scholarly journals Preliminary investigation on the use of allyl isothiocyanate to increase the shelf-life of gilthead sea bream (Sparus aurata) fillets

2015 ◽  
Vol 4 (3) ◽  
Author(s):  
Filippo Giarratana ◽  
Chiara Crinò ◽  
Daniele Muscolino ◽  
Chiara Beninati ◽  
Graziella Ziino ◽  
...  
Keyword(s):  
Shelf Life ◽  
Sparus Aurata ◽  
Preliminary Investigation ◽  
Allyl Isothiocyanate ◽  
Gilthead Sea Bream ◽  
Sea Bream ◽  
In Vitro Tests ◽  
Spoilage Bacteria ◽  
Fish Product

The aim of this work is to evaluate the activity of allyl isothiocyanate (AITC) against fish spoilage bacteria (specific spoilage organisms; SSOs) as well as its possible use in gilthead sea bream (<em>Sparus aurata</em>) fillets to extend their shelf-life. In this regard, in vitro tests are carried out in order to evaluate the inhibitory activity of AITC and its vapours on several strains of SSOs. The AITC effect on the shelflife of sea bream fillets was made by putting them in plastic trays hermetically closed with the addition AITC. Microbiological and sensorial evaluations were made on fish fillets during storage. Treated fillets maintained microbial populations at a significantly lower level compared with the control samples during storage, showing better sensorial characteristics. Therefore, the use of AITC’s vapours seems to be a new and interesting alternative way to increase fish product shelf-life.

scholarly journals Effects of allyl isothiocyanate on the shelf-life of gilthead sea bream (Sparus aurata) fillets

2016 ◽  
Vol 34 (No. 2) ◽  
pp. 160-165 ◽  
Author(s):  
D. Muscolino ◽  
F. Giarratana ◽  
C. Beninati ◽  
G. Ziino ◽  
A. Giuffrida ◽  
...  
Keyword(s):  
Shelf Life ◽  
Sparus Aurata ◽  
Allyl Isothiocyanate ◽  
Gilthead Sea Bream ◽  
Sea Bream

Growth hormone as an in vitro phagocyte-activating factor in the gilthead sea bream ( Sparus aurata )

1997 ◽  
Vol 287 (3) ◽  
pp. 535-540 ◽  
Author(s):  
Josep Alvar Calduch-Giner ◽  
Ariadna Sitjà-Bobadilla ◽  
Pilar Alvarez-Pellitero ◽  
Jaume Pérez-Sánchez
Keyword(s):  
Growth Hormone ◽  
Sparus Aurata ◽  
Gilthead Sea Bream ◽  
Sea Bream

Evidence for a direct action of GH on haemopoietic cells of a marine fish, the gilthead sea bream (Sparus aurata)

1995 ◽  
Vol 146 (3) ◽  
pp. 459-467 ◽  
Author(s):  
J A Calduch-Giner ◽  
A Sitjà-Bobadilla ◽  
P Álvarez-Pellitero ◽  
J Pérez-Sánchez
Keyword(s):  
Binding Sites ◽  
Sparus Aurata ◽  
Binding Capacity ◽  
Specific Binding ◽  
Head Kidney ◽  
Gilthead Sea Bream ◽  
Sea Bream ◽  
Single Class ◽  
Lower Vertebrate

Abstract Receptors for GH were characterized in the head kidney of gilthead sea bream (Sparus aurata), using radioiodinated and biotinylated ligands. The specific binding of radiolabelled recombinant gilthead sea bream GH (rsbGH) to head kidney membrane preparations was dependent on membrane concentration. Salmon prolactin, salmon gonadotrophin and carp gonadotrophin did not compete for 125I-labelled rsbGH-binding sites. Unlabelled rsbGH competitively displaced 125I-labelled rsbGH bound to head kidney membranes. Scatchard plots were always linear, denoting the presence of a single class of binding sites. The binding affinity (Ka=2·7 × 109 m−1) was equivalent to that found in liver membrane preparations, but the binding capacity (2·5 ±0·30 fmol/mg protein) was 50- to 75-fold lower. To identify the cells which express the GH receptor, head kidney smears were incubated with biotinylated rsbGH, followed by incubation with an avidin–biotin complex conjugated to alkaline phosphatase. The reaction with the new-fuchsin substrate gave a red precipitate, showing a specific and intense labelling in erythroblasts, polychromatophilic erythroblasts and myeloblasts. Noticeable binding was observed in myelocytes and immature granulocytes, tending to disappear at the latter stages of granulocyte maturation. Light but appreciable binding was also observed in monocytes, lymphocytes and acidophilic erythroblasts, whereas it was completely absent in proerythrocytes and erythrocytes. The proliferative action of rsbGH and recombinant human IGF-I on in vitro cultures of head kidney cells was demonstrated by a 5-bromo-2′-deoxy-uridine immunoassay. To our knowledge, this is the first report that provides suitable evidence for a role of GH as a haemopoietic growth and differentiation factor in lower vertebrate species. Journal of Endocrinology (1995) 146, 459–467

scholarly journals Isolation of Growth Hormone and in Vitro Translation of mRNA Isolated from Pituitaries of the Gilthead Sea Bream Sparus aurata

1994 ◽  
Vol 95 (3) ◽  
pp. 321-329 ◽  
Author(s):  
B. Cavari ◽  
P.-Y. Le Bail ◽  
B. Levavi-Sivan ◽  
P. Melamed ◽  
H. Kawauchi ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Sparus Aurata ◽  
In Vitro Translation ◽  
Gilthead Sea Bream ◽  
Sea Bream

In vivo and in vitro treatments against Sparicotyle chrysophrii (Monogenea: Microcotylidae) parasitizing the gills of gilthead sea bream (Sparus aurata L.)

