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Understanding the alkali cold gelation of whey proteins with NaCl and SDS

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Abstract

The alkali cold gelation of whey proteins is studied due to its fascinating rheological gelation profiles, as well as to investigate the existence of an alkali dissolution threshold for protein hydrogels with the protein concentration. Alkali cold gelation is achieved by first producing soluble protein aggregates followed by a sudden increase of the pH. At pH > 11.6 there is a de-gelation step with time following an initial quick gelation step. This dynamic transition involves only the formation of non-covalent interactions between the initial covalently crosslinked aggregates; first they are formed but later on they are destroyed. This mechanistic hypothesis is verified here by adding NaCl and SDS in addition to alkali. A sharp transition of the system modulus can be achieved due non-covalent interactions on soluble disulfide crosslinked aggregates in a narrow protein concentration range.

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Acknowledgments

This work was supported by the project funding from the Priority Academic Program Development (PAPD) of Jiangsu Higher Education Institutions and the “Jiangsu Specially-Appointed Professors Program” of China and the Youth Fund of Natural Science Foundation of Jiangsu Province of China (No. BK20140343).

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Authors and Affiliations

  1. Suzhou Key Laboratory of Green Chemical Engineering, School of Chemical and Environmental Engineering, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou City, Jiangsu, 215123, People’s Republic of China

    Lei Zhao, Xiao Dong Chen & Ruben Mercadé-Prieto

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  1. Lei Zhao
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  2. Xiao Dong Chen
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  3. Ruben Mercadé-Prieto
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Correspondence to Ruben Mercadé-Prieto.

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Zhao, L., Chen, X.D. & Mercadé-Prieto, R. Understanding the alkali cold gelation of whey proteins with NaCl and SDS. Rheol Acta 55, 909–920 (2016). https://doi.org/10.1007/s00397-016-0966-z

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  • DOI: https://doi.org/10.1007/s00397-016-0966-z

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