Priacanthus Tayenus Research Articles

Chicken plasma protein affects gelation of surimi from bigeye snapper ( Priacanthus tayenus)

Effect of chicken plasma protein (CPP) at different concentrations on gel properties of grade SA and A bigeye snapper surimi was investigated. Addition of 0.5% CPP in combination with setting at 40 °C for 30 min prior to heating at 90 °C for 20 min resulted in the highest breaking force and deformation ( P<0.05). However, whiteness decreased to some extent. CPP was able to prevent the degradation of surimi proteins as indicated by the decrease in TCA-soluble peptides ( P<0.05). Electrophoretic studies revealed that myosin heavy chain underwent polymerization to a lower extent as CPP concentration increased. Therefore, CPP worked as protease inhibitor rather than protein cross-linker. Microstructure of kamaboko gels, added with 0.5% CPP, had less linkage between protein strands with a coarser fibrillar structure, indicating the interfering effect of CPP on cross-linking of myofibrillar proteins. Thus, at an appropriate amount, CPP possibly worked as a filler in the surimi gel matrix, resulting in gel strengthening.

Comparative study on proteolysis of two species of bigeye snapper, Priacanthus macracanthus and Priacanthus tayenus

AbstractProteolytic activity in muscle from two species of bigeye snapper (Priacanthus macracanthus and Priacanthus tayenus) was studied. Autolysis of mince and washed mince at 50 and 60 °C was compared. Higher degradation of myosin heavy chain was observed in both mince and washed mince from P macracanthus than in those from P tayenus, especially when the incubation time was increased. Autolysis of washed mince from both species was inhibited by soybean trypsin inhibitor, suggesting that myofibril‐associated proteases were serine proteases. When sarcoplasmic proteolytic activity in P macracanthus muscle was studied, two activity peaks with an optimum temperature of 60 °C were observed at pH 6.5 and 8.5. The activities of both peaks were mostly inhibited by soybean trypsin inhibitor, suggesting that the major protease was a serine protease. Major sarcoplasmic proteolytic activity in P macracanthus muscle was found at Mr 62 000 on sodium dodecyl sulphate substrate gel. For P tayenus sarcoplasmic proteolytic activity, two activity peaks with an optimum temperature of 60 °C were found at pH 5.0 and 8.5. The pH 5.0 peak activity was effectively inhibited by pepstatin A, while the pH 8.5 peak activity was inhibited by several inhibitors. The results indicated that various sarcoplasmic proteases were present in P tayenus muscle. The two species contained different sarcoplasmic proteases in terms of composition and activity level. P macracanthus muscle generally had higher sarcoplasmic proteolytic activities than P tayenus muscle. Copyright © 2003 Society of Chemical Industry

Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish

Effects of setting at 25 °C on textural properties and cross-linking of myofibrillar proteins in surimi produced from threadfin bream ( Nemipterus bleekeri), bigeye snapper ( Priacanthus tayenus), barracuda ( Sphyraena jello) and bigeye croaker ( Pennahai macrophthalmus) were investigated. Increase in setting time (0–8 h) resulted in a higher breaking force and deformation for all surimi gels tested ( P<0.05). Increased gel strength was associated with increase in non-disulfide bond formation and decreased heavy chain myosin. Proteins underwent degradation during setting; however polymerization occurred to a much higher extent, leading to a strengthened gel matrix. Therefore, setting at 25 °C, for an appropriate time, should be a promising means to improve gelling properties of surimi produced from tropical fish.

Transglutaminase-mediated setting in bigeye snapper Surimi

Effect of setting induced by endogenous transglutaminase (TGase) in two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus, on gel properties and protein cross-linking was investigated. Setting at either 25 or 40 °C, prior to heating at 90 °C resulted in the increase in both breaking force and deformation of surimi from both species, particularly when setting time increased ( P<0.05). A decrease in solubility of surimi gels in a mixture of sodium dodecyl-sulfate, urea and β-mercaptoethanol suggested increased formation of non-disulfide covalent bonding which coincided with increased gel strength and the decrease in myosin heavy chain (MHC) polypeptide. The optimum conditions for setting of surimi sol was found to be 40 °C for 2 h for P. tayenus and 25 °C for 3 h for P. macracanthus. Assayed by monodancylcadaverine (MDC)-incorporation method, TGase from P. tayenus and P. macracanthus exhibited an optimum temperature at 40 and 25 °C, respectively. In addition, the breaking force and deformation of surimi from both species increased markedly with the addition of calcium chloride, while they decreased considerably in the presence of EDTA, N-methylmaleimide and ammonium chloride. The results confirmed that endogenous transglutaminase played an important role in gel enhancement of surimi from both species of bigeye snapper.

