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Optimization of Selective Hydrolysis of Cruciferins for Production of Potent Mineral Chelating Peptides and Napins Purification to Valorize Total Rapeseed Meal Proteins

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  • معلومة اضافية
    • Contributors:
      Laboratoire Réactions et Génie des Procédés (LRGP); Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS); Démarche intégrée pour l'obtention d'aliments de qualité (UMR QualiSud); Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Avignon Université (AU)-Université de La Réunion (UR)-Institut Agro Montpellier; Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Université de Montpellier (UM); Département Performances des systèmes de production et de transformation tropicaux (Cirad-PERSYST); Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)
    • بيانات النشر:
      HAL CCSD
      MDPI
    • الموضوع:
      2022
    • Collection:
      Université d'Avignon et des Pays de Vaucluse: HAL
    • نبذة مختصرة :
      International audience ; Preventing oxidation and microbial spoilage are both major concerns in food industries. In this context, this study aimed to valorize the total rapeseed meal proteins with controlled enzymatic proteolysis to generate potent mineral-chelating peptides from cruciferins while keeping intact the antimicrobial napins. Implementation of proteolysis of total rapeseed protein isolate with the Prolyve® enzyme highlighted an interesting selective hydrolysis of the cruciferins. Hence, the mechanism of this particular hydrolysis was investigated through a Design of Experiments method to obtain a model for the prediction of kinetics (cruciferin degradation and napin purity) according to the operating conditions applied. Then, multicriteria optimization was implemented to maximize the napin purity and yield while minimizing both enzymatic cost and reaction time. Antioxidant assays of the peptide fraction obtained under the optimal conditions proved the high metal-chelating activity preservation (EC50 = 247 ± 27 µg) for more than three times faster production. This fraction might counteract lipid oxidation or serve as preventing agents for micronutrient deficiencies, and the resulting purified napins may have applications in food safety against microbial contamination. These results can greatly help the development of rapeseed meal applications in food industries.
    • الرقم المعرف:
      10.3390/foods11172618
    • الدخول الالكتروني :
      https://hal.science/hal-04036272
      https://hal.science/hal-04036272v1/document
      https://hal.science/hal-04036272v1/file/foods-11-02618-v2%20%282%29.pdf
      https://doi.org/10.3390/foods11172618
    • Rights:
      info:eu-repo/semantics/OpenAccess
    • الرقم المعرف:
      edsbas.38E9246D