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1.
J Sci Food Agric ; 2024 Jun 11.
Artigo em Inglês | MEDLINE | ID: mdl-38860545

RESUMO

BACKGROUND: Morden advanced analytical tools offer valuable information into the understanding of molecular mechanism of traditional food processing. Chopping temperature is well-known to affect the surimi gel quality of silver carp, but the detailed molecular mechanism is not very clear. In this study, a gel-based proteomics was performed on the extracted surimi proteins under different chopping temperatures (0, 5, 10, and 25 °C) along with other physicochemical characterization of surimi proteins and gels. RESULTS: With increased chopping temperature, protein extractability (in 3% sodium chloride) generally decreased, while the extracted protein generally exhibited larger surface hydrophobicity, reduced intrinsic fluorescence intensity, lower sulfhydryl content. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile of extracted protein showed a clear difference at 25 °C when compared with the other three temperatures, and more protein fragmentation occurred. Proteomic analysis of selected bands indicated that major myofibrillar proteins react differently with chopping temperatures, especially at 25 °C. The selected bands contained a variety of other proteins or their fragments, including adenosine triphosphate (ATP) synthase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate isomerase, heat shock protein, parvalbumin, collagen, and so forth. For the surimi gel, water-holding capacity and gel strength generally decreased with increased chopping temperature. CONCLUSION: Our results suggested that chopping at 0-10 °C is acceptable for the production of silver carp surimi in terms of gel strength and water-holding capacity. However, a chopping temperature near 0 °C led to less protein oxidation and denaturation. The inferior gel quality at 25 °C is linked to a decreased concentration of extracted protein and degradation of major myofibrillar protein, the latter is likely crosslinked with sarcoplasmic proteins. © 2024 Society of Chemical Industry.

2.
Crit Rev Food Sci Nutr ; : 1-24, 2023 Aug 17.
Artigo em Inglês | MEDLINE | ID: mdl-37589389

RESUMO

The demand for clean-label starch, perceived as environmentally friendly in terms of production and less hazardous to health, has driven the advancement of food physical processing technologies aimed at modifying starch. One of the key objectives of these modifications has been to reduce the glycaemic potency and increase resistant starch content of starch, as these properties have the potential to positively impact metabolic health. This review provides a comprehensive overview of recent updates in typical physical processing techniques, including annealing, heat-moisture, microwave and ultrasonication, and a brief discussion of several promising recent-developed methods. The focus is on evaluating the molecular, supramolecular and microstructural changes resulting from these modifications and identifying targeted structures that can foster enzyme-digestion resistance in native starch and its forms relevant to food applications. After a comprehensive search and assessment, the current physical modifications have not consistently improved starch enzymatic resistance. The opportunities for enhancing the effectiveness of modifications lie in (1) identifying modification conditions that avoid the intensive disruption of the granular and supramolecular structure of starch and (2) exploring novel strategies that incorporate multi-type modifications.

3.
Molecules ; 28(14)2023 Jul 15.
Artigo em Inglês | MEDLINE | ID: mdl-37513304

RESUMO

In order to clarify the individual role of freezing and frozen storage on the quality of fish, fillets of large-mouth bass (Micropterus salmoides) were subjected to different freezing rates (freezing with -18 °C (A), -60 °C (B), and -60 °C with forced air circulation at 2 m/s (C), respectively) followed by frozen storage at -18 °C for 30 and 90 days. Another two groups were frozen at -60 °C, followed by storage at -40 °C (D) and -60 °C (E), respectively. Results showed that water-holding and TVBN were mainly affected by storage time. No significant changes were found in free thiol content among treatments. A greater freezing rate and lower storage temperature generally led to lower TBARS. GC × GC-TOFMS revealed a total of 66 volatile compounds, which were related to lipid oxidation. PLS-DA showed that fresh samples were separated from the frozen-thawed ones, and fillets in groups D and E were relatively close to fresh fillets in the composition of oxidation-related volatiles. In conclusion, freezing rate and storage temperature had a significant impact on lipid oxidation and protein denaturation in the fillets of large-mouth bass, while protein oxidation was more affected by freezing rate.


