TY - JOUR
T1 - Functional, bioactive and antigenicity properties of blue whiting protein hydrolysates: Effect of enzymatic treatment and degree of hydrolysis
AU - García Moreno, Pedro Jesús
AU - Pérez-Gálvez, Raúl
AU - Espejo-Carpio, F. Javier
AU - Ruiz-Quesada, Cristina
AU - Pérez-Morilla, Ana I.
AU - Martínez-Agustín, Olga
AU - Guadix, Antonio
AU - Guadix, Emilia M.
PY - 2016
Y1 - 2016
N2 - 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 = 1.36mg 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 = 172μg 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.
AB - 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 = 1.36mg 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 = 172μg 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.
KW - Agronomy and Crop Science
KW - Food Science
KW - Nutrition and Dietetics
KW - Biotechnology
KW - ACE-inhibitory activity
KW - Antigenicity
KW - Antioxidant activity
KW - Discards
KW - Fish protein hydrolysates
KW - Functional properties
U2 - 10.1002/jsfa.7731
DO - 10.1002/jsfa.7731
M3 - Journal article
C2 - 27012152
SN - 0022-5142
JO - Journal of the Science of Food and Agriculture
JF - Journal of the Science of Food and Agriculture
ER -