NMR Relaxometry and Imaging of Dairy Products

Mariette, François

doi:10.1007/978-3-319-28275-6_38-1

Cited by 3 publications

(2 citation statements)

References 61 publications

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“…In addition, for hydrogen as the most abundant nuclei in the organic components, two observing parameters are being obtained including spin-lattice relaxation time with a time constant T 1 and spin-spin relaxation time with a time constant T 2 . Proton relaxation studies were explained in detail by Mariette [47] giving an overview of different applications and examples of NMR relaxation studies, diffusion coefficient measurements and magnetic resonance imaging (MRI) on dairy products. The relaxation measurement studies observe the water distribution and dynamics in the milk products, mainly with regard to the interactions among proteins and water in milk.…”

Section: Whey Proteinsmentioning

confidence: 99%

Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies

Markoska

Vasiljevic

Huppertz

2020

Foods

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Changes in the molecular structure and association of milk proteins lead to many desirable (under controlled conditions) or undesirable characteristics of dairy products. Several methods have been used to study the structure of milk proteins and changes therein in different environments. Whey proteins are an excellent model for secondary structure studies using circular dichroism (CD), Fourier-transform infrared spectroscopy (FTIR) and tertiary structure studies using X-ray crystallography and nuclear magnetic resonance (NMR). However, caseins, the most abundant protein class in milk, are far more difficult to characterize. The tertiary structure of caseins cannot be observed by X-ray crystallography due to the inability to crystallize caseins. However, NMR is an appropriate approach for structural elucidation. Thus far, NMR was applied on specific peptides of individual caseins of the molecules including phosphoserine centers and colloidal calcium phosphate. The literature focuses on these parts of the molecule due to its importance in building the sub-unit particles involving individual caseins and calcium phosphate nanoclusters. This review focuses on present structural studies of milk proteins using NMR and their importance in dairy processing.

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Section: Whey Proteinsmentioning

confidence: 99%

Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies

Markoska

Vasiljevic

Huppertz

2020

Foods

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“…This technique is extensively used in material science studies, including food applications, e.g. to probe the microstructure of heterogenous matrices indirectly via characterizing the molecular mobility of water or solutes therein (Dai & Matsukawa, 2012;Mariette, 2017;Schork et al, 2020). Applications related to gastric milk protein digestion include the monitoring of acid-and rennet-induced casein coagulation, and measurements of WP solutions and gels using water or polyethylene glycol (PEG) as a probe (Colsenet et al, 2005;Mariette, 2017;Mariette et al, 2002).…”

Section: Diffusionmentioning

confidence: 99%

Bridging the gap between in vitro and in vivo: an MRI toolkit for milk protein digestion studies

Mayar

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Cow's milk is an important source of high-quality proteins in the human diet. The major proteins in milk are caseins and whey proteins (WPs), constituting approximately 80% and 20%, respectively. Both caseins and WPs are considered complete proteins, meaning that they contain high levels of all essential AAs required by the human body. Additionally, these proteins have excellent digestibility, as evaluated by the digestible indispensable amino acid score (DIAAS), leading to their high bioavailability (Dupont & Tomé, 2019).

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Understand and characterize draining of acid milk gels using Magnetic Resonance Imaging and Time Domain-Nuclear Magnetic Resonance

Monaretto,

Quellec,

Cambert

et al. 2024

Journal of Food Engineering

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NMR Relaxometry and Imaging of Dairy Products

Cited by 3 publications

References 61 publications

Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies

Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies

Bridging the gap between in vitro and in vivo: an MRI toolkit for milk protein digestion studies

Understand and characterize draining of acid milk gels using Magnetic Resonance Imaging and Time Domain-Nuclear Magnetic Resonance

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