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1.
Food Chem X ; 22: 101335, 2024 Jun 30.
Article in English | MEDLINE | ID: mdl-38595755

ABSTRACT

The purpose of this study was to investigate the volatile flavor changes in silver carp mince (SCM) gel glycated with different reducing sugars (glucose, L-arabinose, and xylose) based on E-nose, GC-IMS, and sensory evaluation. These results showed that glycation reduced the fishy smell of SCM gel and increased the meaty, toasty, and burnt smell. A total of 10 volatile compounds were considered as characteristic flavor compounds and potential markers. Among them, the main contributors of fishy included hexanal, heptanal, n-nonanal, octanal, etc. Toasty and burnt were mainly related to the production of 3-methylbutanal and furfurol. These results heralded that glycation could be used to improve the volatile flavor of SCM. This research provided a theoretical basis and technical support for glycation in aquatic food flavor quality control, aquatic pre-made food development, and aquatic leisure food processing.

2.
J Sci Food Agric ; 104(7): 4128-4135, 2024 May.
Article in English | MEDLINE | ID: mdl-38308538

ABSTRACT

BACKGROUND: Glycation is a green processing technology. Based on our previous studies, glycation with l-arabinose and xylose was beneficial to enhance the texture properties of silver carp mince (SCM) gels. However, the possible enhancement mechanism remained unclear. Therefore, in this study, SCM gels with different types of reducing sugar (glucose, l-arabinose, and xylose) were prepared based on our previous study. The possible mechanism of texture enhancement of SCM gels was analyzed by investigating the changes in water distribution, protein structures, and microstructure in the gel system. RESULTS: The glycation of l-arabinose and xylose enhanced the hardness, cohesiveness, chewiness, and resilience of SCM gels. Hardness increased from 1883.04 (control group) to 3624.54 (l-arabinose group) and 4348.18 (xylose group). Low-field nuclear magnetic resonance (LF-NMR) showed that glycation promoted the tight binding of immobilized water to proteins. Raman spectroscopic analysis showed that glycation increased the surface hydrophobicity and promoted the formation of disulfide bonds. Scanning electron microscopy (SEM) showed that glycation promoted the formation of uniform and dense three-dimensional network structure in SCM gels. CONCLUSION: In summary, glycation enhanced the binding ability of immobilized water to proteins, improved the surface hydrophobicity, promoted the formation of disulfide bonds, and led to a more uniform and dense gel network structure of proteins, thus enhancing the texture properties of SCM gels. This research provided a theoretical basis for a better understanding of the mechanism of the effect of glycation on the quality of gel products and also provided technical support for the application of l-arabinose and xylose in new functional gel foods. © 2024 Society of Chemical Industry.


Subject(s)
Carps , Maillard Reaction , Animals , Xylose/chemistry , Arabinose/chemistry , Carps/metabolism , Gels/chemistry , Proteins , Water , Disulfides
3.
Molecules ; 28(18)2023 Sep 20.
Article in English | MEDLINE | ID: mdl-37764497

ABSTRACT

The aim of this study was to investigate the biochemical properties and gel-forming capacity of duck myofibrillar proteins under the effects of 2,2'-azobis(2-methylpropionamidine) dihydrochloride (AAPH)-mediated oxidation. Duck myofibrillar proteins were extracted and treated with different concentrations of AAPH solutions (0, 1, 3, 5, 10 mmol/L) and then analysed for carbonyl content, dynamic rheology, protein profiles and gel-forming properties (colour, water holding capacity, gel strength and microstructure). The results showed that with increasing AAPH concentration, the carbonyl content of the proteins exhibited an increasing trend (p < 0.05); SDS-PAGE pattern changes indicated that moderate oxidation (3 mmol/L AAPH) induced myosin aggregation via covalent bonds including disulfide, enhanced protein-protein interactions, and thus affected the gel strength of the DMPs' heat-induced gels. However, high oxidation (5 and 10 mmol/L AAPH) led to the partial degradation of the myosin heavy chain (MHC) isoforms, as evidenced by lower storage modulus and irregular microstructures, which significantly reduced gelation ability. These results suggest that the internal relationship between alkylperoxyl radical-induced oxidation should be taken into account in the processing of duck meat, as mild protein oxidation is conducive to improving gel quality.

