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Theses

L'alpha-lactalbumine : susceptibilité à la protéolyse liée aux changements conformationnels induits thermiquement : Recherche de peptides à activité anti-oxydante

Abstract : The MG-like state is the main form at 70°C and the protein is completely hydrolysed for 1 min of incubation at this temperature. The 1-58 amino-terminal and 95-123 carboxy-terminal regions of a-lactalbumin in its MG-like state are quickly hydrolysed by thermolysin, whereas the central region, which includes the binding site of calcium, is more resistant toward the hydrolysis at 70°C. Peptides with antioxidant activity have been identified in thermolysic hydrolysates from bovine and equine a-lactalbumins. Their concentration that decreases by 50% the concentration of the 2,2'-azinobis(3-ethylbenzothiazolin-6-sulfonic acid) radical cation is lower than 10 mM. These antioxydant peptides, that are homologous for the two species, are in general short and contain within their sequences one or two aromatic amino acid residues or a disulphide bridge. To conclude, the hydrolysis of a-lactalbumin at high temperature by a thermostable protease makes it possible to generate peptides with antioxidant activity.
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Theses
File URL :
http://docnum.univ-lorraine.fr/prive/SCD_T_2006_0051_N_NEGUE.pdf
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https://hal.univ-lorraine.fr/tel-01746857
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Submitted on : Thursday, March 29, 2018 - 10:46:13 AM
Last modification on : Friday, February 5, 2021 - 3:43:00 AM

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  • HAL Id : tel-01746857, version 1

Citation

Marie-Andrée N'Negue. L'alpha-lactalbumine : susceptibilité à la protéolyse liée aux changements conformationnels induits thermiquement : Recherche de peptides à activité anti-oxydante. Biochimie [q-bio.BM]. Université Henri Poincaré - Nancy 1, 2006. Français. ⟨NNT : 2006NAN10051⟩. ⟨tel-01746857⟩

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