Threadfin Bream (threadfin + bream)

Distribution by Scientific Domains


Selected Abstracts


Tuna Pepsin: Characteristics and Its Use for Collagen Extraction from the Skin of Threadfin Bream (Nemipterus spp.)

JOURNAL OF FOOD SCIENCE, Issue 5 2008
S. Nalinanon
ABSTRACT:, Pepsin from the stomach of albacore tuna, skipjack tuna, and tongol tuna was characterized. Pepsin from all tuna species showed maximal activity at pH 2.0 and 50 °C when hemoglobin was used as a substrate. Among the stomach extract of all species tested, that of albacore tuna showed the highest activity (40.55 units/g tissue) (P < 0.05). Substrate-Native-PAGE revealed that pepsin from albacore tuna and tongol tuna consisted of 2 isoforms, whereas pepsin from skipjack tuna had only 1 form. The activity was completely inhibited by pepstatin A, while EDTA (ethylenediaminetetraacetic acid), SBTI (soybean trypsin inhibitor), and E-64 (1-(L -trans-epoxysuccinyl-leucylamino)-4-guanidinobutane) exhibited negligible effect. The activity was strongly inhibited by SDS (sodium dodecyl sulfate) (0.05% to 0.1%, w/v). Cysteine (5 to 50 mM) also showed an inhibitory effect in a concentration dependent manner. ATP, molybdate, NaCl, MgCl2, and CaCl2 had no impact on the activity. When tuna pepsin (10 units/g defatted skin) was used for collagen extraction from the skin of threadfin bream for 12 h, the yield of collagen increased by 1.84- to 2.32-fold and albacore pepsin showed the comparable extraction efficacy to porcine pepsin. The yield generally increased with increasing extraction time (P < 0.05). All collagen obtained with the aid of tuna pepsin showed similar protein patterns compared with those found in acid-solubilized collagen. Nevertheless, pepsin from skipjack tuna caused the degradation of , and , components. All collagens were classified as type I with large portion of ,-chain. However, proteins with molecular weight (MW) greater than 200 kDa were abundant in acid-solubilized collagen. [source]


Biochemical and Conformation Changes of Actomyosin from Threadfin Bream Stored in Ice

JOURNAL OF FOOD SCIENCE, Issue 3 2002
J. Yongswawatdigul
ABSTRACT: Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca2+ -, EDTA-, Mg2+ -, and Mg2+ -Ca2+ -ATPase activities of actomyosin decreased, whereas Mg2+ -EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A significant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE. [source]


Colour improvement of common carp (Cyprinus carpio) fillets by hydrogen peroxide for surimi production

INTERNATIONAL JOURNAL OF FOOD SCIENCE & TECHNOLOGY, Issue 9 2008
Ali Jafarpour
Summary The preferred colour for surimi is white, but surimi prepared from light fillets of common carp (Cyprinus carpio) is slightly pink. Hydrogen peroxide (H2O2; 1,3% v/v) with and without sodium tri-polyphosphate (STP; 1,2% w/v) was added to a sodium carbonate bath (pH 7.0,11.5) resulting in a final pH range of 4.4,10.1 which was injected into carp fillets. After soaking and tumbling for 30 min at 4,10 °C, the fillets were evaluated for colour and water holding capacity (WHC). Fillets tumbled with treatment solution with different pH levels (7.0,11.5), but with no H2O2 or STP added, had improved colour with significantly (P < 0.05) higher L* compared with untreated fillets as the control. However, the colour improvement [(L* and colour deviation (,E)] was not significantly different (P > 0.05) within the pH levels (7.0,11.5) trialled. With increasing H2O2 levels (1,3%), fillets became lighter and ,E increased significantly (P < 0.05), especially with a 3% H2O2 treatment at pH of 10.5 (adjusted pH before H2O2 addition, actual pH after H2O2 addition was 8.2). The whiteness (L*,3b*) of kamaboko produced from treated (3% H2O2, pH 10.5) common carp light fillets was not significantly different to that of kamaboko from Alaska pollock and threadfin bream. Treatments combining H2O2 (3%) with STP (1,2%) significantly reduced the L* value obtained in comparison with fillets treated with only H2O2 (3%). Similarly, fillets treated with STP (1%) alone, resulting in lower L* values, irrespective of treatment pH (7.0,11.5). WHC, an indicator of the quality of the fillet texture, increased from 816 g/kg at pH 7.0 without STP to 841 g/kg at pH 11.5 with 1% STP. Treatment with H2O2 (without STP) decreased the WHC of the fillets. [source]


