RESUMEN
In this study, similarities and differences of sodium tripolyphosphate (STPP) and sodium trimetaphosphate (STMP) pre-soaking on the stability of muscle proteins in shrimp were investigated during 12 weeks of frozen storage (-30 °C). The physicochemical analysis indicated significant improvements in the WHC, springiness, chewiness, and thermal stability of STPP and STMP pre-soaked samples when compared to the control. Interestingly, STMP pre-soaking showed better cryoprotective effects than the STPP treatment when the storage period reached the end of the 12 weeks. Furthermore, the label-free based proteomics results indicated that 62 upregulated differentially abundant proteins (DAPs) were detected in STMP when compared to STPP. These identified DAPs specifically included 40S ribosomal proteins, actin-related proteins, heat shock proteins, myosin heavy chain, and tubulin beta chain. Additionally, the gene ontology (GO) and eukaryotic clusters of orthologous group (KOG) analyses verified that the incorporation of STMP molecules enhanced the resistance of cytoskeleton proteins to cold-temperature stress.
Asunto(s)
Almacenamiento de Alimentos/métodos , Penaeidae/metabolismo , Polifosfatos/química , Alimentos Marinos/análisis , Animales , Cromatografía Líquida de Alta Presión , Congelación , Proteínas de Choque Térmico/metabolismo , Penaeidae/química , Péptidos/análisis , Proteínas de Mariscos/metabolismo , Espectrometría de Masas en Tándem , Factores de TiempoRESUMEN
The main aim of the present work was to investigate the effect of the inherent differences in the raw muscle on the textural quality of the cooked meat from different sized Eriocheir sinensis. The content of entrapped water was 73.8-77.7 g/100 g in raw muscle. The density and diameter of muscle thick microfilaments ranged between 137 and 158/µm2 and 20.9-27.0 nm. These results demonstrated that the raw muscle from the tender group had a smaller density of larger diameter thick microfilaments and more entrapped water than other samples, which could explain the high tenderness of the cooked meat (P < 0.05). The potential structural proteins that indicated tenderness include myosin regulatory light chain 2, ancient ubiquitous protein 1, tubulin α-2 chain, and ß-catenin, was determined using liquid chromatography-tandem mass spectrometry. The inherent attributes of raw muscle could explain the textural differences of the cooked meat from Eriocheir sinensis.
Asunto(s)
Braquiuros/metabolismo , Músculos/patología , Alimentos Marinos/análisis , Proteínas de Mariscos/análisis , Animales , Cromatografía Líquida de Alta Presión , Culinaria , Espectrometría de Masas , Microscopía Electrónica de Transmisión , Músculos/metabolismo , Proteínas de Mariscos/metabolismoRESUMEN
The diverse modes of sexual reproduction in Bivalvia make it an excellent clade to understand the evolution of sex and sex determination. The cosmopolitan Pacific oyster Crassostrea gigas is an ideal model for bivalve sex determination studies because of its complicated sexuality, including dioecy, sex change and rare hermaphroditism. A major barrier to C. gigas sex determination study has been the lack of information on the type of sex determination. To identify its sex-determining system, sex observation by following the same individual in two consecutive years was conducted on 760 oysters from distinct populations. Stable sexuality and sex reversal in both directions were observed, which provides a case against the protandry of C. gigas. Restriction site-associated DNA sequencing (RAD-seq) based on 26 samples with unchanged and converted sexualities was carried out for identifying sex-linked marker. One SNP Cgsl-40 was proved to be sex-related, but sex-biased heterozygosity varied between populations for RAD-seq and validation, showing no evidence for sex chromosomes or single-locus models for C. gigas primary sex determination. Information obtained in our study provides novel insight into sex determination mechanism in C. gigas.
Asunto(s)
Crassostrea/genética , Procesos de Determinación del Sexo/genética , Animales , Femenino , Masculino , Modelos Biológicos , Polimorfismo de Nucleótido Simple , ARN/química , ARN/metabolismo , RNA-Seq , Proteínas de Mariscos/metabolismoRESUMEN
Aquatic protein hydrolysates are usually associated with unpleasant odors and high fat content, which seriously restricts their industrial utilization. In this study, chitosans with different molecular weights produced by hydrogen peroxide degradation were applied to establish a flocculation method, using for the deodorization and defatting of oyster (Crassostrea gigas) hydrolysates. GC-MS analysis showed that the method markedly decreased the content of the fishy odor constituents. Up to 92 % fat and part of the heavy metals were effectively removed. Protein recovery percentage and solid recovery percentage were 83.43 ± 0.35 % and 76.36 ± 0.52 %, respectively, at the optimum dose (150 mg/L) of chitosan (83 % of deacetylation degree, 77 kDa). Thus, chitosan flocculation-coupled centrifugation (5000g, 1 min) can effectively solve the current drawbacks of engineering disc centrifuges and can be industrially used for defatting and deodorization during aquatic food processing.
Asunto(s)
Quitosano/metabolismo , Crassostrea/química , Proteínas de Mariscos/metabolismo , Animales , Quitosano/química , Crassostrea/metabolismo , Floculación , Peróxido de Hidrógeno/química , Peróxido de Hidrógeno/metabolismo , Peso Molecular , Tamaño de la Partícula , Hidrolisados de Proteína , Proteínas de Mariscos/química , Propiedades de SuperficieRESUMEN
Tropomyosin (TM) is the main allergen of shrimp. Glycation reportedly reduced the allergenicity of TM, and the allergenicity reduction was heavily dependent upon the sources of saccharides. In this work we investigated, how glycation of tropomyosin by functional oligosaccharides affected the allergenicity. Compared to TM, the TM glycated by galacto-oligosaccharide (TM-GOS), mannan-oligosaccharide (TM-MOS) and maltopentaose (TM-MPS) had lower allergenicity and induced weaker mouse allergy responses. While the TM glycated by fructo-oligosaccharide (TM-FOS) had stronger allergenicity and induced severe mouse allergy symptoms, due to the generation of neoallergns that belonged to advanced glycation end products (e.g. CML). Therefore, GOS, MOS and MPS could be applied to desensitize shrimp TM-induced food allergy through glycation, while FOS was not suitable to reduce TM allergenicity. Glycation of TM by GOS, MOS and MPS, especially for MPS, significantly reduced allergenicity and alleviated allergy symptoms, which could be potentially explored for immunotherapy for shrimp-allergic patients.
