Utilisation of fish industry residuals: Screening the taurine concentration and angiotensin converting enzyme inhibition potential in cod and salmon

Dragnes, Bjørn Tore; Stormo, Svein Kristian; Larsen, Roger B.; Ernstsen, Hege Holm; Elvevoll, Edel O.

doi:10.1016/j.jfca.2009.01.020

Cited by 25 publications

(10 citation statements)

References 15 publications

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“…The results suggest that the increasing inhibition with the time of proteolysis is likely due to the accumulation of biological active peptides. This is in concordance with previous reports of ACE-inhibitory activities identified in muscle and by-products of fish such as Alaska pollock, blue whiting and cod ( Byun and Kim, 2001 ; Dragnes et al, 2009b ; Geirsdottir et al, 2011 ; Jensen et al, 2014 ). The determined IC50 values reflect that the ACE-inhibitory activity was measured directly in the hydrolysates without any further concentration by e.g freeze drying of the peptides.…”

Section: Resultssupporting

confidence: 93%

“…The determined IC50 values reflect that the ACE-inhibitory activity was measured directly in the hydrolysates without any further concentration by e.g freeze drying of the peptides. This is evident from the results in Table 5 reporting a higher protein concentration in μg/ml needed to reach the IC50 compared to previous reports based on analysis of freeze dried hydrolysates ( Byun and Kim, 2001 ; Dragnes et al, 2009b ; Geirsdottir et al, 2011 ; Jensen et al, 2014 ). However, the main purpose of the measurement was fulfilled as the result demonstrate that biological activity is retained despite the multiple thermal treatments of raw-material proteins during the processing to WFM.…”

Section: Resultsmentioning

confidence: 53%

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Nutritional and functional properties of fishmeal produced from fresh by-products of cod ( Gadus morhua L .) and saithe ( Pollachius virens )

Ween

Stangeland

Fylling

et al. 2017

Heliyon

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Fresh by-products of whitefish such as cod and saithe is processed to fishmeal (FM) on-board seagoing Norwegian trawlers. The aim of this study was to document the properties of whitefish FM (WFM) protein with respect to, physicochemical and bioactive properties. Analysis of the proximate composition of representative seasonal WFM batches show that the production is robust without much variance. The mean protein (61.9 ± 1.2), fat (8.9 ± 1.1%), moisture (5 ± 1.2%) and ash content (22.4 ± 0.8%), reflect the use of lean and bony raw-material. The WFM has a low content of free amino acids (0.7%) and biogenic amines (< 1000 mg/kg) that confirm the high quality and freshness of the raw material. Amino-acid analysis identified the presence of all nutritionally essential amino acids. The WFM physicochemical properties was comparable to soy-bean meal (SBM) by analysis of solubility, water-holding capacity (WHC), the emulsion stability (ES). Proteolytic degradation of the WFM was used to demonstrate the presence of bioactive peptides with inhibiting activity against angiotensin-converting enzyme (ACE) activity, in vitro. Taken together, WFM produced from fresh by-products is an excellent protein source with attributes of interest beyond the aquafeed-market.

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Section: Resultssupporting

confidence: 93%

Section: Resultsmentioning

confidence: 53%

Nutritional and functional properties of fishmeal produced from fresh by-products of cod ( Gadus morhua L .) and saithe ( Pollachius virens )

Ween

Stangeland

Fylling

et al. 2017

Heliyon

View full text Add to dashboard Cite

show abstract

“…Bioactive peptides can be released by proteolysis of food proteins (Ukeda and others ; Mullally and others ; Dragnes and others ; Lee and others ; Jimsheena and Gowda ). To produce ACEIP, ribbonfish backbone was hydrolyzed using various commercial digestive enzymes, and acid protease was selected as the best enzyme (Wang and others ).…”

Section: Resultsmentioning

confidence: 99%

Purification, Identification, and In Vivo Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptide, from Ribbonfish (Trichiurus haumela) Backbone

