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1.
Mar Drugs ; 22(8)2024 Aug 09.
Article in English | MEDLINE | ID: mdl-39195477

ABSTRACT

The inhibition of dipeptidyl peptidase-IV (DPP-IV) is a promising approach for regulating the blood glucose levels in patients with type 2 diabetes (T2D). Oysters, rich in functional peptides, contain peptides capable of inhibiting DPP-IV activity. This study aims to identify the hypoglycemic peptides from oysters and investigate their potential anti-T2D targets and mechanisms. This research utilized virtual screening for the peptide selection, followed by in vitro DPP-IV activity assays to validate the chosen peptide. Network pharmacology was employed to identify the potential targets, GO terms, and KEGG pathways. Molecular docking and molecular dynamics simulations were used to provide virtual confirmation. The virtual screening identified LRGFGNPPT as the most promising peptide among the screened oyster peptides. The in vitro studies confirmed its inhibitory effect on DPP-IV activity. Network pharmacology revealed that LRGFGNPPT exerts an anti-T2D effect through multiple targets and signaling pathways. The key hub targets are AKT1, ACE, and REN. Additionally, the molecular docking results showed that LRGFGNPPT exhibited a strong binding affinity with targets like AKT1, ACE, and REN, which was further confirmed by the molecular dynamics simulations showcasing a stable peptide-target interaction. This study highlights the potential of LRGFGNPPT as a natural anti-T2D peptide, providing valuable insights for potential future pharmaceutical or dietary interventions in T2D management.


Subject(s)
Diabetes Mellitus, Type 2 , Dipeptidyl Peptidase 4 , Dipeptidyl-Peptidase IV Inhibitors , Molecular Docking Simulation , Peptides , Diabetes Mellitus, Type 2/drug therapy , Dipeptidyl-Peptidase IV Inhibitors/pharmacology , Dipeptidyl-Peptidase IV Inhibitors/chemistry , Dipeptidyl-Peptidase IV Inhibitors/isolation & purification , Animals , Dipeptidyl Peptidase 4/metabolism , Dipeptidyl Peptidase 4/chemistry , Peptides/pharmacology , Peptides/chemistry , Peptides/isolation & purification , Humans , Molecular Dynamics Simulation , Hypoglycemic Agents/pharmacology , Hypoglycemic Agents/chemistry , Ostreidae/chemistry , Network Pharmacology , Drug Discovery
2.
Mar Drugs ; 22(8)2024 Aug 07.
Article in English | MEDLINE | ID: mdl-39195475

ABSTRACT

Pearl and nacre powders have been valuable traditional Chinese medicines with whitening properties for thousands of years. We utilized a high-temperature and high-pressure method along with compound enzyme digestion to prepare the enzymatic hydrolysates of nacre powder of Pinctada martensii (NP-PMH). The peptides were identified using LC-MS/MS and screened through molecular docking and molecular dynamics simulations. The interactions between peptides and tyrosinase were elucidated through enzyme kinetics, circular dichroism spectropolarimetry, and isothermal titration calorimetry. Additionally, their inhibitory effects on B16F10 cells were explored. The results showed that a tyrosinase-inhibitory peptide (Ala-His-Tyr-Tyr-Asp, AHYYD) was identified, which inhibited tyrosinase with an IC50 value of 2.012 ± 0.088 mM. The results of the in vitro interactions showed that AHYYD exhibited a mixed-type inhibition of tyrosinase and also led to a more compact enzyme structure. The binding reactions of AHYYD with tyrosinase were spontaneous, leading to the formation of a new set of binding sites on the tyrosinase. The B16F10 cell-whitening assay revealed that AHYYD could reduce the melanin content of the cells by directly inhibiting the activity of intracellular tyrosinase. Additionally, it indirectly affects melanin production by acting as an antioxidant. These results suggest that AHYYD could be widely used as a tyrosinase inhibitor in whitening foods and pharmaceuticals.


