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1.
Mar Drugs ; 22(4)2024 Apr 03.
Artículo en Inglés | MEDLINE | ID: mdl-38667779

RESUMEN

With the aim to upcycle fish side-streams, enzymatic hydrolysis is often applied to produce protein hydrolysates with bioactive properties or just as a protein source for food and feed. However, the production of hydrolysates generates a side-stream. For underutilized fish and fish backbone this side-stream will contain fish bones and make it rich in minerals. The aim of this study was to assess the relative bioaccessibility (using the standardized in vitro model INFOGEST 2.0) of minerals in a dietary supplement compared to bone powder generated after enzymatic hydrolysis of three different fish side-streams: undersized whole hake, cod and salmon backbones consisting of insoluble protein and bones. Differences in the bioaccessibility of protein between the powders were also investigated. The enzyme hydrolysis was carried out using different enzymes and hydrolysis conditions for the different fish side-streams. The content and bioaccessibility of protein and the minerals phosphorus (P), calcium (Ca), potassium (K) and magnesium (Mg) were measured to evaluate the potential of the powder as an ingredient in, e.g., dietary supplements. The bone powders contained bioaccessible proteins and minerals. Thus, new side-streams generated from enzymatic hydrolysis can have possible applications in the food sector due to bioaccessible proteins and minerals.


Asunto(s)
Huesos , Suplementos Dietéticos , Minerales , Alimentos Marinos , Animales , Huesos/metabolismo , Hidrólisis , Salmón/metabolismo , Disponibilidad Biológica , Proteínas de Peces/metabolismo , Peces/metabolismo , Hidrolisados de Proteína/química , Polvos
2.
Mar Drugs ; 22(7)2024 Jun 27.
Artículo en Inglés | MEDLINE | ID: mdl-39057406

RESUMEN

This study generated bioactive hydrolysates using the enzyme Alcalase and autolysis from mesopelagic fish, including Maurolicus muelleri and Benthosema glaciale. Generated hydrolysates were investigated for their bioactivities using in vitro bioassays, and bioactive peptides were identified using mass spectrometry in active hydrolysates with cyclooxygenase, dipeptidyl peptidase IV and antioxidant activities. In silico analysis was employed to rank identified peptide sequences in terms of overall bioactivity using programmes including Peptide Ranker, PrepAIP, Umami-MRNN and AntiDMPpred. Seven peptides predicted to have anti-inflammatory, anti-type 2 diabetes or Umami potential using in silico strategies were chemically synthesised, and their anti-inflammatory activities were confirmed using in vitro bioassays with COX-1 and COX-2 enzymes. The peptide QCPLHRPWAL inhibited COX-1 and COX-2 by 82.90% (+/-0.54) and 53.84%, respectively, and had a selectivity index greater than 10. This peptide warrants further research as a novel anti-inflammatory/pain relief peptide. Other peptides with DPP-IV inhibitory and Umami flavours were identified. These offer potential for use as functional foods or topical agents to prevent pain and inflammation.


Asunto(s)
Antiinflamatorios , Proteínas de Peces , Peces , Péptidos , Hidrolisados de Proteína , Animales , Hidrolisados de Proteína/farmacología , Hidrolisados de Proteína/química , Péptidos/farmacología , Péptidos/química , Péptidos/aislamiento & purificación , Antiinflamatorios/farmacología , Antiinflamatorios/química , Proteínas de Peces/farmacología , Proteínas de Peces/química , Antioxidantes/farmacología , Antioxidantes/química , Ciclooxigenasa 2/metabolismo , Simulación por Computador , Inhibidores de la Dipeptidil-Peptidasa IV/farmacología , Inhibidores de la Dipeptidil-Peptidasa IV/química , Inhibidores de la Dipeptidil-Peptidasa IV/aislamiento & purificación , Ciclooxigenasa 1/metabolismo , Inhibidores de la Ciclooxigenasa/farmacología , Inhibidores de la Ciclooxigenasa/química
3.
Mar Drugs ; 21(11)2023 Oct 25.
Artículo en Inglés | MEDLINE | ID: mdl-37999376

RESUMEN

Fish by-catches, along with other fish side-streams, were previously used as raw material for the production of fishmeal and fish oil but appropriate handling allows their use in more valuable options. The aim of this research was to valorize undersized hake (Merluccius merluccius) as a model of using fish by-catch from the Bay of Biscay to produce protein hydrolysates with bioactivities. Six enzymes, with different proteolytic activities (endo- or exoproteases) and specificities, were tested to produce protein hydrolysates. Products obtained with an endoprotease of serine resulted in the most promising results in terms of protein extraction yield (68%), with an average molecular weight of 2.5 kDa, and bioactivity yield (antioxidant activity = 88.5 mg TE antioxidant capacity/g fish protein; antihypertensive activity = 47% inhibition at 1 mg/mL). Then, process conditions for the use of this enzyme to produce bioactive products were optimized using Box-Behnken design. The most favorable process conditions (time = 2 h, solids = 50% and enzyme/substrate = 2% with respect to protein) were scaled up (from 0.5 L to 150 L reactor) to confirm laboratory scale and model forecasts. The results obtained in the pilot-scale testing matched the outcomes predicted by the model, confirming the technical viability of the proposed process.