Assuntos
Bass , Animais , Congelamento , Temperatura , Lipídeos , Boca , Armazenamento de Alimentos/métodos
4.
Molecules ; 28(16)2023 Aug 21.
Artigo em Inglês | MEDLINE | ID: mdl-37630413

RESUMO

Irradiation can be used for the preservation of chickpea protein as it can destroy microorganisms, bacteria, virus, or insects that might be present. However, irradiation may provoke oxidative stress, and therefore modify the functionality and nutritional value of chickpea protein. In order to study the effects of irradiation on the physicochemical properties and digestion behaviour of chickpea protein, chickpea protein concentrate (CPC) was treated with electron beam irradiation (EBI) at doses of 5, 10, 15, and 20 kGy. After irradiation, protein solubility first increased at 10 kGy and 15 kGy, and then decreased at the higher dose of 20 kGy. This was supported by SDS-PAGE, where the intensity of major protein bands first increased and then decreased. Increased doses of EBI generally led to greater oxidative modification of proteins in CPC, indicated by reduced sulfhydryls and increased carbonyls. In addition, the protein structure was modified by EBI as shown by Fourier transform infrared spectroscopy analysis, where α-helix generally decreased, and ß-sheet increased. Although the protein digestibility was not significantly affected by EBI, the peptidomic analysis of the digests revealed significant differences among CPC irradiated with varying doses. A total of 337 peptides were identified from CPC irradiated with 0 kGy, 10 kGy, and 20 kGy, with 18 overlapping peptides and 60, 29, and 40 peptides specific to the groups of 0, 10, and 20 kGy respectively. Theoretical calculation showed that the distribution of peptide length, hydrophobicity, net charge, and C-terminal residues were affected by irradiation. The 2, 2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity showed a marginal decrease with an increasing dose of irradiation. In conclusion, EBI led to oxidative modification and structural changes in chickpea protein, which subsequently affected the physicochemical properties of peptides obtained from in-vitro digestion of CPC, despite similar digestibility.


Assuntos
Cicer , Elétrons , Eletroforese em Gel de Poliacrilamida , Valor Nutritivo , Estresse Oxidativo
5.
Crit Rev Food Sci Nutr ; : 1-16, 2022 Oct 04.
Artigo em Inglês | MEDLINE | ID: mdl-36193875

RESUMO

Heating is a vital step in the gelation of surimi. Conventional water bath heating (WB) has the advantages of easy operation and low equipment requirements. However, the slow heat penetration during WB may lead to poor gel formation or gels prone to deterioration, especially with one-step heating. The two-step WB is time-consuming, and a large amount of water used tends to cause environmental problems. This review focuses on key factors affecting the quality of surimi gels in various heating technologies, such as surimi protein structure, chemical forces, or the activity of endogenous enzymes. In addition, the relationships between these factors and the gel performance of surimi under various heating modes are discussed by analyzing the heating temperature and heating rate. Compared with WB, the gel performance can be improved by controlling the heating conditions of microwave heating and ohmic heating, which are mainly achieved by changing the molecular structure of myofibrillar proteins or the activity of endogenous enzymes in surimi. Nevertheless, the novel thermal technologies still face several limitations and further research is needed to realize large-scale industrial production. This review provides ideas and directions for developing heat-induced surimi products with excellent gel properties.

