Bioactivities of fish protein hydrolysates from defatted salmon backbones

[Display omitted] •Defatted bulk fish protein hydrolysates (FPH) exhibit many bioactivities.•Defatted FPH inhibit lipid oxidation.•Defatted FPH reduce blood pressure and glucose uptake into enterocyte.•Trypsin, Bromelain+Papain and Protamex lead to the most bioactive hydrolysates.•Prolonged hydrolys...

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Veröffentlicht in:Biotechnology reports (Amsterdam, Netherlands) Netherlands), 2016-09, Vol.11 (C), p.99-109
Hauptverfasser: Slizyte, Rasa, Rommi, Katariina, Mozuraityte, Revilija, Eck, Peter, Five, Kathrine, Rustad, Turid
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Sprache:eng
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Zusammenfassung:[Display omitted] •Defatted bulk fish protein hydrolysates (FPH) exhibit many bioactivities.•Defatted FPH inhibit lipid oxidation.•Defatted FPH reduce blood pressure and glucose uptake into enterocyte.•Trypsin, Bromelain+Papain and Protamex lead to the most bioactive hydrolysates.•Prolonged hydrolysis gives higher bioactivities. Bioactivities of bulk fish protein hydrolysates (FPH) from defatted salmon backbones obtained with eight different commercial enzymes and their combinations were tested. All FPH showed antioxidative activity in vitro. DPPH scavenging activity increased, while iron chelating ability decreased with increasing time of hydrolysis. All FPH showed ACE inhibiting effect which depended on type of enzyme and increased with time of hydrolysis. The highest effect was found for FPH produced with Trypsin. Bromelain+Papain hydrolysates reduced the uptake of radiolabelled glucose into CaCo-2 cells, a model of human enterocytes, indicating a potential antidiabetic effect of FPH. FPH obtained by Trypsin, Bromelain+Papain and Protamex showed the highest ACE inhibitory, cellular glucose transporter (GLUT/SGLT) inhibitory and in vitro antioxidative activities, respectively. Correlation was observed between the measured bioactivities, degree of hydrolysis and molecular weight profiles, supporting prolonged hydrolysis to obtain high bioactivities.
ISSN:2215-017X
2215-017X
DOI:10.1016/j.btre.2016.08.003