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Functional, bioactive and antigenicity properties of blue whiting protein hydrolysates: effect of enzymatic treatment and degree of hydrolysis.
García-Moreno, Pedro J; Pérez-Gálvez, Raúl; Espejo-Carpio, F Javier; Ruiz-Quesada, Cristina; Pérez-Morilla, Ana I; Martínez-Agustín, Olga; Guadix, Antonio; Guadix, Emilia M.
Afiliación
  • García-Moreno PJ; Department of Chemical Engineering, University of Granada, 18071, Granada, Spain.
  • Pérez-Gálvez R; Department of Chemical Engineering, University of Granada, 18071, Granada, Spain.
  • Espejo-Carpio FJ; Department of Chemical Engineering, University of Granada, 18071, Granada, Spain.
  • Ruiz-Quesada C; Department of Chemical Engineering, University of Granada, 18071, Granada, Spain.
  • Pérez-Morilla AI; Department of Chemical Engineering, University of Granada, 18071, Granada, Spain.
  • Martínez-Agustín O; Department of Biochemistry and Molecular Biology II, University of Granada, 18071, Granada, Spain.
  • Guadix A; Department of Chemical Engineering, University of Granada, 18071, Granada, Spain.
  • Guadix EM; Department of Chemical Engineering, University of Granada, 18071, Granada, Spain.
J Sci Food Agric ; 97(1): 299-308, 2017 Jan.
Article en En | MEDLINE | ID: mdl-27012152
BACKGROUND: Fish discards represent an important under-utilisation of marine resources. This study evaluated the up-grading of the protein fraction of blue whiting (Micromesistius poutassou) discards by the production of fish protein hydrolysates (FPHs) exhibiting functional, antioxidant, angiotensin-I converting enzyme (ACE)-inhibitory and antigenicity properties. RESULTS: FPHs with low DH (4%) showed better emulsifying, foaming and oil binding capacities, particularly those obtained using only trypsin. FPHs with DH 4% exhibited also the stronger antioxidant activity, especially the one obtained using only subtilisin (IC50 = 1.36 mg protein mL-1 ). The presence of hydrophobic residues at the C-terminal of the FPH produced using subtilisin also led to the stronger ACE-inhibitory activity. However, FPHs with high DH (12%), which implies a higher proportion of short peptides, was required to enhance ACE-inhibition (IC50 = 172 µg protein mL-1 ). The antigenic levels of the FPH were also reduced with DH independently of the enzymatic treatment. Nevertheless, the highest degradation of fish allergens (e.g. parvalbumin) was also obtained when using only subtilisin. CONCLUSION: These results suggest that added-value products for food applications can be produced from the protein fraction of discards. © 2016 Society of Chemical Industry.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hidrolisados de Proteína / Alimentos Marinos / Proteínas de Peces / Gadiformes Límite: Animals Idioma: En Revista: J Sci Food Agric Año: 2017 Tipo del documento: Article País de afiliación: España Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hidrolisados de Proteína / Alimentos Marinos / Proteínas de Peces / Gadiformes Límite: Animals Idioma: En Revista: J Sci Food Agric Año: 2017 Tipo del documento: Article País de afiliación: España Pais de publicación: Reino Unido