Stability of casein micelles reticulated by genipin at acid pH
2014
Nogueira Silva, Naaman Francisco | Bahri, Asma | Guyomarc'h, Fanny | Gaucheron, Frederic
Modify casein micelles (CMs) constitutes a challenge to create new stable structures and functionalities. The objective of this study was to prepare cross-linked CMs by genipin (GP) and evaluate their stabilities (in comparison with native CMs) at pH 7.1 or 5.2 knowing that acid pH induce demineralization and dissociation of CMs. The dimensional characteristics of these new structures were appreciated by diffusion light scattering and atomic force microscopy. For control CMs (without GP), and as expected, they were stable at pH 7.1 and dissociated at acidic pH because it was impossible to observe particle by DLS and AFM. As control sample, CMs reticulated by GP were stable at pH 7.1. In the opposite to the native CMs, they remained also stable at acidic pH. The dimensional characteristics of these modified CMs determined by DLS and AFM revealed slight changes in their size and morphology (height, diameter and contact angle) but the particles were not dissociated. These stabilities in extreme conditions for CMs were related to intra micellar cross linking between basic amino acids (lysyl and arginyl residues) present in casein molecules. Due to their structure and stability, these new particles could be proposed as nanovehicle
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