Effect of nonenzymatic deamidation on the structure stability of Camelus dromedarius α-lactalbumin - Université de Lorraine Access content directly
Journal Articles Food Chemistry Year : 2019

Effect of nonenzymatic deamidation on the structure stability of Camelus dromedarius α-lactalbumin

Abstract

Camelid α-lactalbumin is the only known protein that can undergo nonenzymatic deamidation on two Asn residues. This leads to the generation of a mixture of unusual isoAsp and d-Asp residues that may impact health. The effect of deamidation on camel α-lactalbumin instability was investigated. Circular dichroism showed that the altered protein acquired secondary structure resulting in an increase in α-helix content. In good agreement, the 3D structure of camel α-lactalbumin determined by X-ray crystallography, displayed a short additional α-helix probably induced by deamidation, compared to the human and bovine counterparts. This α-helix was located in the C-terminal region and included residues 101–106. Differential scanning calorimetry together with the susceptibility to thermolysin showed that the deamidation process reinforced the structural stability of the α-lactalbumin at high temperature and its resistance toward proteolysis.
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Dates and versions

hal-02095313 , version 1 (22-10-2021)

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Attribution - NonCommercial

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Saliha Si Ahmed Zennia, Abderrahmane Mati, Christophe Charron, Céline Cakir-Kiefer, Alexandre Kriznik, et al.. Effect of nonenzymatic deamidation on the structure stability of Camelus dromedarius α-lactalbumin. Food Chemistry, 2019, 291, pp.207-213. ⟨10.1016/j.foodchem.2019.04.033⟩. ⟨hal-02095313⟩
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