Aquaculture ◽  
2006 ◽  
Vol 261 (3) ◽  
pp. 856-864 ◽  
Author(s):  
Ariadna Sitjà-Bobadilla ◽  
Magnolia Conde de Felipe ◽  
Pilar Alvarez-Pellitero
Keyword(s):  
Sparus Aurata ◽  
Gilthead Sea Bream ◽  
Sea Bream

scholarly journals Evaluation of the in Vitro Anti-Atherogenic Properties of Lipid Fractions of Olive Pomace, Olive Pomace Enriched Fish Feed and Gilthead Sea Bream (Sparus aurata) Fed with Olive Pomace Enriched Fish Feed

Marine Drugs ◽  
2013 ◽  
Vol 11 (10) ◽  
pp. 3676-3688 ◽  
Author(s):  
Constantina Nasopoulou ◽  
Vassiliki Gogaki ◽  
Giorgos Stamatakis ◽  
Leonidas Papaharisis ◽  
Constantinos Demopoulos ◽  
...  
Keyword(s):  
Sparus Aurata ◽  
Gilthead Sea Bream ◽  
Sea Bream ◽  
Fish Feed ◽  
Olive Pomace ◽  
Lipid Fractions

Study of the microbiological quality, prevalence of foodborne pathogens and product shelf-life of Gilthead sea bream (Sparus aurata) and Sea bass (Dicentrarchus labrax) from aquaculture in estuarine ecosystems of Andalusia (Spain)

2020 ◽  
Vol 90 ◽  
pp. 103498 ◽  
Author(s):  
Jean Carlos Correia Peres Costa ◽  
Belén Floriano ◽  
Isabel María Bascón Villegas ◽  
Juan Pablo Rodríguez-Ruiz ◽  
Guiomar Denisse Posada-Izquierdo ◽  
...  
Keyword(s):  
Shelf Life ◽  
Foodborne Pathogens ◽  
Sparus Aurata ◽  
Microbiological Quality ◽  
Dicentrarchus Labrax ◽  
Sea Bass ◽  
Gilthead Sea Bream ◽  
Sea Bream ◽  
Estuarine Ecosystems

scholarly journals Structural and functional characterizations of activin type 2B receptor (acvr2b) ortholog from the marine fish, gilthead sea bream, Sparus aurata: evidence for gene duplication of acvr2b in fish

2012 ◽  
Vol 49 (3) ◽  
pp. 175-192 ◽  
Author(s):  
Bruria Funkenstein ◽  
Ekaterina Krol ◽  
Elena Esterin ◽  
Yong-soo Kim
Keyword(s):  
Transforming Growth Factor ◽  
Sparus Aurata ◽  
Fish Larvae ◽  
Larval Growth ◽  
Amino Acid Sequences ◽  
Negative Regulator ◽  
Gilthead Sea Bream ◽  
Sea Bream ◽  
Luciferase Assay

Myostatin (MSTN), a negative regulator of muscle growth and a member of the transforming growth factor-β superfamily, can bind the two activin type 2 receptors (ACVR2). It has been previously shown that WT mice injected with ACVR2B extracellular domain (ACVR2B-ECD) had higher muscle mass. Likewise, fish larvae immersed inPichia pastorisculture supernatant, containing goldfish Acvr2b-ECD, showed enhanced larval growth. However, it is not clear whether fish Mstn1 and Mstn2 signal through the same receptor and whether fish express more than oneacvr2bgene. In the current study, three cDNAs encodingacvr2b(saacvr2b-1, saacvr2b-2a, and saacvr2b-2b) were cloned from gilthead sea bream. All three contain the short extracellular binding domain, a short transmembrane region, and a conserved catalytic domain of serine/threonine protein kinase. Bioinformatics analysis provided evidence for the existence of twoacvr2bgenes (acvr2b-1 andacvr2b-2) in several other fish species as well, probably as a result of gene or genome duplication. The two isoforms differ in their amino acid sequences. The direct inhibitory effect of Acvr2b-ECD on Mstn activity was testedin vitro. The saAcvr2b-1-ECD was expressed in the yeastP. pastoris. Evidence is provided for N-glycosylation of Acvr2b-1-ECD. The affinity-purified Acvr2b-1-ECD inhibited recombinant mouse/rat/human mature MSTN activity when determinedin vitrousing the CAGA-luciferase assay in A204 cells. A lower inhibitory activity was obtained when unprocessed purified, furin-digested, and activated saMstn1 was used. Results of this study demonstrate for the first time the existence of twoacvr2bgenes in fish. In addition, the study shows that bioactive fish Acvr2b-ECD can be produced fromP. pastoris.

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