Subject(s)
Enzyme Inhibitors , Melanins , Molecular Docking Simulation , Monophenol Monooxygenase , Peptides , Pinctada , Animals , Monophenol Monooxygenase/antagonists & inhibitors , Peptides/pharmacology , Peptides/chemistry , Peptides/isolation & purification , Mice , Enzyme Inhibitors/pharmacology , Enzyme Inhibitors/chemistry , Melanins/antagonists & inhibitors , Cell Line, Tumor , Melanoma, Experimental/drug therapy , Molecular Dynamics Simulation , Computer Simulation , Antioxidants/pharmacology , Antioxidants/chemistry , Antioxidants/isolation & purification
3.
Mar Drugs ; 22(9)2024 Sep 15.
Article in English | MEDLINE | ID: mdl-39330301

ABSTRACT

For thousands of years, pearl and nacre powders have been important traditional Chinese medicines known for their skin whitening effects. To prepare the enzymatic hydrolysates of Hyriopsis cumingii nacre powder (NP-HCH), complex enzymatic hydrolysis by pineapple protease and of neutral protease was carried out after the powder was pre-treated with a high-temperature and high-pressure method. The peptides were identified using LC-MS/MS and picked out through molecular docking and molecular dynamics simulations. Subsequently, the tyrosinase inhibitory and antioxidant properties of novel tyrosinase inhibitory peptides were investigated in vitro. In addition, the enzymatic activity of tyrosinase in B16F10 cells as well as melanin content and antioxidant enzyme levels were also examined. The results showed that a tyosinase inhibitory peptide (Tyr-Pro-Asn-Pro-Tyr, YPNPY) with an efficient IC50 value of 0.545 ± 0.028 mM was identified. The in vitro interaction results showed that YPNPY is a reversible competitive inhibitor of tyrosinase, suggesting that it binds to the free enzyme. The B16F10 cell whitening test revealed that YPNPY can reduce the melanin content of B16F10 cells by directly inhibiting the activity of intracellular tyrosinase. Additionally, it indirectly affects melanin production by acting as an antioxidant. These results suggest that YPNPY could be widely used as a tyrosinase inhibitor in whitening foods and drugs.


Subject(s)
Antioxidants , Melanins , Molecular Docking Simulation , Monophenol Monooxygenase , Peptides , Monophenol Monooxygenase/antagonists & inhibitors , Animals , Peptides/pharmacology , Peptides/chemistry , Peptides/isolation & purification , Mice , Antioxidants/pharmacology , Antioxidants/chemistry , Enzyme Inhibitors/pharmacology , Enzyme Inhibitors/chemistry , Cell Line, Tumor , Melanoma, Experimental/drug therapy , Computer Simulation , Tandem Mass Spectrometry , Skin Lightening Preparations/pharmacology , Skin Lightening Preparations/chemistry , Skin Lightening Preparations/isolation & purification , Molecular Dynamics Simulation
4.
Molecules ; 29(4)2024 Feb 18.
Article in English | MEDLINE | ID: mdl-38398650

ABSTRACT

Oysters contain significant amounts of the zinc element, which may also be found in their proteins. In this study, a novel zinc-binding protein was purified from the mantle of the oyster Magallana hongkongensis using two kinds of gel filtration chromatograms. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that its molecular weight was approximately 36 kDa. The protein identified by the Q-Exactive mass spectrometer shared the highest sequence identity with carbonic anhydrase derived from Crassostrea gigas concerning amino acid sequence similarity. Based on homologous cloning and RACE PCR, the full-length cDNA of carbonic anhydrase from Magallana hongkongensis (designated as MhCA) was cloned and sequenced. The cDNA of MhCA encodes a 315-amino-acid protein with 89.74% homology to carbonic anhydrase derived from Crassostrea gigas. Molecular docking revealed that the two zinc ions primarily form coordination bonds with histidine residues in the MhCA protein. These results strongly suggest that MhCA is a novel zinc-binding protein in Magallana hongkongensis.