Asunto(s)
Hipersensibilidad a los Alimentos/inmunología , Productos Finales de Glicación Avanzada/metabolismo , Palaemonidae/inmunología , Proteínas de Mariscos/metabolismo , Tropomiosina/metabolismo , Adulto , Alérgenos/inmunología , Alérgenos/metabolismo , Animales , Preescolar , Femenino , Hipersensibilidad a los Alimentos/sangre , Glicosilación , Humanos , Masculino , Ratones Endogámicos BALB C , Persona de Mediana Edad , Oligosacáridos/inmunología , Oligosacáridos/metabolismo , Proteínas de Mariscos/química , Proteínas de Mariscos/inmunología , Tropomiosina/química , Tropomiosina/inmunologíaRESUMEN
Scylla paramamosain is an important aquaculture crab, which has great economical and nutritional value. To the best of our knowledge, few full-length crab transcriptomes are available. In this study, a library composed of 12 different tissues including gill, hepatopancreas, muscle, cerebral ganglion, eyestalk, thoracic ganglia, intestine, heart, testis, ovary, sperm reservoir, and hemocyte was constructed and sequenced using Pacific Biosciences single-molecule real-time (SMRT) long-read sequencing technology. A total of 284803 full-length non-chimeric reads were obtained, from which 79005 high-quality unique transcripts were obtained after error correction and sequence clustering and redundant. Additionally, a total of 52544 transcripts were annotated against protein database (NCBI nonredundant, Swiss-Prot, KOG, and KEGG database). A total of 23644 long non-coding RNAs (lncRNAs) and 131561 simple sequence repeats (SSRs) were identified. Meanwhile, the isoforms of many genes were also identified in this study. Our study provides a rich set of full-length cDNA sequences for S. paramamosain, which will greatly facilitate S. paramamosain research.
Asunto(s)
Braquiuros/genética , Sistemas de Lectura Abierta/genética , Animales , Bases de Datos Genéticas , Femenino , Biblioteca de Genes , Masculino , Repeticiones de Microsatélite/genética , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Empalme del ARN , ARN Largo no Codificante/genética , ARN Largo no Codificante/metabolismo , Proteínas de Mariscos/metabolismo , TranscriptomaRESUMEN
The effect of a hydroxyl radical generating system (HRGS), which contained FeCl3, sodium ascorbate, and different concentrations of H2O2, on the physiochemical properties of myofibrillar protein (MP) from squid mantles, has been investigated. The effect of different exposure times to HRGS was also considered. Compared to non-oxidized MP, a significant (pâ¯<â¯0.05) increase in carbonyl content (more than 50% of its original content) and protein solubility, as well as in surface hydrophobicity, was observed in the oxidative MP. With different treatment times, a sharp decrease (pâ¯<â¯0.05) in sulfhydryl content was detected. In addition, hydroxyl radical treatment significantly reduced the MP gel's texture properties, whiteness and water holding capacity, especially at higher concentrations of H2O2. This observation could be attributed to extensive disorderly and less compact structure of MP gels. The results demonstrate the negative effect of HRGS on the structural and functional properties of MP from squid mantles.
Asunto(s)
Decapodiformes/metabolismo , Proteínas de Mariscos/química , Animales , Ácido Ascórbico/química , Geles/química , Interacciones Hidrofóbicas e Hidrofílicas , Radical Hidroxilo/química , Oxidación-Reducción , Reología , Proteínas de Mariscos/metabolismo , Solubilidad , Compuestos de Sulfhidrilo/análisis , Agua/químicaRESUMEN
Molluscan shells, mainly composed of calcium carbonate, also contain organic components such as proteins and polysaccharides. Shell organic matrices construct frameworks of shell structures and regulate crystallization processes during shell formation. To date, a number of shell matrix proteins (SMPs) have been identified, and their functions in shell formation have been studied. However, previous studies focused only on SMPs extracted from adult shells, secreted after metamorphosis. Using proteomic analyses combined with genomic and transcriptomic analyses, we have identified 31 SMPs from larval shells of the pearl oyster, Pinctada fucata, and 111 from the Pacific oyster, Crassostrea gigas. Larval SMPs are almost entirely different from those of adults in both species. RNA-seq data also confirm that gene expression profiles for larval and adult shell formation are nearly completely different. Therefore, bivalves have two repertoires of SMP genes to construct larval and adult shells. Despite considerable differences in larval and adult SMPs, some functional domains are shared by both SMP repertoires. Conserved domains include von Willebrand factor type A (VWA), chitin-binding (CB), carbonic anhydrase (CA), and acidic domains. These conserved domains are thought to play crucial roles in shell formation. Furthermore, a comprehensive survey of animal genomes revealed that the CA and VWA-CB domain-containing protein families expanded in molluscs after their separation from other Lophotrochozoan linages such as the Brachiopoda. After gene expansion, some family members were co-opted for molluscan SMPs that may have triggered to develop mineralized shells from ancestral, nonmineralized chitinous exoskeletons.