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.
journal_name
Food Chemjournal_title
Food chemistryauthors
Si Ahmed Zennia S,Mati A,Charron C,Cakir-Kiefer C,Kriznik A,Girardet JMdoi
10.1016/j.foodchem.2019.04.033subject
Has Abstractpub_date
2019-09-01 00:00:00pages
207-213eissn
0308-8146issn
1873-7072pii
S0308-8146(19)30682-Xjournal_volume
291pub_type
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