4.
Foods ; 12(7)2023 Apr 04.
Article in English | MEDLINE | ID: mdl-37048351

ABSTRACT

A recently identified broiler myopathy known as wooden breast (WB) is predominantly found in the pectoralis major muscle of fast-growing broiler hybrids and is causing significant losses to the poultry industry. The aim of this study was to investigate the effects of WB syndrome on raw meat texture, purge loss and thermal properties of intramuscular connective tissue of pectoralis major muscle in the early postmortem period (1-3 days). Results showed that the presence of the WB muscles condition at 1 day postmortem was associated with significantly increased stiffness (27.0 N vs. 23.1 N) and significantly increased purge loss (1.8% vs. 1.0%) compared to normal breast (NB). However, on 3 days postmortem, these parameters did not differ between WB and NB groups. Insoluble and total collagen content was significantly higher in WB muscles compared to NB muscles, and the extractability of intramuscular connective tissue (IMCT) of WB was also higher (0.42% vs. 0.37%) compared to NB and remained stable in the early postmortem period. There was significantly lower protein content in the sarcoplasmic protein fraction and myofibrillar protein fraction of WB muscles compared to NB muscles (p < 0.05). The IMCT of these two groups showed different thermal properties, as the enthalpy of denaturation (ΔH) was significantly lower in WB muscles compared to NB muscles. The WB syndrome had a great effect on the texture and connective tissue properties of the meat compared to normal muscle, with a tendency for having a lower purge loss and higher raw meat hardness.

5.
Front Nutr ; 9: 1029116, 2022.
Article in English | MEDLINE | ID: mdl-36466406

ABSTRACT

This paper focuses on the changes of physicochemical properties and gel-forming ability of duck myofibrillar proteins (DMPs) induced using hydroxyl radical oxidizing systems. DMPs were firstly extracted and then oxidized at various H2O2 concentrations (0, 4, 8, and 12 mmol/L) using Fenton reagent (Fe3+-Vc-H2O2) to generate hydroxyl radicals, and the effects of hydroxyl radical oxidation on the physicochemical changes and heat-induced gel-forming capacity of DMPs were analyzed. We observed obvious increases in the carbonyl content (p < 0.05) and surface hydrophobicity of DMPs with increasing of H2O2 concentrations (0-12 mmol/L). In contrast, the free thiol content (p < 0.05) and water retention ability of DMPs decreased with increasing H2O2 concentrations (0-12 mmol/L). These physicochemical changes suggested that high concentrations of hydroxyl radicals significantly altered the biochemical structure of DMPs, which was not conducive to the formation of a gel mesh structure. Furthermore, the gel properties were reduced based on the significant decrease in the water holding capacity (p < 0.05) and increased transformation of immobilized water of the heat-induced gel to free water (p < 0.05). With the increase of H2O2 concentrations, secondary structure of proteins analysis results indicated α-helix content decreased significantly (p < 0.05), however, random coil content increased (p < 0.05). And more cross-linked myosin heavy chains were detected at higher H2O2 concentrations groups through immunoblot analysis (p < 0.05). Therefore, as H2O2 concentrations increased, the gel mesh structure became loose and porous, and the storage modulus and loss modulus values also decreased during heating. These results demonstrated that excessive oxidation led to explicit cross-linking of DMPs, which negatively affected the gel-forming ability of DMPs. Hence, when processing duck meat products, the oxidation level of meat gel products should be controlled, or suitable antioxidants should be added.

6.
Gels ; 8(10)2022 Oct 06.
Article in English | MEDLINE | ID: mdl-36286134

ABSTRACT

This paper focuses on the effect of malondialdehyde-induced oxidative modification (MiOM) on the gel properties of duck myofibrillar proteins (DMPs). DMPs were first prepared and treated with oxidative modification at different concentrations of malondialdehyde (0, 0.5, 2.5, 5.0, and 10.0 mmol/L). The physicochemical changes (carbonyl content and free thiol content) and gel properties (gel whiteness, gel strength, water holding capacity, rheological properties, and microstructural properties) were then investigated. The results showed that the content of protein carbonyl content increased with increasing MDA oxidation (p < 0.05), while the free thiol content decreased significantly (p < 0.05). Meanwhile, there was a significant decrease in gel whiteness; the gel strength and water-holding capacity of protein gels increased significantly under a low oxidation concentration of MDA (0−5 mmol/L); however, the gel strength decreased under a high oxidation concentration (10 mmol/L) compared with other groups (0.5−5 mmol/L). The storage modulus and loss modulus of oxidized DMPs also increased with increasing concentrations at a low concentration of MDA (0−5 mmol/L); moreover, microstructural analysis confirmed that the gels oxidized at low concentrations (0.5−5 mmol/L) were more compact and homogeneous in terms of pore size compared to the high concentration or blank group. In conclusion, moderate oxidation of malondialdehyde was beneficial to improve the gel properties of duck; however, excessive oxidation was detrimental to the formation of dense structured gels.