Subject(s)
Carbonic Anhydrases , Carrier Proteins , Crassostrea , Animals , DNA, Complementary/genetics , Molecular Docking Simulation , Cloning, Molecular , Crassostrea/metabolism , Carbonic Anhydrases/metabolism , Zinc
5.
Microb Pathog ; 182: 106260, 2023 Sep.
Article in English | MEDLINE | ID: mdl-37467812

ABSTRACT

Although Vibrio parahaemolyticus infections cause severe diseases of large yellow croaker (Larimichthys crocea), using antibiotics and other chemical agents to treat these infections could result in antimicrobial resistance, environmental pollution, and other associated problems. This study identified seven peptides from Lacticaseibacillus paracasei fermentation broth using ultra-high-performance liquid chromatography-mass spectrometry and screened antimicrobial peptide Y2Fr (VEIKNGLLKLNGKPLLIR) through its net charge, hydrophobicity and predicted secondary structure. Antibacterial activity analysis revealed that Y2Fr had a minimum inhibitory concentration (MIC) of 125 µg/mL, minimum bactericidal concentration (MBC) of 250 µg/mL against V. parahaemolyticus and a time-kill of 3 h. In a bacterial membrane environment, the secondary structure of peptide Y2Fr changed from a random coil to a ß-sheet to enhance its membrane permeability and binding to bacteria DNA to exert its antibacterial effect. Further molecular docking analysis revealed that peptide Y2Fr could bind to the membrane protein KKI11460.1 and DNA polymerase A0A0L8TVA4 of V. parahaemolyticus through hydrogen bonds. Meanwhile, treatment of Y2Fr with mammalian red blood cells and plasma revealed that it was noncytotoxic, nonhemolytic, and stable under physiological conditions. Thus, peptide Y2Fr has great potential use in treating and preventing infections caused by V. parahaemolyticus or similar bacteria in aquatic animals.


Subject(s)
Perciformes , Vibrio parahaemolyticus , Animals , Vibrio parahaemolyticus/genetics , Lacticaseibacillus , Fermentation , Molecular Docking Simulation , Anti-Bacterial Agents/chemistry , Peptides/pharmacology , Peptides/metabolism , Perciformes/metabolism , Bacteria/metabolism , Mammals/metabolism
6.
Crit Rev Food Sci Nutr ; : 1-20, 2023 Nov 15.
Article in English | MEDLINE | ID: mdl-37966171

ABSTRACT

Taste peptides are oligopeptides that enhance both aroma and taste of food, and they are classified into five categories based on their taste characteristics: salty, sour, umami, sweet, bitter, and kokumi peptide. Recently, taste peptides have attracted the attention of several fields of research in food science and commercial applications. However, research on taste receptors of taste peptides and their taste transduction mechanisms are not clearly understood and we present a comprehensive review about these topics here. This review covers the aspects of taste peptides perceived by their receptors in taste cells, the proposed transduction pathway, as well as structural features of taste peptides. Apart from traditional methods, molecular docking, peptidomic analysis, cell and animal models and taste bud biosensors can be used to explore the taste mechanism of taste peptides. Furthermore, synergistic effect, Maillard reaction, structural modifications and changing external environment are employed to improve the taste of taste peptides. Consequently, we discussed the current challenges and future trends in taste peptide research. Based on the summarized developments, taste peptides derived from food proteins potentially appear to be important taste substances. Their applications meet the principles of "safe, nutritious and sustainable" in food development.