Gel‐forming properties of surimi produced from bigeye snapper, Priacanthus tayenus and P macracanthus, stored in ice

AbstractThe influence of iced storage of two species of bigeye snapper, Priacanthus tayenus and P macracanthus, on the gel‐forming ability of the resulting surimi was investigated. Upon iced storage, whole fish underwent deterioration faster than beheaded/eviscerated fish. Total volatile base and trimethylamine contents of whole fish were higher than those of beheaded/eviscerated fish, particularly after 9 days of storage (P &lt; 0.05). P macracanthus muscle was more susceptible to proteolytic degradation than P tayenus muscle. Ca2+‐ATPase activity decreased as the storage time increased (P &lt; 0.05), indicating the denaturation of myosin. A marked decrease in Ca2+‐ATPase activity was found in whole fish kept for more than 6 days in ice (P &lt; 0.05). Breaking force and deformation of surimi gels from both species decreased, with a concomitant decrease in whiteness, as the storage time increased (P &lt; 0.05). Beheading and evisceration of fish retarded the deterioration. However, the gel‐forming ability of surimi produced from both species decreased continuously throughout iced storage (P &lt; 0.05), probably owing to the denaturation and degradation of myofibrillar proteins.© 2002 Society of Chemical Industry

GEL PROPERTIES OF BIGEYE SNAPPER (PRIACANTHUS TAYENUS) SURIMI AS AFFECTED BY SETTING AND PORCINE PLASMA PROTEINS

ABSTRACTEffects of setting temperature, time, and addition of porcine plasma protein (PPP) on gel properties of surimi from bigeye snapper (Priacanthus tayenus) were investigated. Breaking force and deformation of the surimi gels increased as the setting time and temperature increased. The gel preincubated at 35C for 90 min in the presence of 0.5% PPP, followed by cooking at 90C for 20 min showed the maximum force and deformation. The decrease in solubility of the resultant suwari and kamaboko gels in solution containing sodium dodecyl sulfate, urea and β‐mercaptoethanol suggested that gel enhancement was mainly mediated through the formation of nondisulfide covalent bonds catalyzed by both transglutaminase (TGase) in fish muscle and porcine plasma. Addition of PPP slightly decreased the whiteness of the kamaboko gels.

Differences in Gelation Characteristics of Natural Actomyosin from Two Species of Bigeye Snapper, Priacanthus tayenus and Priacanthus macracanthus

ABSTRACT: Natural actomyosin (NAM) of P. tayenus exhibited higher turbidity and storage modulus (G′) upon heating, compared to that of P. macracanthus, suggesting the higher protein aggregation and rigidity. At temperature above 35 °C, P. tayenus NAM had higher surface hydrophobicity and disulfide bond formation than P. macracanthus NAM. The α‐helix content of NAM from both fish species decreased as the temperature increased, indicating changes in structural conformation during heating. NAM gel from P. tayenus rendered more three‐dimensional network than that from P. macracanthus. These results indicated that P. tayenus NAM possessed superior gelling characteristic to P. macracanthus NAM due to the higher aggregation of protein caused by both hydrophobic interaction and disulfide bond.

Porcine plasma protein as proteinase inhibitor in bigeye snapper (Priacanthus tayenus) muscle and surimi

AbstractPorcine plasma protein (PPP) showed inhibitory activity towards trypsin, papain, digestive enzymes and modori‐inducing proteinases from bigeye snapper. Among the fractions prepared, fraction IV‐1 exhibited the highest inhibitory activity against all proteinases tested and the autolysis of fish muscle. At a level of 0.5% (w/w), both PPP and fraction IV‐1 effectively prevented the degradation of myosin heavy chain in fish muscle. The inhibitory activity of fraction IV‐1 was stable up to 60 °C. Incorporation of fraction IV‐1 significantly increased the breaking force, deformation and water‐holding capacity of surimi gel from bigeye snapper (P &lt; 0.05). However, no increase in breaking force and deformation was found when fraction IV‐1 was added at a level above 0.3% (w/w) (P &gt; 0.05). No significant change in whiteness of surimi gel was observed with the addition of fraction IV‐1 (P &gt; 0.05).© 2001 Society of Chemical Industry