6.
Crit Rev Food Sci Nutr ; : 1-20, 2022 Sep 19.
Artigo em Inglês | MEDLINE | ID: mdl-36122384

RESUMO

In addition to microbial spoilage and lipid peroxidation, protein oxidation is increasingly recognized as a major cause for quality deterioration of muscle-based foods. Although protein oxidation in muscle-based foods has attracted tremendous interest in the past decade, specific oxidative pathways and underlying mechanisms of protein oxidation in aquatic products remain largely unexplored. The present review covers the aspects of the origin and site-specific nature of protein oxidation, progress on the characterization of protein oxidation, oxidized proteins in aquatic products, and impact of protein oxidation on protein functionalities. Compared to meat protein oxidation, aquatic proteins demonstrate a less extent of oxidation on aromatic amino acids and are more susceptible to be indirectly oxidized by lipid peroxidation products. Different from traditional measurement of protein carbonyls and thiols, proteomics-based strategy better characterizes the targeted oxidation sites within proteins. The future trends using more robust and accurate targeted proteomics, such as parallel reaction monitoring strategy, to characterize protein oxidation in aquatic products are also given.

7.
Compr Rev Food Sci Food Saf ; 20(6): 5548-5569, 2021 11.
Artigo em Inglês | MEDLINE | ID: mdl-34564951

RESUMO

Over the recent decades,protein oxidation in muscle foods has gained increasing research interests as it is known that protein oxidation can affect eating quality and nutritional value of meat and aquatic products. Protein oxidation occurs during freezing/thawing and frozen storage of muscle foods, leading to irreversible physicochemical changes and impaired quality traits. Controlling oxidative damage to muscle foods during such technological processes requires a deeper understanding of the mechanisms of freezing-induced protein oxidation. This review focus on key physicochemical factors in freezing/thawing and frozen storage of muscle foods, such as formation of ice crystals, freeze concentrating and macromolecular crowding effect, instability of proteins at the ice-water interface, freezer burn, lipid oxidation, and so on. Possible relationships between these physicochemical factors and protein oxidation are thoroughly discussed. In addition, the occurrence of protein oxidation, the impact on eating quality and nutrition, and controlling methods are also briefly reviewed. This review will shed light on the complicated mechanism of protein oxidation in frozen muscle foods.


Assuntos
Alimentos Congelados , Carne , Congelamento , Carne/análise , Músculos , Oxirredução
8.
Crit Rev Food Sci Nutr ; 59(22): 3564-3578, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-30040449

RESUMO

Protein oxidation readily occurs in postmortem muscle during storage and processing. Over the past decade new analytical methods have been developed and new aspects of protein oxidation in meat have been studied, such as the reaction mechanism, and impacts on eating quality and nutritional value. It is now evident that amino acid side chains in myofibrillar proteins undergoes modifications due to oxidative stress. In turn this will lead to formation of new protein-protein cross-links in structural proteins, however, also the overall level of fixed-charge groups attached to the peptide backbones is modified. Meat texture and water-holding are important quality attributes and they are affected by the oxidation of structural proteins. Different mechanisms have been suggested to explain the oxidation-induced quality changes, focusing mainly on reduced proteolysis and formation of cross-links. This review explores the current understanding of protein oxidation in fresh meat in relation to texture and water-holding. The consequences of protein oxidation at molecular level in relation to oxidation-induced cross-linking and changes in net charges of myofibrillar proteins, and the impacts on texture and water-holding are discussed.


Assuntos
Carne , Proteínas , Água , Aminoácidos/química , Aminoácidos/metabolismo , Oxirredução , Proteínas/química , Proteínas/metabolismo , Água/análise
9.
Cell Mol Biol Lett ; 24: 38, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31182966

