Peptide identification in a salmon gelatin hydrolysate with antihypertensive, dipeptidyl peptidase IV inhibitory and antioxidant activities

Neves, Adriana da Costa; Harnedy, Pádraigín A.; O’Keeffe, Martina B.; Alashi, Monisola A.; Aluko, Rotimi E.; Fitzgerald, Richard J.

doi:10.1016/j.foodres.2017.06.065

Cited by 124 publications

(71 citation statements)

References 42 publications

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“…Salmon protein hydrolysates/peptides exhibit antidiabetic activity in vitro and in vivo. In previous studies we have shown that muscle protein and gelatin hydrolysates derived from Atlantic salmon trimmings inhibit dipeptidyl peptidase-IV (DPP-IV) in vitro (Neves, Harnedy, O'Keeffe, Alashi, et al, 2017;. This was also seen with hydrolysates generated from salmon muscle protein and salmon skin derived gelatin (Falkenberg, Stagsted, & Nielsen, 2014;Li-Chan, Hunag, Jao, Ho, & Hsu, 2012).…”

Section: Accepted Manuscriptmentioning

confidence: 85%

“…and Flavourzyme 500L from salmon trimmings had more potent DPP-IV inhibitory activity than those generated with Alcalase 2.4L and Promod 144MG (Neves, Harnedy, O'Keeffe, Alashi, et al, 2017;. However, the IC 50 values obtained herein for hydrolysates generated from salmon skin gelatin (0.90 ± 0.05 mg/mL) and trimmings derived proteins (0.84 ± 0.04 mg/mL), with Alcalase 2.4L and Flavourzyme 500L, were significantly higher than values obtained previously for salmon trimmings derived gelatin (0.55 mg/mL) and protein (0.10 mg/mL) hydrolysates generated with the same enzymes (Neves, Harnedy, O'Keeffe, Alashi, et al, 2017;. This difference in DPP-IV inhibitory response may be due to the source of the gelatin isolate and the method used to generate the muscle protein hydrolysates.…”

Section: Accepted Manuscriptmentioning

confidence: 86%

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Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides

Harnedy

Parthsarathy²,

McLaughlin³

et al. 2018

Food Research International

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Large quantities of low-value protein rich co-products, such as salmon skin and trimmings, are generated annually. These co-products can be upgraded to high-value functional ingredients. The aim of this study was to assess the antidiabetic potential of salmon skin gelatin and trimmings-derived protein hydrolysates in vitro. The gelatin hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L exhibited significantly higher (p < 0.001) insulin and GLP-1 secretory activity from pancreatic BRIN-BD11 and enteroendocrine GLUTag cells, respectively, when tested at 2.5 mg/mL compared to hydrolysates generated with Alcalase 2.4L or Promod 144MG. The gelatin hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L showed significantly more potent (p < 0.01) DPP-IV inhibitory activity than those generated with Alcalase 2.4L or Promod 144MG. No significant difference was observed in the insulinotropic activity mediated by any of the trimmings-derived hydrolysates when tested at 2.5 mg/mL. However, the trimmings hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L exhibited significantly higher DPP-IV inhibitory (p < 0.05:Alcalase 2.4L and p < 0.01:Promod 144MG) and GLP-1 (p < 0.001, 2.5 mg/mL) secretory activity than those generated with Alcalase 2.4L or Promod 144MG. The salmon trimmings hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L when subjected to simulated gastrointestinal digestion (SGID) was shown to retain its GLP-1 secretory and DPP-IV inhibitory activities, in addition to improving its insulin secretory activity. However, the gelatin hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L was shown to lose GLP-1 secretory activity following SGID. A significant increase in membrane potential (p < 0.001) and intracellular calcium (p < 0.001) by both co-product hydrolysates generated with Alcalase 2.4L and Flavourzyme 500L suggest that both hydrolysates mediate their insulinotropic activity through the K channel-dependent pathway. Additionally, by stimulating a significant increase in intracellular cAMP release (p < 0.05) it is likely that the trimmings-derived hydrolysate may also mediate insulin secretion through the protein kinase A pathway. The results presented herein demonstrate that salmon co-product hydrolysates exhibit promising in vitro antidiabetic activity.