Functional properties of surimi powder from three Malaysian marine fish

SummaryLizardfish (Saurida tumbil), threadfin bream (Nemipterus japonicus) and purple‐spotted bigeye (Priacanthus tayenus) surimi were freeze‐dried to produce surimi powder. The resulting surimi powder contained 72.8–73.4% protein and 16.8–17.5% carbohydrate. Functional properties such as solubility, gelation capacity, water‐holding capacity (WHC), emulsification, foaming properties and colour varied from species to species. The surimi powder formed gels and produced about 90% emulsification at a concentration of 1.0%. Threadfin bream was found to be the best source for surimi powder production, followed by purple‐spotted bigeye and lizardfish, respectively.

A Specific DNA Probe to Identify the Intermediate Host of a Common Microsporidian Parasite of Penaeus merguiensis and P. monodon

The intermediate host required for transmission or a common microsporidian (Agmasoma) parasite of the penaeid shrimp, Penaeus merguiensis and P. monodon is still unknown, so cross­infection studies and studies to develop preventive or therapeutic measures are not possible. The purpose of this study was to develop a specific nucleic acid probe to aid in finding the intermedi­ate host, and in tracing the life cycle of the parasite. To prepare the probe, DNA was extracted from purified microsporidian spores derived from infections in P. merguiensis and P. monodon. The prepared genomic DNAs were then incompletely digested with Sau3AI and fragments were ligated to the pGEM7Zf+ vector before being transformed to Escherichia coli JM109. Candidate probes were screened by in situ colony hybridization, slot blot hybridization and Southern blot hybridization using dATP32P labelled Agmasoma DNA. All the candidate probes from each Agmasoma source cross-hybridized with whole Agmasoma DNA digest from the other source and with roughly the same quality of signal. Finally, a probe (I-mo) derived from Agmasoma of P. monodon gave the best sensitivity because it was found to be derived from a multicopy sequence and it did not cross-hybridize with other organisms from shrimp ponds (i.e., both shrimp species, Artemia, mixed protozoa, E. coli and Vibrio parahaemolyticus). DNA extracts were prepared from 22 animal species (including fish, crustaceans, molluscs and mixed plankton) present in seawater canals where microsporidian-infected shrimp were present. These were probed with digoxigenin (DIG) labelled 1-mo probe. Two fish species, Priacanthus tayenus and Scatophagus argus, gave positive hybridization signals.

Growth, mortality, parasitism, and potential yields of two Priacanthus species in the South China Sea

In the northern part of the South China Sea the ‘big‐eye’, Priacanthus tayenus, spawned once a year in June, had von Bertalanffy growth parameters of k = 0.8 and L∞= 30 cm, and a mean total annual instantaneous mortality of Z= 2.0, calculated from adjusted catch curves and a mean length equation. The natural mortality rate M= 1.4, fishing mortality rate F= 0.6, and the exploitation rate (E) was 0.27. The maximum potential yield, calculated using Marten's method, was 0.06 kg/recruit when F= 5.4. The fish were heavily parasitised by the protozoan Pleistophora priacanthicola.A second big‐eye, P. macracanthus, spawned twice a year in May‐June and September, had growth parameters of κ= 0.7 and L∞= 32, and population parameters of Z= 2.0, .F= 0.7, and E= 0.34. The maximum potential yield was 0.13 kg/recruit when F= 5.8.A marked reduction in fishing mortality occurred for both species between 1965 and 1966, coinciding with the onset of the Chinese Cultural Revolution. Our estimates of maximum potential yield correspond to fishing mortalities eight times estimated levels, though such heavy exploitation could risk recruitment failure.

A new species of Pleistophora from big‐eyes, Priacanthm tayenus Richardson, and P. macracanthus Cuvier and Valenciennes, from the South China Sea

Abstract. Pleistophora priacanthusis sp. nov. is described from big‐eyes, Priacanthus tayenus and P. macracanthus, from the South China Sea. The clinical signs, prevalence, intensity and site of infection of the infected fish, the general effect of the parasite on the host, seasonal distribution and sex differences are reported. The morphology of cysts, spores, sporonts and the characteristic features of the new species using the light microscope are described.