RESUMO

BACKGROUND: Exploration of the genes with abnormal expression during the development of breast cancer is essential to provide a deeper understanding of the mechanisms involved. Transcriptome sequencing and bioinformatics analysis of invasive ductal carcinoma and paracancerous tissues from the same patient were performed to identify the key genes and signaling pathways related to breast cancer development. METHODS: Samples of breast tumor tissue and paracancerous breast tissue were obtained from 6 patients. Sequencing used the Illumina HiSeq platform. All. Only perfectly matched clean reads were mapped to the reference genome database, further analyzed and annotated based on the reference genome information. Differentially expressed genes (DEGs) were identified using the DESeq R package (1.10.1) and DEGSeq R package (1.12.0). Using KOBAS software to execute the KEGG bioinformatics analyses, enriched signaling pathways of DEGs involved in the occurrence of breast cancer were determined. Subsequently, quantitative real time PCR was used to verify the accuracy of the expression profile of key DEGs from the RNA-seq result and to explore the expression patterns of novel cancer-related genes on 8 different clinical individuals. RESULTS: The transcriptomic sequencing results showed 937 DEGs, including 487 upregulated and 450 downregulated genes in the breast cancer specimens. Further quantitative gene expression analysis was performed and captured 252 DEGs (201 downregulated and 51 upregulated) that showed the same differential expression pattern in all libraries. Finally, 6 upregulated DEGs (CST2, DRP2, CLEC5A, SCD, KIAA1211, DTL) and 6 downregulated DEGs (STAC2, BTNL9, CA4, CD300LG, GPIHBP1 and PIGR), were confirmed in a quantitative real time PCR comparison of breast cancer and paracancerous breast tissues from 8 clinical specimens. KEGG analysis revealed various pathway changes, including 20 upregulated and 21 downregulated gene enrichment pathways. The extracellular matrix-receptor (ECM-receptor) interaction pathway was the most enriched pathway: all genes in this pathway were DEGs, including the THBS family, collagen and fibronectin. These DEGs and the ECM-receptor interaction pathway may perform important roles in breast cancer. CONCLUSION: Several potential breast cancer-related genes and pathways were captured, including 7 novel upregulated genes and 76 novel downregulated genes that were not found in other studies. These genes are related to cell proliferation, movement and adhesion. They may be important for research into breast cancer mechanisms, particularly CST2 and CA4. A key signaling pathway, the ECM-receptor interaction signal pathway, was also identified as possibly involved in the development of breast cancer.


Assuntos
Neoplasias da Mama/genética , Perfilação da Expressão Gênica , Regulação Neoplásica da Expressão Gênica , Receptores de Superfície Celular/metabolismo , Transdução de Sinais/genética , Regulação para Baixo/genética , Feminino , Humanos , Proteínas de Neoplasias/genética , Proteínas de Neoplasias/metabolismo , Reprodutibilidade dos Testes , Análise de Sequência de RNA , Transcriptoma/genética , Regulação para Cima/genética
10.
Sensors (Basel) ; 18(1)2018 Jan 18.
Artigo em Inglês | MEDLINE | ID: mdl-29346289

RESUMO

In this study, we used bands 7, 4, and 3 of the Advance Himawari Imager (AHI) data, combined with a Threshold Algorithm and a visual interpretation method to monitor the entire process of grassland fires that occurred on the China-Mongolia border regions, between 05:40 (UTC) on April 19th to 13:50 (UTC) on April 21st 2016. The results of the AHI data monitoring are evaluated by the fire point product data, the wind field data, and the environmental information data of the area in which the fire took place. The monitoring result shows that, the grassland fire burned for two days and eight hours with a total burned area of about 2708.29 km². It mainly spread from the northwest to the southeast, with a maximum burning speed of 20.9 m/s, a minimum speed of 2.52 m/s, and an average speed of about 12.07 m/s. Thus, using AHI data can not only quickly and accurately track the dynamic development of a grassland fire, but also estimate the spread speed and direction. The evaluation of fire monitoring results reveals that AHI data with high precision and timeliness can be highly consistent with the actual situation.