7.
Mar Drugs ; 20(12)2022 Nov 28.
Article in English | MEDLINE | ID: mdl-36547896

ABSTRACT

This study aimed to purify and identify antiphotoaging peptides from oyster (Crassostrea hongkongensis) protein enzymatic hydrolysates (OPEH) and to investigate the possible mechanism underlying its antiphotoaging effect. Multiple methods (Ultrafiltration, G25 Chromatography, RP-HPLC, and LC/MS/MS) had been used for this purpose, and eventually, two peptides, including WNLNP and RKNEVLGK, were identified. Particularly, WNLNP exerted remarkable antiphotoaging effect on the UVB-irradiated HaCaT photoaged cell model in a dose-dependent manner. WNLNP exerted its protective effect mainly through inhibiting ROS production, decreasing MMP-1 expression, but increasing extracellular pro-collagen I content. Furthermore, WNLNP downregulated p38, JNK, ERK, and p65 phosphorylation in the MAPK/NF-κB signaling pathway and attenuated bax over-expressions but reversed bcl-2 reduction in UVB- irradiated HaCaT cells. The molecular docking analysis showed that WNLNP forms five and seven hydrogen bonds with NF-κB (p65) and MMP-1, respectively. This study suggested that a pentapeptide WNLNP isolated from OPEH had great potential to prevent and regulate skin photoaging.


Subject(s)
Crassostrea , Oligopeptides , Skin Aging , Animals , Humans , Crassostrea/chemistry , HaCaT Cells , Matrix Metalloproteinase 1/metabolism , Molecular Docking Simulation , NF-kappa B/metabolism , Skin Aging/drug effects , Tandem Mass Spectrometry , Ultraviolet Rays/adverse effects , Oligopeptides/chemistry , Oligopeptides/isolation & purification , Oligopeptides/pharmacology
8.
Food Chem ; 463(Pt 4): 141514, 2024 Oct 02.
Article in English | MEDLINE | ID: mdl-39378722

ABSTRACT

To elucidate the correlation between variations in thermal hysteresis activity (THA) and the physicochemical properties and structure, antifreeze peptides (AFPs) of isolated fractions (CCP-1 and CCP-2) were characterized on based peptidomics and bioinformatics. The results revealed a positive correlation between the THA of cod collagen antifreeze peptide (CCAFP) and peptide chain length, isoelectric point, and hydrophobic amino acid content. Notably, the THA of CCP-1, which has higher alkaline amino acid content, was 2.60 °C at a concentration of 10 mg/mL, significantly higher than CCP (1.90 °C) and CCP-2 (2.27 °C). Glycine, proline, and valine were the vital amino acids to the formation of hydrogen bonds. Conversely, aspartic and glutamic acids at terminal regions of AFPs tended to introduce kinks in their structures. This distortion reduced binding sites for ice crystals, thereby decreasing their THA, providing a theory for understanding the physicochemical properties and structure of AFPs that influence their THA.

9.
Front Nutr ; 11: 1365282, 2024.
Article in English | MEDLINE | ID: mdl-38515524

ABSTRACT

In this study, the antimicrobial mechanism of plasma-activated water (PAW) against Vibrio parahaemolyticus and the effectiveness of PAW in artificially contaminated Litopenaeus vannamei were investigated. The results demonstrated a significant reduction (p < 0.05) in viable counts of V. parahaemolyticus with increasing plasma discharge time (5, 10, 20, and 30 min) and PAW immersion time (3, 5, 10, 20, and 30 s). Specifically, the count of V. parahaemolyticus decreased by 2.1, 2.7, 3.3, and 4.4 log CFU/mL after exposed to PAW 5, PAW 10, PAW 20, and PAW 30 for 30 s, respectively. Significant cell surface wrinkling, accompanied by notable nucleic acid and protein leakage were observed after treatment with PAW. The permeability of the inner and outer cell membranes was significantly increased (p < 0.05), along with an increase in electrical conductivity (p < 0.05). The reactive oxygen species (ROS) within V. parahaemolyticus cells were significantly increased (p < 0.05), while superoxide dismutase (SOD) activity, and the relative expression of the ompW, emrD, and luxS genes were significantly decreased (p < 0.05). A reduction number of 1.3, 1.8, 2.1, and 2.2 log CFU/g of V. parahaemolyticus in artificially contaminated L. vannamei was obtained with PAW for 5 min. The study elucidated that PAW could destroy cell membranes, leading to cell death. The findings would strengthen strategies for V. parahaemolyticus control and provide a potential application of PAW for preserving aquatic products.

