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2D-Cross Correlation Spectroscopy Coupled with Molecular Fluorescence Spectroscopy for Analysis of Molecular Structure Modification of Camel Milk and Cow Milk Mixtures during Coagulation

Oumayma BoukriaApplied Organic Chemistry Laboratory, Sciences and Techniques Faculty, Sidi Mohamed Ben Abedallah University, Route d’Immouzer, Fès BP 2202, MoroccoEl Mestafa El HadramiApplied Organic Chemistry Laboratory, Sciences and Techniques Faculty, Sidi Mohamed Ben Abedallah University, Route d’Immouzer, Fès BP 2202, MoroccoShakhnoza SultanovaDepartment of Food Engineering, Faculty of Mechanical Building, Tashkent State Technical University Named after Islam Karimov, University str. 2, Tashkent 100095, UzbekistanJasur SafarovDepartment of Food Engineering, Faculty of Mechanical Building, Tashkent State Technical University Named after Islam Karimov, University str. 2, Tashkent 100095, UzbekistanFrançoise LericheUniversité Clermont-Auvergne, INRAE, VetAgro Sup, 63370 Lempdes, FranceAbderrahmane Aït‐KaddourUniversité Clermont-Auvergne, INRAE, VetAgro Sup, 63370 Lempdes, France
Foodsjournal2020en
ABI

Аннотация

Synchronous fluorescence spectroscopy (SFS) coupled with two-dimensional correlation spectroscopy (2DCOS) was employed to monitor, at the molecular level, the coagulation of five mixture ratios of camel's milk (CaM) and cow's milk (CM) (100% CaM, 75% CaM:25% CM, 50% CaM:50% CM, 25% CaM:75% CM and 100% CM). The dissimilarities among the different formulations are highlighted on the synchronous 2DCOS-SFS. In addition, according to the cross-peak symbols in synchronous and asynchronous spectra, the rate of response modification in riboflavin, protein and vitamin A matched with common coagulation phenomena usually reported during chymosin coagulation (hydrolysis of κ-casein, destabilization of casein micelles and aggregation). This study demonstrated that 2DCOS-SFS is a successful strategy to discriminate milk mixtures and to monitor molecular structure modifications during coagulation process.

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