Effect of N-ethylmaleimide as a blocker of disulfide crosslinks formation on the alkali-cold gelation of whey proteins

Zhao Lei, Xiao Dong Chen, Ruben Mercadé-Prieto

Producción científica: Artículo en revista indizadaArtículorevisión exhaustiva

5 Citas (Scopus)

Resumen

N-ethylmaleimide (NEM) was used to verify that no new disulfide crosslinks were formed during the fascinating rheology of the alkali cold-gelation of whey proteins, which show Sol-Gel-Sol transitions with time at pH > 11.5. These dynamic transitions involve the formation and subsequent destruction of non-covalent interactions between soluble whey aggregates. Therefore, incubation of aggregates with NEM was expected not to affect much the rheology. Experiments show that very little additions of NEM, such as 0.5 mol per mol of protein, delayed and significantly strengthened the metastable gels formed. Interactions between whey protein aggregates were surprisingly enhanced during incubation with NEM as inferred from oscillatory rheometry at different protein concentrations, dynamic swelling, Trp fluorescence and SDS-PAGE measurements.

Idioma originalInglés
Número de artículoe0164496
PublicaciónPLoS ONE
Volumen11
N.º10
DOI
EstadoPublicada - oct 2016
Publicado de forma externa

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