10.
Foods ; 13(6)2024 Mar 14.
Article in English | MEDLINE | ID: mdl-38540873

ABSTRACT

In our previous study, two peptides with favorable anti-inflammatory effects, Asp-Gln-Thr-Phe (DQTF) and Gly-Tyr-Thr-Arg (GYTR), were screened from Ruditapes philippinarum using an in vitro-in silico strategy. The present study aims to investigate the ameliorative effect of Ruditapes philippinarum peptides (RPPs) on acute inflammation and clarify the potential mechanism through in vitro and in vivo experiments. The anti-inflammatory effects of DQTF and GYTR were verified with a lipopolysaccharide (LPS)-induced RAW264.7 cell acute inflammation model and the anti-inflammatory effect of the enzymatic hydrolysates of Ruditapes philippinarum was explored in vivo using an LPS-induced acute inflammatory injury model in mice. The results show that DQTF and GYTR improved the morphology of LPS-injured cells and decreased the concentrations of tumor necrosis factor (TNF)-α and interleukin (IL)-6 in LPS-induced cells. Moreover, the antioxidant enzyme activity in cells was markedly increased with DQTF and GYTR. The enzymatic hydrolysates of Ruditapes philippinarum were obtained with hydrolysis using pepsin-chymotrypsin-trypsin (PeCTHC) and pepsin-trypsin (PeTHC), respectively. PeCTHC and PeTHC significantly reduced pro-inflammatory cytokines and nitric oxide (NO) in the serum. Additionally, the blood indices and levels of superoxide dismutase (SOD), glutathione peroxidase (GSH-PX), and malondialdehyde (MDA) in the livers of mice were markedly improved with RPPs administration. In conclusion, RPPs have preventive and protective effects on acute inflammation, with significant prospects for development in the field of functional foods.

11.
Heliyon ; 10(5): e26980, 2024 Mar 15.
Article in English | MEDLINE | ID: mdl-38463779

ABSTRACT

In this study, we have developed a novel fluorescent "OFF-ON" quantum dots (QDs) sensor based on CdTe/CdS/SiO2 cores. Ammonium pyrrolidine dithiocarbamate (APDC), ethylenediamine tetraacetic acid (EDTA), and 1,10-phenanthroline (Phen) served as potential chemical etchants. Among these three etchants, APDC exhibited the most pronounced quenching effect (94.06%). The APDC-etched CdTe/CdS/SiO2 QDs demonstrated excellent optical properties: the fluorescence of the APDC-etched CdTe/CdS/SiO2 QDs system (excitation wavelength: 365 nm and emission wavelength: 622 nm) was significantly and selectively restored upon the addition of cadmium ions (Cd2+) (89.22%), compared to 15 other metal ions. The linear response of the APDC-etched CdTe/CdS/SiO2 QDs was observed within the cadmium ion (Cd2+) concentration ranges of 0-20 µmol L-1 and 20-160 µmol L-1 under optimized conditions (APDC: 300 µmol L-1, pH: 7.0, reaction time: 10 min). The detection limit (LOD) of the APDC-etched CdTe/CdS/SiO2 QDs for Cd2+ was 0.3451 µmol L-1 in the range of 0-20 µmol L-1. The LOD achieved by the QDs in this study surpasses that of the majority of previously reported nanomaterials. The feasibility of using APDC-etched CdTe/CdS/SiO2 QDs for Cd2+ detection in seawater, freshwater, and milk samples was verified, with average recoveries of 95.27%-110.68%, 92%-106.47%, and 90.73%-111.60%, respectively, demonstrating satisfactory analytical precision (RSD ≤ 8.26).