11.
Sensors (Basel) ; 18(11)2018 Nov 19.
Artigo em Inglês | MEDLINE | ID: mdl-30463259

RESUMO

This paper presents two approaches for the structural damage identification of a bridge from the dynamic response recorded from a test vehicle during its passage over the bridge. Using the acceleration response recorded by the vibration sensors mounted on a test vehicle during its passage over the bridge, along with the computed displacement response, the bending stiffness of the bridge can be determined using either: (1) the frequency-domain method based on the improved directed stiffness method with the identified frequency and corresponding mode shape, or (2) the time-domain method based on the residual vector of the least squares method with a fourth-order displacement moment. By comparing the bending stiffness values identified from the vehicle-collected data for the bridge under the undamaged and damaged states that are monitored regularly by the test vehicle, the bridge damage location and severity can be identified. Through numerical simulations and field tests, the present approaches are shown to be effective and feasible.

12.
Sensors (Basel) ; 14(2): 3207-26, 2014 Feb 18.
Artigo em Inglês | MEDLINE | ID: mdl-24553086

RESUMO

In this paper, an Urban Light Index (ULI) is constructed to facilitate analysis and quantitative evaluation of the process of urbanization and expansion rate by using DMSP/OLS Nighttime Light Data during the years from 1992 to 2010. A unit circle urbanization evaluation model is established to perform a comprehensive analysis of the urbanization process of 34 prefecture-level cities in Northeast China. Furthermore, the concept of urban light space is put forward. In this study, urban light space is divided into four types: the core urban area, the transition zone between urban and suburban areas, suburban area and fluorescent space. Proceeding from the temporal and spatial variation of the four types of light space, the pattern of morphologic change and space-time evolution of the four principal cities in Northeast China (Harbin, Changchun, Shenyang, Dalian) is analyzed and given particular attention. Through a correlation analysis between ULI and the traditional urbanization indexes (urban population, proportion of the secondary and tertiary industries in the regional GDP and the built-up area), the advantages and disadvantages as well as the feasibility of using the ULI in the study of urbanization are evaluated. The research results show that ULI has a strong correlation with urban built-up area (R2 = 0.8277). The morphologic change and history of the evolving urban light space can truly reflect the characteristics of urban sprawl. The results also indicate that DMSP/OLS Nighttime Light Data is applicable for extracting urban space information and has strong potential to urbanization research.

13.
Food Res Int ; 195: 114963, 2024 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-39277235

RESUMO

This study aimed to investigate the effect of oxidation on fish gelatin and its emulsifying properties. Fish gelatin was oxidized with varying concentrations of H2O2 (0-30 mM). Increased concentrations of the oxidant led to a decrease in amino acids in the gelatin, including glycine, lysine, and arginine. Additionally, the relative content of ordered secondary structure and triple helix fractions decreased. Zeta potential decreased, while particle size, surface hydrophobicity, and water contact angle increased. Regarding emulsifying behavior, oxidation promoted the adsorption of gelatin to the oil-water interface and reduced interfacial tension. With increased degrees of oxidation, the zeta potential and size of the emulsion droplets decreased. The oxidized gelatin exhibited better emulsifying activity but worse emulsifying stability. Based on these results, a mechanism for how oxidation affects the emulsifying properties of gelatin was proposed: the increase in gelatin's hydrophobicity and the decrease in triple helix structure induced by oxidation reduced the interfacial tension at the oil-water interface. This promoted protein adsorption at the oil-water interface, allowing the formation of smaller oil droplets and enhancing gelatin's emulsifying activity. However, the decrease in electrostatic repulsion between emulsion droplets and the decrease in solution viscosity increased the flocculation and aggregation of oil droplets, ultimately weakening the emulsifying stability of gelatin.