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Section: Accepted Manuscriptmentioning

confidence: 85%

Section: Accepted Manuscriptmentioning

confidence: 86%

Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides

Harnedy

Parthsarathy²,

McLaughlin³

et al. 2018

Food Research International

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“…Others have demonstrated that a collagen hydrolysate exhibited DPP‐IV inhibitory activity and stimulated glucagon‐like‐peptide‐1 (GLP‐1) secretion in vitro (Iba et al ., ). Furthermore, they showed that a collagen hydrolysate also improved glucose tolerance in response to oral glucose in normal mice, which was thought to be mediated partially through enhanced GLP‐1 secretion as well as inhibition of intestinal glucose uptake (Iba et al ., ; Neves et al ., ).…”

Section: Discussionmentioning

confidence: 97%

Boarfish (Capros aper) protein hydrolysate has potent insulinotropic and GLP‐1 secretory activity in vitro and acute glucose lowering effects in mice

Parthsarathy

McLaughlin

Harnedy

et al. 2018

Int J of Food Sci Tech

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The anti-diabetic actions of a boarfish protein hydrolysate (BPH) were investigated in cultured cells and mice. A boarfish (Capros aper) muscle protein hydrolysate was generated using the enzymes Alcalase 2.4 L and Flavourzyme 500 L. Furthermore, the BPH was subjected to simulated gastrointestinal digestion (SGID). BPH and SGID samples (0.01-2.5 mg mL À1 ) were tested in vitro for DPP-IV inhibition and insulin and GLP-1 secretory activity from BRIN-BD11 and GLUTag cells, respectively. The BPH and SGID samples, caused a dose-dependent increase (4.2 to 5.3-fold, P < 0.001) in insulin secretion from BRIN-BD11 cells and inhibited DPP-IV activity (IC 50 1.18 AE 0.04 and 1.21 AE 0.04 mg mL À1 ), respectively. The SGID sample produced a 1.3-fold (P < 0.01) increase in GLP-1 secretion. An oral glucose tolerance test (OGTT) was conducted in healthy mice (n = 8), with or without BPH (50 mg/kg bodyweight). BPH mediated an increase in plasma insulin levels (AUC (0-120 min), P < 0.05) and a consequent reduction in blood glucose concentration (P < 0.01), after OGTT in mice versus controls. The BPH showed potent anti-diabetic actions in cells and improved glucose tolerance in mice.Keywords Boarfish protein hydrolysate, dipeptidyl peptidase-IV inhibition, glucagon-like peptide-1, glycaemic control in mice, insulin secretion.

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“…Collagen can be converted to gelatin by high temperature treatment. Both collagen and gelatin-which contain glycine, proline, and hydroxyproline as the major amino acids-have significant potential as the initial substrates to produce bioactive peptides [11,12]. The biological properties of the derived peptides are largely dependent on the structure and molecular weight.…”

Section: Introductionmentioning

confidence: 99%

Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin

et al. 2020

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Skin waste from tuna processing needs to be utilized, such as extraction of its collagen and gelatin. Their functional properties can be improved by enzymatic hydrolysis for conversion to peptides. Thus, the research objectives were to examine the characteristics and antioxidant activity of collagen, gelatin, and the derived peptide from yellowfin tuna skin. Collagen was extracted using 0.75 M acetic acid at 4 °C, while gelatin was prepared using 0.25% citric acid and extracted at 65 °C. Hydrolysis was carried out with 2% Alcalase, followed by fractionation with a molecular weight cut off sieve for both collagen and gelatin. Collagen yield was 22.6% with pH value of 6.63 and whiteness of 96.7%. Gelatin yield was 20.0% with pH value of 4.94 and whiteness of 51.0%. Hydrolysis for three hours resulted in 52.7% and 45.2% degree of hydrolysis for collagen and gelatin, respectively. The molecular weights of collagen peptides ranged from 2.94 to 11.93 kDa, while those of gelatin peptides ranged from 3.54 to 16,620 kDa. Antioxidant activities of these peptides were higher than those before hydrolysis. The high antioxidant activity (IC50) of collagen peptides were found in <3, 3–10, and 10–30 kDa fractions as well as in the gelatin peptides.

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Peptide identification in a salmon gelatin hydrolysate with antihypertensive, dipeptidyl peptidase IV inhibitory and antioxidant activities

Cited by 124 publications

References 42 publications

Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides

Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides

Boarfish (Capros aper) protein hydrolysate has potent insulinotropic and GLP‐1 secretory activity in vitro and acute glucose lowering effects in mice

Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin

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