7.
Foods ; 11(11)2022 May 30.
Article in English | MEDLINE | ID: mdl-35681371

ABSTRACT

This study aimed to investigate the effect of pea protein isolate (PPI) on the functional, instrumental and textural quality parameters of duck meat batters (DMB). Ground duck breast meat was mixed with different concentrations of PPI (0%, 3%, 6% or 9%, w/w) to prepare DMB. The color, cooking yield, water-holding capacity, water distribution and migration, rheological properties and texture profile of the DMB were evaluated. The results showed that the L* value of the gel decreased and the b* value increased with the increasing pea protein addition. The cooking yield and water-holding capacity showed a gradual increase, but the difference was not significant (p > 0.05). Compared with the control, the storage modulus (G') and loss modulus (G″) were higher at the beginning and at the end and increased with the addition of pea protein, which was in accordance with the Fourier series relationship. The hardness, chewiness and gumminess of the gels gradually increased; on the contrary, the springiness and cohesiveness first increased and then decreased, respectively, reaching a maximum value of 0.96 and 0.81 when the addition amount reached 6%. Adding pea protein to the gels not only increased the area of immobilized water but also decreased the area of free water, thus improving the water-holding capacity of the batters. Therefore, pea protein can promote the formation of a stable and elastic network structure of duck meat batters.

8.
Foods ; 11(7)2022 Apr 03.
Article in English | MEDLINE | ID: mdl-35407127

ABSTRACT

This paper investigates the relationship between the molecular structure and thermally induced gel properties of duck myofibrillar protein isolate (DMPI) as influenced by the addition of pea protein isolate (PPI). The results showed that b* value of the gels increased; however, a* value decreased with the increase of PPI content (p < 0.05). The whiteness of the gels decreased significantly with the addition of pea protein compared with 0% vs. 0.5% addition. Nuclear magnetic resonance tests showed the area of immobilized water also increased with increasing PPI addition (0−2%), thus consistent with the increased water-holding capacity (p < 0.05). The penetration force of the gels increased with increasing PPI addition (p < 0.05), while the storage modulus and loss modulus of the gels were also found to increase, accompanied by the transformation of the α-helix structure into ß-sheet, resulting in better dynamics of gel formation. These results indicated the gel-forming ability of DMPI, including water retention and textural properties, improves with increasing PPI addition. Principal component analysis verified these interrelationships. Thus, pea protein could improve the properties of duck myofibrillar protein gels to some extent and improve their microstructure, potentially facilitating the transition from a weak to a non-aggregated, rigid structure.

9.
Fish Shellfish Immunol ; 72: 443-451, 2018 Jan.
Article in English | MEDLINE | ID: mdl-29146449

ABSTRACT

Despite the economic and evolutionary importance of aquatic host-infecting microsporidian species, at present, limited information has been provided about the microsporidia-host interactions. This study focused on Hepatospora eriocheir, an emerging microsporidian pathogen for the Chinese mitten crab Eriocheir sinensis. Hypertrophy of hepatopancreas cells was a common feature of H. eriocheir infection. More importantly, mitochondria of the hepatopancreas were drawn around the H. eriocheir, most likely to aid the uptake of ATP directly from the host. To better understand the crab anti-microsporidian response, de novo transcriptome sequencing of the hepatopancreas tissue was furtherly proceeded. A total of 47.84 M and 57.21 M clean reads were generated from the hepatopancreas of H. eriocheir infected and control groups respectively. Based on homology searches, functional annotation with 6 databases (Nr, Swiss-Prot, KEGG, KOGs, Pfam and GO) for 88,168 unigenes was performed. 2619 genes were identified as differently up-regulated and 2541 genes as differently down-regulated. Prominent functional categories enriched with differentially expressed genes (DEGs) were "ATP binding", "mitochondrion and extracellular region", "oxygen transporter activity", "oxidoreductase activity", "alanine, aspartate and glutamate metabolism", "carbohydrate metabolic process", "starch and sucrose metabolism" and "fatty acid biosynthesis". These results confirmed a parasite external energy supply and an integrated metabolic stress. In addition, simple sequence repeats (SSRs) and single nucleotide polymorphisms (SNPs) were also identified from the gene library. Taken together, these findings allow us to better understand the underlying mechanisms regulating interactions between H. eriocheir and the crab E. sinensis.