Assuntos
Emulsões , Proteínas de Peixes , Gelatina , Interações Hidrofóbicas e Hidrofílicas , Oxirredução , Gelatina/química , Emulsões/química , Animais , Proteínas de Peixes/química , Tamanho da Partícula , Peróxido de Hidrogênio/química , Viscosidade , Aminoácidos/química , Tensão Superficial , Emulsificantes/química , Peixes , Adsorção , Estrutura Secundária de Proteína
14.
Food Chem ; 458: 140324, 2024 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-38970954

RESUMO

In order to investigate the effects of multi-frequency ultrasound-assisted immersion freezing (MUIF) on the meat quality of Macrobrachium rosenbergii, tail meat was subjected to different MUIF treatments respectively, namely 20 + 40 kHz (MUIF-20 + 40), 20 + 60 kHz (MUIF-20 + 60), 40 + 60 kHz (MUIF-40 + 60) and 20 + 40 + 60 kHz (MUIF-20 + 40 + 60), and the immersion freezing (IF) as control. Results showed that average diameter of ice crystals was 28 µm in IF, and that was only 8 µm in MUIF-20 + 40 + 60. When compared to IF, MUIF alleviated oxidative deterioration of lipids and proteins, but only at higher ultrasound frequency (MUIF-40 + 60; MUIF-20 + 40 + 60). Carbonyl content of MUIF-20 + 40 + 60 was only 40% of that in IF. Similarly, protein denaturation was inhibited in MUIF (except for MUIF-20 + 40). Transmission electron microscopy showed greater distortion of the ultrastructural components in IF, MUIF-40 + 60, and MUIF-20 + 40 + 60, suggested by bended Z-line. In conclusion, MUIF can be an effective strategy to mitigate mechanical damage and protein deterioration in the meat of Macrobrachium rosenbergii.


Assuntos
Congelamento , Palaemonidae , Animais , Palaemonidae/química , Conservação de Alimentos/métodos , Conservação de Alimentos/instrumentação , Manipulação de Alimentos
15.
J Agric Food Chem ; 72(25): 14364-14374, 2024 Jun 26.
Artigo em Inglês | MEDLINE | ID: mdl-38867641

RESUMO

Cypermethrin (CP) is a neurotoxic insecticide found accumulated in oysters, one of the most commonly consumed seafoods, posing potential health risks to the human body. We designed a gastrointestinal tracing method allowing for accurate quantification of the propulsion of chyme and further established the mouse in vivo digestion model to explore the behavior of CP in the digestion of raw, steamed, and roasted oysters. The results showed that bioaccumulation of CP in oysters may be accompanied by the biotransformation of CP. Thermal processing decreased both the CP content in oysters and its bioaccessibility. The small intestine is the main site for CP digestion and absorption. The cis-isomers of CP might finally accumulate in the body at a higher ratio and further become the predominant configuration for toxic effects. Taken together, the study contributes to the risk assessment of the dietary exposure of CP from aquatic products.


Assuntos
Crassostrea , Digestão , Trato Gastrointestinal , Inseticidas , Piretrinas , Animais , Piretrinas/metabolismo , Piretrinas/análise , Crassostrea/metabolismo , Crassostrea/química , Trato Gastrointestinal/metabolismo , Camundongos , Inseticidas/metabolismo , Inseticidas/química , Isomerismo , Frutos do Mar/análise , Contaminação de Alimentos/análise , Humanos , Masculino , Manipulação de Alimentos/métodos
16.
Food Chem ; 450: 139269, 2024 Aug 30.
Artigo em Inglês | MEDLINE | ID: mdl-38613961

RESUMO

The purpose of this study was to determine the effect of pre-rigor salting on the quality characteristics of surimi gels prepared from snakehead fish muscle. Pre-rigor and post-rigor muscle were mixed with 0.3% or 3% NaCl (w/w) and made into surimi gels, respectively. Results showed that pre-rigor muscle had a higher content of ATP, longer sarcomere, higher pH and greater protein solubility. Metabolic profile suggested that pre-rigor muscle had higher content (a 28-fold increase) of antioxidants such as butyryl-l-carnitine. Transmission electron microscopy showed more damage of mitochondria in post-rigor muscle. Surimi paste from pre-rigor meat chopped with 3% NaCl generally showed greater radical scavenging ability and had higher content of free sulfhydryl. Surimi gel made from pre-rigor muscle salted with 3% NaCl showed a larger gel strength (3.18 kg*mm vs. 2.22 kg*mm) and better water-holding (86% vs. 80%) than that of post-rigor group. Based on these findings, we hypothesized that: In addition to other factors such as pH, degree of denaturation, etc., less protein oxidation in pre-rigor salted surimi also contributes to the improved gel properties.