12.
Food Chem ; 442: 138464, 2024 Jun 01.
Article in English | MEDLINE | ID: mdl-38245988

ABSTRACT

An oyster peptide (OPs)-loaded composite nanogel based on carboxymethyl cellulose and carboxymethyl chitosan (CMC@CMCS@OPs) was prepared, and the characterization, absorption and transport mechanism were further investigated. CMC@CMCS@OPs, a dense spherical microstructure with a diameter of ∼64 nm, which enhanced the thermal and digestive stabilities of individual OPs and improved its retention rate of hypoglycemic activity in vitro. The swelling response and in-vitro release profiles showed that CMC@CMCS@OPs could help OPs achieve targeted and controlled release in the intestine. In addition, CMC@CMCS@OPs had no cytotoxicity on Caco-2 cells, and its apparent permeability coefficients increased 4.70-7.45 times compared with OPs, with the absorption rate increased by 129.38 %. Moreover, the transcytosis of CMC@CMCS@OPs nanogel occurred primarily through the macropinocytosis pathway, endocytosis pathway and intestinal efflux transporter-mediated efflux. Altogether, these results suggested that CMC@CMCS@OPs nanogel could be as an effective OPs delivery device for enhancing its stability and absorption.


Subject(s)
Carboxymethylcellulose Sodium , Chitosan , Polyethylene Glycols , Polyethyleneimine , Humans , Carboxymethylcellulose Sodium/chemistry , Nanogels , Caco-2 Cells , Chitosan/chemistry , Peptides
13.
Foods ; 13(15)2024 Jul 29.
Article in English | MEDLINE | ID: mdl-39123582

ABSTRACT

Colitis causes inflammation, diarrhoea, fever, and other serious illnesses, posing a serious threat to human health and safety. Current medications for the treatment of colitis have serious side effects. Therefore, the new strategy of creating a defence barrier for immune function by adding anti-inflammatory foods to the daily diet is worth advocating for. Low-molecular weight oyster peptides (LOPs) are a natural food with anti-inflammatory activity extracted from oysters, so intervention with LOPs is likely to be an effective preventive solution. The aim of this study was to investigate the preventive effect of LOPs on lipopolysaccharide (LPS)-induced acute colitis inflammation in mice and its underlying mechanism. The results showed that LOPs not only inhibited the colonic histopathy in mice induced by LPS-induced inflammation but also reduced the inflammatory response in the blood. In addition, LOPs significantly increased the number of beneficial bacteria (Alistipes, Mucispirillum, and Oscillospira), decreased the number of harmful bacteria (Coprobacillus, Acinetobater) in the intestinal microbiota, and further affected the absorption and utilisation of short-chain fatty acids (SCFAs) in the intestinal tract. In conclusion, dietary supplementation with LOPs is a promising health-promoting dietary supplement and nutraceutical for the prevention of acute colitis by reducing the inflammatory response and modulating the intestinal microbial communities.

14.
Food Chem ; 451: 139471, 2024 Sep 01.
Article in English | MEDLINE | ID: mdl-38692241

ABSTRACT

To compare the bioavailability of protein-binding zinc, we investigated the impact of baking on the structure of zinc-binding proteins. The results showed that zinc-binding proteins enriched in zinc with relative molecular weights distributed at 6 kDa and 3 kDa. Protein-binding zinc is predisposed to separate from proteins' interiors and converge on proteins' surface after being baked, and its structure tends to be crystalline. Especially -COO, -C-O, and -C-N played vital roles in the sites of zinc-binding proteins. However, baking did not affect protein-binding zinc's bioavailability which was superior to that of ZnSO4 and C12H22O14Zn. They were digested in the intestine, zinc-binding complexes that were easily transported and uptaken by Caco-2 cells, with transport and uptake rates as high as 62.15% and 15.85%. Consequently, baking can alter the conformation of zinc-binding proteins without any impact on protein-binding zinc's bioavailability which is superior to that of ZnSO4 and C12H22O14Zn.


Subject(s)
Biological Availability , Ostreidae , Zinc , Humans , Caco-2 Cells , Animals , Zinc/metabolism , Zinc/chemistry , Ostreidae/chemistry , Ostreidae/metabolism , Cooking , Carrier Proteins/chemistry , Carrier Proteins/metabolism , Hot Temperature , Protein Binding , Shellfish/analysis
15.
Food Chem X ; 18: 100695, 2023 Jun 30.
Article in English | MEDLINE | ID: mdl-37234402