Asunto(s)
Gadiformes , Perciformes , Animales , Hidrólisis , Gadiformes/metabolismo , Hidrolisados de Proteína/química , Péptidos/química , Antihipertensivos/farmacología , Peces/metabolismo , Perciformes/metabolismo , Antioxidantes/farmacología , Antioxidantes/metabolismo
4.
Heliyon ; 10(5): e27030, 2024 Mar 15.
Artículo en Inglés | MEDLINE | ID: mdl-38468971

RESUMEN

Fish protein hydrolysates were obtained from cultured rainbow trout (Oncorhynchus mykiss) viscera using commercial and endogenous enzymes. Two methods were employed for hydrolysis: acid autolysis (also known as silage) at room temperature for 10 days in acidic conditions, until total solubilisation, and enzymatic hydrolysis using Alcalase 2.4 LFG, Protana Prime, and the endogenous enzymes in the viscera. The effectiveness of both methods in releasing free amino acids (FAA) was assessed. After evaluating the results, the most effective enzymatic hydrolysis was optimized. The findings indicated that enzymatic hydrolysis with Alcalase, Protana Prime and endogenous enzymes combined for 7 h at a dose of 1% of protein, and a 7-day acid autolysis yielded the highest degree of hydrolysis (83.8% and 75.8%), a yield of FAA from viscera of 5.9% and 3.2%, and a yield of FAA from total protein of 71.3% and 52.5%, respectively. In conclusion, the use of commercial enzymes was more efficient in releasing amino acids, but endogenous enzymes showed a strong proteolytic capacity during acid autolysis, suggesting it also as a promising method to produce FAA-rich hydrolysates.

6.
Food Chem ; 136(3-4): 1370-6, 2013 Feb 15.
Artículo en Inglés | MEDLINE | ID: mdl-23194537

RESUMEN

A new quantitative structure activity relationship (QSAR) model is established for oligopeptides that inhibit angiotensin I-converting enzyme (ACE). Information concerning the C-terminal pentapeptide is considered to describe the peptide structure in the model. A database is constructed, with 263 ACE inhibitory peptides and 38 physicochemical descriptors, abstracted from the published literature. The model is generated through a generalised linear model, with a gamma distribution that yields a coefficient of determination of 94.4%. The whole C-terminal pentapeptide information is a determinant for modelling the ACE inhibition activity of oligopeptides. Starting from the C-terminus, the C-1 position is the most relevant position in the model; this is followed by position C-4. In C-1, there is a preference for aliphatic and tiny residues. However, in the C-4 position, the model indicates a clear preference for bulky hydrophobic amino acids and for sulphur-containing amino acids. Due to its good predictive capability, this model could be used as a tool for identifying and prioritizing the potential ACE inhibitory peptides present in a complex matrix.


Asunto(s)
Inhibidores de la Enzima Convertidora de Angiotensina/química , Oligopéptidos/química , Inhibidores de la Enzima Convertidora de Angiotensina/farmacología , Cinética , Modelos Teóricos , Oligopéptidos/farmacología , Relación Estructura-Actividad Cuantitativa
7.
N Biotechnol ; 30(6): 647-55, 2013 Sep 25.
Artículo en Inglés | MEDLINE | ID: mdl-23689042

RESUMEN

By-products generated every year by the European fruit and cereal processing industry currently exceed several million tons. They are disposed of mainly through landfills and thus are largely unexploited sources of several valuable biobased compounds potentially profitable in the formulation of novel food products. The opportunity to design novel strategies to turn them into added value products and food ingredients via novel and sustainable processes is the main target of recently EC-funded FP7 project NAMASTE-EU. NAMASTE-EU aims at developing new laboratory-scale protocols and processes for the exploitation of citrus processing by-products and wheat bran surpluses via the production of ingredients useful for the formulation of new beverage and food products. Among the main results achieved in the first two years of the project, there are the development and assessment of procedures for the selection, stabilization and the physical/biological treatment of citrus and wheat processing by-products, the obtainment and recovery of some bioactive molecules and ingredients and the development of procedures for assessing the quality of the obtained ingredients and for their exploitation in the preparation of new food products.


Asunto(s)
Citrus , Industria de Procesamiento de Alimentos , Residuos Industriales , Triticum , Administración de Residuos , Unión Europea , Industria de Procesamiento de Alimentos/métodos , Industria de Procesamiento de Alimentos/organización & administración , Industria de Procesamiento de Alimentos/tendencias , Humanos , Administración de Residuos/métodos , Administración de Residuos/normas
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