Zou

Wang

et al. 2013

Journal of Food Science

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Ribbonfish (Trichiurus haumela) backbone is normally discarded as an industrial waste from fish processing. A method of developing angiotensin I-converting enzyme inhibitory (ACEI) peptides from ribbonfish backbone was previously optimized. The purposes of the study were to characterize the active peptides in the hydrolysate and to evaluate its in vivo activity. Ribbonfish backbone protein hydrolysate prepared by acid protease was fractionated into 4 fractions (I, MW < 1 kDa; II, MW = 1 to 5 kDa; III, MW = 5 to 10 kDa; and IV, MW > 10 kDa) through ultrafiltration membranes. Fraction I, showing the highest ACEI activity, was further purified using consecutive chromatographic techniques including gel filtration and reversed phase high-performance liquid chromatography. The purified ACE inhibitory peptide was determined to have a molecular weight of 317.25 Da, with a sequence of Leu-Trp and an IC₅₀ value of 5.6 μM. Systolic blood pressure of spontaneously hypertensive rats was significantly decreased from 181 ± 2.0 to 161.3 ± 2.3 mm Hg after 4 h of oral administration of Leu-Trp at a dose of 10 mg/kg of body weight. These results indicated that ribbonfish backbone protein could be used for development of antihypertensive agent.

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“…Only enriched fractions from grass carp scale hydrolysates showed a similar activity (IC 50 = 0.13 mg mL −1 ) [29] and hydrolysates of salmon and cod skin, performed as simulated gastro-intestinal digestion, showed a slightly higher activity (IC 50 = 0.10 mg mL −1 ). [32] The generally higher activity of hydrolysates from fish skin and scales in comparison to heads and viscera might be related to their high content of collagen. Collagen is rich in Pro residues which, when present in the C-terminal sequence of released peptides, are associated with high ACE-I activity.…”

Section: Ace-inhibitory Activitymentioning

confidence: 99%

Angiotensin-I converting enzyme inhibitory and antioxidant activity of bioactive peptides produced by enzymatic hydrolysis of skin from grass carp (Ctenopharyngodon idella)

Jie-rong¹,

Gobba²,

Skibsted³

et al. 2016

International Journal of Food Properties

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Grass carp skin pieces were homogenized in water and hydrolyzed by Alcalase®, collagenase, proteinase K, and/or trypsin at their optimum conditions. Samples were taken at various degrees of hydrolysis and were evaluated for antioxidant, antimicrobial, and angiotensin-converting enzyme inhibitory activities. Alcalase and collagenase completely hydrolyzed the skin with different rates, and released peptides with antioxidant and angiotensin-converting enzyme-inhibitory activity. These activities increased linearly with increasing degrees of hydrolysis. Subsequent incubation of the collagenase hydrolysates with trypsin slightly increased the antioxidant activity. Proteinase K, although only partially hydrolyzing the skin, also catalyzed the release of peptides with antioxidant and angiotensin-converting enzyme-inhibitory activities. These results show that skin byproducts from grass carp can be a source of bioactive peptides produced by a one-step reaction. Such hydrolysates may be applied in food products to prolong shelf life and provide beneficial effects on blood pressure.

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Utilisation of fish industry residuals: Screening the taurine concentration and angiotensin converting enzyme inhibition potential in cod and salmon

Cited by 25 publications

References 15 publications

Nutritional and functional properties of fishmeal produced from fresh by-products of cod ( Gadus morhua L .) and saithe ( Pollachius virens )

Nutritional and functional properties of fishmeal produced from fresh by-products of cod ( Gadus morhua L .) and saithe ( Pollachius virens )

Purification, Identification, and In Vivo Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptide, from Ribbonfish (Trichiurus haumela) Backbone

Angiotensin-I converting enzyme inhibitory and antioxidant activity of bioactive peptides produced by enzymatic hydrolysis of skin from grass carp (Ctenopharyngodon idella)

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