ABSTRACT

Cold plasma (CP) is a non-thermal novel technology for the processing of heat-sensitive food products, but there is concern regarding its impact on food quality. Voltage is one of the most direct factors affecting the bacteriostatic effect of CP. Golden pompano (Trachinotus ovatus) was treated with CP at different voltages (10, 20, and 30 kV). The total viable count decreased as the CP voltage increased, reaching a maximum reduction of 1.54 lg CFU/g on golden pompano treated at 30 kV. No effects on water-holding capacity, pH, total volatile base nitrogen, and T2b relaxation time were observed, indicating that all CP treatments retained the freshness and bound water of the samples. However, as the CP voltage increased, peroxide value and thiobarbituric acid-reactive substances of golden pompano gradually increased, the protein tertiary structure unfolded, and α-helices converted to ß-sheets, indicating inevitable lipid and protein oxidation caused by excessive CP voltage. Therefore, a suitable voltage of CP should be selected to inhibits the growth of microorganisms, which avoids deterioration of sea-foods quality.

16.
Foods ; 12(11)2023 May 25.
Article in English | MEDLINE | ID: mdl-37297379

ABSTRACT

Oysters are nutritious and tasty but difficult to store. Drying can extend the storage period of oysters and give them a unique flavor. In this study, the effects of four drying procedures, namely, vacuum freeze drying (VFD), vacuum drying (VD), natural sun-drying (NSD), and hot air drying (HAD), on the flavor characteristics of oysters (Crassostrea hongkongensis) were investigated using blanched oysters as a control (CK). Results showed that HAD produced more free amino acids than the other methods, but VFD retained the most flavor nucleotides. Compared with cold drying (VFD), hot drying (VD, NSD, and HAD) increased the abundance of organic acids, betaine, and aroma substances. Glutamic acid, alanine, AMP, hexanal, octanal, heptanal, (E, E)-2,4-heptadienal, (E)-2-decenal, nonanal, etc., are defined as the characteristic flavor compounds of dried oysters, with umami, sweet, green, fatty, and fruity aromas being the main organoleptic attributes of dried oysters. Glutamic acid, glycine, betaine, IMP, pentanal, ethyl heptanoate, (E, Z)-2,4-nonadienal, 1-octen-3-one, 2-hexenal, 2-octenal, hexanal, decanal were defined as markers to distinguish different drying methods. Overall, HAD showed improved flavor qualities and characteristics and was better suited for the highly commercialized production of dried oysters.

17.
Food Chem ; 407: 135119, 2023 May 01.
Article in English | MEDLINE | ID: mdl-36512910

ABSTRACT

In this study, we investigated the effects of cold atmospheric plasma (CAP) technology on endogenous enzyme characteristics and muscle protein properties of the golden pomfret (Trachinotus ovatus) under different treatment power and time conditions. Results showed that the enzymatic activity of cathepsin B, L, and calpain in crude protease extracts (CPE) decreased significantly as the treatment power and treatment time of CAP increased (p < 0.05). Oxidative degradation of the CPE after exposure to CAP resulted in significant changes in the structure, total sulfhydryl, and carbonyl content of the CPE (p < 0.05). CAP of an appropriate intensity resulted in significant improvements in the color parameters, hydration properties, and textural property parameters of muscle proteins (p < 0.05). These results suggest that CAP, as a non-thermophysical modification technique, can inhibit the activity of endogenous enzymes as well as alter the protein function in food.


Subject(s)
Muscle Proteins , Plasma Gases , Animals , Plasma Gases/pharmacology , Fishes
18.
Foods ; 12(9)2023 Apr 26.
Article in English | MEDLINE | ID: mdl-37174342

ABSTRACT

The increasing threat posed by antibiotic-resistant pathogens has prompted a shift to the use of naturally-derived antimicrobial peptides (AMPs) in place of chemical preservatives in controlling foodborne pathogens. In this study, ten peptides were identified from salt-fermented shrimps (Penaeus vannamei) using ultra-performance liquid chromatography-mass spectrometry. One of the peptides, designated PV-Q5 (QVRNFPRGSAASPSALASPR), with most features of an AMP, was further explored and found to possess strong antibacterial activity against Vibrio parahaemolyticus and Escherichia coli, with a minimum inhibitory concentration of 31.25 µg/mL. Moreover, PV-Q5 increased bacterial cell membrane permeability and ruptured bacteria cell membranes, as revealed by transmission electron microscopy. Circular dichroism analysis showed that the conformation of PV-Q5 was a random coil in phosphate-buffered saline and α-helical in sodium dodecyl sulfate, which is conducive for interaction with bacteria cell membranes. These findings indicated that PV-Q5 could find potential use in food preservation to control foodborne pathogenic bacteria.