Assuntos
Produtos Pesqueiros , Proteínas de Peixes , Géis , Oxirredução , Animais , Géis/química , Produtos Pesqueiros/análise , Proteínas de Peixes/química , Cloreto de Sódio/química , Cloreto de Sódio/análise , Peixes , Manipulação de Alimentos , Água/química , Perciformes/metabolismo , Concentração de Íons de Hidrogênio
17.
Food Res Int ; 189: 114547, 2024 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-38876606

RESUMO

Phenolic compounds represent natural compounds endowed with diverse biological functionalities. However, their inherent limitations, characterized by poor water solubility and low oral bioavailability, limit their broader applications. Encapsulation delivery systems are emerging as a remedy, able to ameliorate these limitations by enhancing the stability and solubility of phenolic compounds. In this study, a novel, customized pH-driven approach was developed by determining the optimal deprotonation and protonation points of three different types of polyphenols: ferulic acid, resveratrol, and rhein. The polyphenols were successfully encapsulated in a casein carrier. The solubility, stability, LogD, and LogS curves of the three polyphenols at different pH values were analyzed to identify the optimal deprotonation points for ferulic acid (pH 9), resveratrol (pH 11), and rhein (pH 10). Based on these findings, three different nanoparticles were prepared. The encapsulation efficiencies of the three phenolic compounds were 95.86%, 94.62%, and 94.18%, respectively, and the casein nanoparticles remained stable at room temperature for seven days. FTIR spectroscopy, fluorescence spectroscopy, and molecular docking study substantiated the encapsulation of phenolic compounds within the hydrophobic core of casein-based complexes, facilitated by hydrogen bonding interactions and hydrophobic interactions. Furthermore, the analysis of antioxidant activity elucidated that casein nanoparticles heightened both the water solubility and antioxidant efficacy of the phenolic compounds. This customized encapsulation technique, by establishing a transitional pH value, resolves the challenges of chemical instability and facile degradation of polyphenols under alkaline conditions in the application process of pH-driven methods. It presents novel insights for the application of polyphenols in the domains of food and biomedical fields.


Assuntos
Caseínas , Ácidos Cumáricos , Simulação de Acoplamento Molecular , Polifenóis , Solubilidade , Caseínas/química , Concentração de Íons de Hidrogênio , Polifenóis/química , Ácidos Cumáricos/química , Resveratrol/química , Antraquinonas/química , Nanopartículas/química , Composição de Medicamentos , Espectroscopia de Infravermelho com Transformada de Fourier , Interações Hidrofóbicas e Hidrofílicas , Antioxidantes/química
18.
Food Res Int ; 187: 114357, 2024 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-38763641

RESUMO

The oxidation of fish lipids and proteins is interconnected. The LOX (lipoxygenase)-catalyzed LA (linoleic acid) oxidation system on MPs (myofibrillar proteins) was established in vitro, to investigate the impact of lipoxidation on the physicochemical properties of fish MPs. By detecting HNE (4-hydroxy-2-nonenal) concentration during LA oxidation, the HNE treatment system was established to investigate the role of HNE in this process. In addition, the site specificity of modification on MPs was detected utilizing LC-MS/MS. Both treatments could induce sidechain modification, increase particle size, and cause loss of nutritional value through the reduction in amino acid content of MPs. The HNE group is more likely to alter the MPs' surface hydrophobicity compared to the LA group. By increasing the exposure of modification sites in MPs, the HNE group has more types and number of modifications compared to the LA group. LA group mainly induced the modification of single oxygen addition on MPs instead, which accounted for over 50 % of all modifications. The LA group induced a more pronounced reduction in the solubility of MPs as compared to the HNE group. In conclusion, HNE binding had a high susceptibility to Lys on MPs. Protein aggregation, peptide chain fragmentation, and decreased solubility occurred in the LA group mainly induced by peroxide generated during lipid oxidation or the unreacted LA instead of HNE. This study fills in the mechanism of lipoxidation on protein oxidation in fish and sheds light on the HNE modification sites of MPs, paving the way for the development of oxidation control technology.


