with the highest efficiency. The efficiency of the prepared microreactor was evaluated under HPLC chromatographic conditions using a small-molecule trypsin substrate (BAEE). The obtained hydrolysates from the microreactor and the classical digestion in solution method in the presence of ZipTip pipette tips and without were analyzed by MALDI-TOF MS.

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Post-translational Modifications of Caseins

Cited by 13 publications

References 126 publications

Investigation of rheological, physicochemical, and sensorial properties of traditional low‐fat Doogh formulated

Investigation of rheological, physicochemical, and sensorial properties of traditional low‐fat Doogh formulated

New Protease Produced by Solid State Fermentation of Penicillium camemberti 0798400075 Using Coffee Hull Applied in Milk Coagulation

Identification of post-translational modifications of milk and whey proteins with different structures

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