19.
Foods ; 12(21)2023 Oct 24.
Article in English | MEDLINE | ID: mdl-37959003

ABSTRACT

In order to realize the multi-level utilization of marine shellfish resources and to develop the potential biological activity of processing by-products of Atrina pectinata, gelatin was extracted from the mantle and the potential whitening effect of its enzymatic peptides was explored. Taking tyrosinase inhibitory activity as the evaluation index, the enzyme hydrolysate process was optimized by response-surface methodology, and the optimal enzyme hydrolysate conditions were as follows: pH 5.82, 238 min enzyme hydrolysate time, and temperature of 54.5 °C. Under these conditions, the tyrosinase inhibition activity of Atrina pectinata mantle gelatin peptide (APGP) was 88.6% (IC50 of 3.268 ± 0.048 mg/mL). The peptides obtained from the identification were separated by ultrafiltration and LC-MS/MS, and then four new peptides were screened by molecular docking, among which the peptide Tyr-Tyr-Pro (YYP) had the strongest inhibitory effect on tyrosinase with an IC50 value of 1.764 ± 0.025 mM. The molecular-docking results indicated that hydrogen bonding is the main driving force for the interaction of the peptide YYP with tyrosinase. From the Lineweaver-Burk analysis, it could be concluded that YYP is inhibitory to tyrosinase and exhibits a mixed mechanism of inhibition. These results suggest that YYP could be widely used as a tyrosinase inhibitor in whitening foods and pharmaceuticals.

20.
Food Sci Nutr ; 11(5): 2418-2426, 2023 May.
Article in English | MEDLINE | ID: mdl-37181326

ABSTRACT

This study was to examine the protective effects of curcumin/cyclodextrin polymer inclusion complex (CUR/CDP) on ethanol-induced liver injury in mice and to explore its potential mechanisms. In the ethanol-induced acute injury mouse model, the effects of pretreatment with silymarin, cyclodextrin polymer (CDP), curcumin (CUR) and CUR/CDP at low, middle, and high doses were evaluated by biochemical and histopathological examination. The liver index, alanine aminotransferase (ALT), aspartate aminotransferase (AST), and lactate dehydrogenase (LDH) levels in serum of the mice were measured. The superoxide dismutase (SOD), glutathione peroxidase (GSH-PX) activities, and malondialdehyde (MDA) level in liver tissue were assessed by assay kits. Moreover, hematoxylin-eosin (HE) staining was carried out to observe pathological changes of liver. Western blotting was performed for determining the changes in the expressions of DNA damage-associated proteins. The results showed that compared with the control group, the liver index and the levels of ALT, AST, LDH, and MDA in the ethanol treatment group were significantly increased and the activities of GSH-Px and SOD were obviously decreased. However, pretreatment with silymarin, CUR, and CUR/CDP reversed the change of above indicators except CDP. Moreover, CUR/CDP at high dose further weakened the liver index, inhibited the biochemical indexes, and enhanced the activities of antioxidant enzymes to a greater extent than silymarin and CUR. Western blot analysis indicated that CUR/CDP significantly down-regulated the expressions of DNA damage-related proteins including p-ATM, γ-H2AX, p-p53, and p-p38MAPK, which inhibited ethanol-induced the G2/M arrest and ultimately prevented liver function from oxidative stress injury. These results indicated that CUR/CDP possessed good protective effect on mice liver damage in vivo by increasing the activities of GSH-Px and SOD to suppress DNA damage.

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