Parthsarathy, Vadivel;
McLaughlin, Christopher M.;
Harnedy, Padraigin A.;
Allsopp, Philip J.;
Crowe, William;
McSorley, Emeir M.;
FitzGerald, Richard J.;
O'Harte, Finbarr P. M.
Boarfish (Capros aper) protein hydrolysate has potent insulinotropic and GLP‐1 secretory activity in vitro and acute glucose lowering effects in mice
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Media type:
E-Article
Title:
Boarfish (Capros aper) protein hydrolysate has potent insulinotropic and GLP‐1 secretory activity in vitro and acute glucose lowering effects in mice
Contributor:
Parthsarathy, Vadivel;
McLaughlin, Christopher M.;
Harnedy, Padraigin A.;
Allsopp, Philip J.;
Crowe, William;
McSorley, Emeir M.;
FitzGerald, Richard J.;
O'Harte, Finbarr P. M.
imprint:
Wiley, 2019
Published in:International Journal of Food Science & Technology
Description:
<jats:title>Summary</jats:title><jats:p>The anti‐diabetic actions of a boarfish protein hydrolysate (<jats:styled-content style="fixed-case">BPH</jats:styled-content>) were investigated in cultured cells and mice. A boarfish (<jats:italic>Capros aper</jats:italic>) muscle protein hydrolysate was generated using the enzymes Alcalase 2.4 L and Flavourzyme 500 L. Furthermore, the <jats:styled-content style="fixed-case">BPH</jats:styled-content> was subjected to simulated gastrointestinal digestion (<jats:styled-content style="fixed-case">SGID</jats:styled-content>). <jats:styled-content style="fixed-case">BPH</jats:styled-content> and <jats:styled-content style="fixed-case">SGID</jats:styled-content> samples (0.01–2.5 mg mL<jats:sup>−1</jats:sup>) were tested <jats:italic>in vitro</jats:italic> for <jats:styled-content style="fixed-case">DPP</jats:styled-content>‐<jats:styled-content style="fixed-case">IV</jats:styled-content> inhibition and insulin and <jats:styled-content style="fixed-case">GLP</jats:styled-content>‐1 secretory activity from <jats:styled-content style="fixed-case">BRIN</jats:styled-content>‐<jats:styled-content style="fixed-case">BD</jats:styled-content>11 and <jats:styled-content style="fixed-case">GLUT</jats:styled-content>ag cells, respectively. The <jats:styled-content style="fixed-case">BPH</jats:styled-content> and <jats:styled-content style="fixed-case">SGID</jats:styled-content> samples, caused a dose‐dependent increase (4.2 to 5.3‐fold, <jats:italic>P</jats:italic> < 0.001) in insulin secretion from <jats:styled-content style="fixed-case">BRIN</jats:styled-content>‐<jats:styled-content style="fixed-case">BD</jats:styled-content>11 cells and inhibited <jats:styled-content style="fixed-case">DPP</jats:styled-content>‐<jats:styled-content style="fixed-case">IV</jats:styled-content> activity (<jats:styled-content style="fixed-case">IC</jats:styled-content><jats:sub>50</jats:sub> 1.18 ± 0.04 and 1.21 ± 0.04 mg mL<jats:sup>−1</jats:sup>), respectively. The <jats:styled-content style="fixed-case">SGID</jats:styled-content> sample produced a 1.3‐fold (<jats:italic>P</jats:italic> < 0.01) increase in <jats:styled-content style="fixed-case">GLP</jats:styled-content>‐1 secretion. An oral glucose tolerance test (<jats:styled-content style="fixed-case">OGTT</jats:styled-content>) was conducted in healthy mice (<jats:italic>n</jats:italic> = 8), with or without <jats:styled-content style="fixed-case">BPH</jats:styled-content> (50 mg/kg bodyweight). <jats:styled-content style="fixed-case">BPH</jats:styled-content> mediated an increase in plasma insulin levels (<jats:styled-content style="fixed-case">AUC</jats:styled-content><jats:sub>(0–120 min),</jats:sub> <jats:italic>P</jats:italic> < 0.05) and a consequent reduction in blood glucose concentration (<jats:italic>P</jats:italic> < 0.01), after <jats:styled-content style="fixed-case">OGTT</jats:styled-content> in mice versus controls. The <jats:styled-content style="fixed-case">BPH</jats:styled-content> showed potent anti‐diabetic actions in cells and improved glucose tolerance in mice.</jats:p>