Present work comprises the use of different solid-state Nuclear Magnetic Resonance strategies for characterizing structural and motional aspects of the peptide matrix that compose a set of four lyophilized Mexican cheese aqueous soluble extracts, each with a controlled ripening. Heteronuclear dipolar coupling modulation schemes allowed to characterize local mobility and structural homogeneity of cheeses' peptide segments in the solid-state as a function of ripening. Results suggest that ripened samples with certain local flexibility but important structural homogeneity present efficient microbial inhibition against tested bacterial strains, whilst high local rigidity of peptides within ripened cheese soluble fractions could partially explain the observed lack of antimicrobial activity. The present study attempts to propose novel observables for lyophilized cheese water soluble extracts that could be partially associated to their ripening-dependent antimicrobial activities, whereas said observables shall contribute to the better targeting, design and optimization of solid-state natural food bio-preservatives.
Keywords: Antimicrobial peptides; Bioactive cheese water-soluble fractions; Cheese ripening; Cross polarization inversion; Cross polarization magic angle spinning; Dipolar dephasing; Solid-state NMR spectroscopy.
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