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1.
Front Nutr ; 10: 1136490, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-36998903

RESUMO

In this study, we analyzed the eicosapentaenoic acid/docosahexaenoic acid (EPA/DHA) lipid composition of fish oil obtained through enzymatic treatment, fractional distillation and silica gel column purification, and further assessed EPA/DHA bioavailability. Lipid subclass composition information was obtained through ultra-performance liquid chromatography-electrospray ionization tandem mass spectrometry (UPLC-ESI-MS/MS), and bioavailability tests were performed using the Caco-2 cell monolayer model. Results showed that enzymatic treatment improved the incorporation of EPA/DHA as diacylglycerol (DG) while silica gel column chromatography enriched the content of EPA/DHA as phosphatidylglycerol (PG) (12.58%) and phosphatidylethanolamine (PE) (4.99%). Furthermore, increasing the purity of EPA/DHA could improve its bioavailability and after 24 incubation, binding forms of triglyceride (TG) was superior to ethyl ester (EE) (p < 0.05) at the same purity level. Those findings are helpful to provide research basis for exploring the bioactivity of fish oil.

2.
Foods ; 11(22)2022 Nov 17.
Artigo em Inglês | MEDLINE | ID: mdl-36429278

RESUMO

Cold Atmospheric Plasma (CAP) is a novel non-thermal preservation method that extends the shelf-life of food. Therefore, this study investigated the effect of CAP on the quality parameters of hairtail (Trichiurus lepturus) during cold storage conditions (at 4 °C and RH range 45−55%). For that reason, different quality parameters including the total bacteria count (TBC), total volatile basic nitrogen (TVB-N), pH, thiobarbituric acid reacting substances value (TBARS), color, texture, and sensory evaluation have been measured. The hairtail was exposed to CAP at 50 kV voltage for 2, 3, 4, and 5 min. The results showed that the samples treated with CAP at 50 kV for 5 min had significantly lower (p < 0.05) TBC (7.04 ± 0.26 log CFU/g) compared with the control sample (8.69 ± 0.06 log CFU/g). Similar results were found concerning TVB-N, which strongly decreased in the treated samples (16.63 ± 0.03 mg N/100 g) in comparison with the control sample (22.79 ± 0.03 mg N/100 g). In addition, the CAP-treated samples had lower (p < 0.05) changes in color than those of the control group. With reference to the sensory evaluation, the shelf-life of CAP-treated samples (at 50 kV for 5 min) was longer than the untreated samples by about 6 days. These results led us to the conclusion that CAP can effectively delay spoilage and deterioration, slow the rise in pH, and maintain the sensory attributes of hairtail during cold storage conditions.

3.
Mar Drugs ; 13(4): 1993-2009, 2015 Apr 03.
Artigo em Inglês | MEDLINE | ID: mdl-25854645

RESUMO

In the current study, the preparation conditions of neutrase hydrolysate (SMH) from skate (Raja porosa) muscle protein were optimized using orthogonal L9(3)4 tests, and R values indicated that pH was the most important factor affecting HO· scavenging activity of SMH. Under the optimum conditions of pH 7.0, enzymolysis temperature 60 °C, enzyme/substrate ratio (E/S) 2%, and enzymolysis time 5 h, EC50 of SMH on HO· was 2.14 ± 0.17 mg/mL. Using ultrafiltration, gel filtration chromatography, and RP-HPLC, two novel antioxidant nonapeptides (SP-A and SP-B) were isolated from SMH and their amino acid sequences were found to be APPTAYAQS (SP-A) and NWDMEKIWD (SP-B) with calculated molecular masses of 904.98 Da and 1236.38 Da, respectively. Both showed strong antioxidant activities. SP-A and SP-B exhibited good scavenging activities on HO· (EC50 0.390 and 0.176 mg/mL), DPPH· (EC50 0.614 and 0.289 mg/mL), and O2-· (EC50 0.215 and 0.132 mg/mL) in a dose-dependent manner. SP-B was also effective against lipid peroxidation in the model system. The aromatic (2Trp), acidic (2Asp and Glu), and basic (Lys) amino acid residues within the sequences of SP-B might account for its pronounced antioxidant activity. The results of this study suggested that protein hydrolysate and peptides from skate muscle might be effective as food additives for retarding lipid peroxidation occurring in foodstuffs.


Assuntos
Antioxidantes/isolamento & purificação , Proteínas de Peixes/isolamento & purificação , Conservantes de Alimentos/isolamento & purificação , Músculo Esquelético/química , Oligopeptídeos/isolamento & purificação , Fragmentos de Peptídeos/isolamento & purificação , Rajidae , Sequência de Aminoácidos , Animais , Antioxidantes/química , Antioxidantes/metabolismo , Endopeptidases/metabolismo , Proteínas de Peixes/química , Proteínas de Peixes/metabolismo , Conservantes de Alimentos/química , Conservantes de Alimentos/metabolismo , Alimentos Congelados/análise , Alimentos Congelados/economia , Concentração de Íons de Hidrogênio , Peroxidação de Lipídeos , Peso Molecular , Oligopeptídeos/química , Oligopeptídeos/metabolismo , Fragmentos de Peptídeos/química , Fragmentos de Peptídeos/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Alimentos Marinhos/análise , Alimentos Marinhos/economia
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