Subject(s)
Apansporoblastina/physiology , Arthropod Proteins/genetics , Brachyura/immunology , Gene Expression Regulation , Hepatopancreas/immunology , Transcriptome , Animals , Arthropod Proteins/immunology , Brachyura/genetics , Brachyura/microbiology , Female , Hepatopancreas/microbiology , Male
10.
J Antibiot (Tokyo) ; 70(6): 743-746, 2017 Jun.
Article in English | MEDLINE | ID: mdl-28196973

ABSTRACT

Leptosphaerins H and I (1 and 2), two new xanthone derivatives, and six known compounds, leptosphaerin F (3), monodictysin B (4), norlichexanthone (5), leptosphaerin D (6), moniliphenone (7) and emodinbianthrone (8) have been isolated from a scale-up fermentation of the ascomycete fungus Leptosphaeria sp. Their structures were primarily elucidated by interpretation of NMR spectroscopic data. The absolute configuration of 1 was assigned using the modified Mosher method, whereas that of C-8a in 2 was determined via the CD data. Compound 6 showed modest cytotoxicity against a panel of three human tumor cell lines.


Subject(s)
Antineoplastic Agents/isolation & purification , Ascomycota/metabolism , Neoplasms/drug therapy , Polyketides/isolation & purification , Xanthones/isolation & purification , Antineoplastic Agents/chemistry , Antineoplastic Agents/pharmacology , Cell Line, Tumor , Humans , Magnetic Resonance Spectroscopy , Neoplasms/pathology , Polyketides/chemistry , Polyketides/pharmacology , Xanthones/chemistry , Xanthones/pharmacology
11.
Mitochondrial DNA A DNA Mapp Seq Anal ; 27(6): 4691-4692, 2016 11.
Article in English | MEDLINE | ID: mdl-26678029

ABSTRACT

Chinese skink (Eumeces chinensis) is a ground-dwelling oviparous sincid lizard, which is widely distributed in the southern Provinces of China, including Taiwan and Hainan. Here, the complete mitochondrial genome of E. chinensis (17 175 bp in length) has been analyzed for building the database. It contains 37 genes (13 protein-coding genes, 2 rRNA genes and 22 tRNA genes) and a non-coding region (D-loop). Overall base composition of the complete mitochondrial DNA is A (32.1%), G (14.3%), C (28.8%), and T (24.8%), so the percentage of A and T (56.9%) is slightly higher than G and C (43.1%). All the genes in E. chinensis were distributed on the H-strand, except for the ND6 subunit gene and nine tRNA genes which were encoded on the L-strand. Our phylogeny study shows that E. chinensis and P. egregius are the sister group which belongs to the genus, Plestiodon. In addition, we also prove that Lacertidae is sister to the families, Gekkonidae and Scincidae.


Subject(s)
Genes, Mitochondrial , Genome, Mitochondrial , Lizards/classification , Lizards/genetics , Phylogeny , Animals , Base Composition , Evolution, Molecular , Sequence Analysis, DNA
12.
Meat Sci ; 89(2): 181-8, 2011 Oct.
Article in English | MEDLINE | ID: mdl-21663805

ABSTRACT

This study investigated the effect of early post-mortem temperature on broiler protein characteristics and meat quality. Muscles were kept at different temperatures (0, 20 and 40 °C) until 4h post-mortem and then stored at 4 °C. Rapid degradation of ATP and glycogen, thus inducing a high rate of lactate formation and pH drop, were found in the 40 °C group during incubation. When extracting proteins, a lower protein content of the sarcoplasmic fraction and a higher protein content of the myofibrillar fraction were found in the 40 °C group at 24h post-mortem; SDS-PAGE and western-blotting results revealed that phosphorylase was associated with the myofibrillar fraction. Furthermore, the 40 °C group had paler surfaces, higher drip loss and lower processing properties. These data suggest that elevated temperature during early post-mortem period, resulting in rapid glycolysis, induced phosphorylase denaturation and association with myofibrillar proteins thus generating pale and exudative characteristics.


Subject(s)
Glycogen Phosphorylase, Muscle Form/analysis , Glycolysis , Meat/analysis , Pectoralis Muscles/physiology , Protein Denaturation , Actin Cytoskeleton/chemistry , Actin Cytoskeleton/metabolism , Adenosine Triphosphate/analysis , Animals , Body Temperature , Chickens , Electrophoresis, Polyacrylamide Gel/methods , Food Handling/methods , Glycogen/analysis , Glycogen Phosphorylase, Muscle Form/metabolism , Hot Temperature , Hydrogen-Ion Concentration , Muscle Proteins/chemistry , Muscle Proteins/metabolism , Pectoralis Muscles/chemistry
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