Assuntos
Aldeídos , Ácido Linoleico , Oxirredução , Espectrometria de Massas em Tandem , Aldeídos/metabolismo , Animais , Ácido Linoleico/química , Ácido Linoleico/metabolismo , Cromatografia Líquida/métodos , Proteínas de Peixes/metabolismo , Proteínas Musculares/metabolismo , Peixes , Interações Hidrofóbicas e Hidrofílicas , Lipoxigenase/metabolismo , Espectrometria de Massa com Cromatografia Líquida
19.
Int J Biol Macromol ; 260(Pt 2): 129532, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38246447

RESUMO

The pH buffering capacity is an important functionality of muscle proteins, and muscle foods are susceptible to being oxidized during storage and processing. In order to study the effect of oxidation on the pH buffering capacity of myofibrillar proteins, myofibrils extracted from snakehead fish (Channa argus) were oxidized with H2O2. Results showed that increased oxidation led to loss of free sulfhydryl groups, formation of carbonyl groups, increased surface hydrophobicity, and aggregation of myofibrillar proteins. In addition, there was a significant reduction in the content of histidine in oxidized myofibrillar proteins. The pH buffering capacity of myofibrillar proteins significantly decreased from 3.14 ± 0.03 mM H+/(mL × ΔpH) down to 2.55 ± 0.03 mM H+/(mL × ΔpH) after oxidation with 50 mM H2O2. Both oxidized myofibrillar proteins and histidine showed a high pH buffering capacity at pH near 5.8, which is the histidine pKa value. Here, we hypothesize that oxidation-induced changes in the pH buffering capacity of myofibrillar proteins were driven by oxidative modification of histidine and structural changes of myofibrillar proteins. The significance of this study to food industry may be the awareness that protein oxidation may affect pH through changes in buffering capacity. And the use of antioxidants, especially those targeting at histidine will be promising in addressing this issue.


Assuntos
Histidina , Peróxido de Hidrogênio , Animais , Histidina/metabolismo , Peróxido de Hidrogênio/metabolismo , Oxirredução , Proteínas Musculares/química , Concentração de Íons de Hidrogênio , Miofibrilas/química
20.
Food Chem ; 451: 139325, 2024 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-38657519

RESUMO

Muscle protein stability during freeze-thaw (F-T) cycles was investigated with tilapia cultured in recirculating aquaculture systems (RAS) and traditional aquaculture in ponds (TAP). This study found that fatty acids (eg., palmitic acid) were enriched in TAP, while antioxidants (eg., glutathione) were enriched in RAS. Generally, proteins in the RAS group exhibited greater stability against denaturation during the F-T cycle, suggested by a less decrease in haem protein content (77% in RAS and 86% in TAP) and a less increase in surface hydrophobicity of sarcoplasmic protein (63% in RAS and 101% in TAP). There was no significant difference in oxidative stability of myofibrillar protein between the two groups. This study provides a theoretical guide for the quality control of tilapia cultured in RAS during frozen storage.


Assuntos
Aquicultura , Proteínas de Peixes , Congelamento , Estabilidade Proteica , Tilápia , Animais , Tilápia/metabolismo , Proteínas de Peixes/química , Proteínas de Peixes/metabolismo , Proteínas Musculares/metabolismo , Proteínas Musculares/química , Metabolômica , Lagoas/química , Músculos/química , Músculos/metabolismo , Ácidos Graxos/metabolismo , Ácidos Graxos/química , Ácidos Graxos/análise
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