Age and growth of the Randall's threadfin bream Nemipterus randalli (Russell, 1986), a recent Lessepsian migrant in Iskenderun Bay, northeastern Mediterranean

JOURNAL OF APPLIED ICHTHYOLOGY, Issue 3 2010
D. Erguden
Summary Randall's threadfin bream, Nemipterus randalli, first recorded in Iskenderun Bay in Turkey in 2008, seems to have increased in the region. The species, widespread in the western Indian Ocean and with a rapid expansion, appears to have migrated to the bay via the Red Sea. Although its presence in the region has been published, there has been little or no information as to age and growth parameters of this Lessepsian migrant in its new habitat. The present study aims to determine the basic age and growth parameters of the species colonized in the region. A total of 379 collected individuals were studied from November 2007 to October 2008. Total specimen lengths ranged from 4.80 to 21.50 cm, and weights from 1.10 to 138.36 g. Maximum age was 3 years for both sexes. The length,weight relationship was described as W = 0.0011 × L3.061 (r2 = 0.982). The von Bertalanffy growth parameters were: L, = 34.96 cm; K = 0.214 year,1; t0 = ,1.244 year for the entire population. These data were compared with results from studies made in other geographic areas. [source]


Tuna Pepsin: Characteristics and Its Use for Collagen Extraction from the Skin of Threadfin Bream (Nemipterus spp.)

JOURNAL OF FOOD SCIENCE, Issue 5 2008
S. Nalinanon
ABSTRACT:, Pepsin from the stomach of albacore tuna, skipjack tuna, and tongol tuna was characterized. Pepsin from all tuna species showed maximal activity at pH 2.0 and 50 °C when hemoglobin was used as a substrate. Among the stomach extract of all species tested, that of albacore tuna showed the highest activity (40.55 units/g tissue) (P < 0.05). Substrate-Native-PAGE revealed that pepsin from albacore tuna and tongol tuna consisted of 2 isoforms, whereas pepsin from skipjack tuna had only 1 form. The activity was completely inhibited by pepstatin A, while EDTA (ethylenediaminetetraacetic acid), SBTI (soybean trypsin inhibitor), and E-64 (1-(L -trans-epoxysuccinyl-leucylamino)-4-guanidinobutane) exhibited negligible effect. The activity was strongly inhibited by SDS (sodium dodecyl sulfate) (0.05% to 0.1%, w/v). Cysteine (5 to 50 mM) also showed an inhibitory effect in a concentration dependent manner. ATP, molybdate, NaCl, MgCl2, and CaCl2 had no impact on the activity. When tuna pepsin (10 units/g defatted skin) was used for collagen extraction from the skin of threadfin bream for 12 h, the yield of collagen increased by 1.84- to 2.32-fold and albacore pepsin showed the comparable extraction efficacy to porcine pepsin. The yield generally increased with increasing extraction time (P < 0.05). All collagen obtained with the aid of tuna pepsin showed similar protein patterns compared with those found in acid-solubilized collagen. Nevertheless, pepsin from skipjack tuna caused the degradation of , and , components. All collagens were classified as type I with large portion of ,-chain. However, proteins with molecular weight (MW) greater than 200 kDa were abundant in acid-solubilized collagen. [source]


Biochemical and Conformation Changes of Actomyosin from Threadfin Bream Stored in Ice

JOURNAL OF FOOD SCIENCE, Issue 3 2002
J. Yongswawatdigul
ABSTRACT: Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca2+ -, EDTA-, Mg2+ -, and Mg2+ -Ca2+ -ATPase activities of actomyosin decreased, whereas Mg2+ -EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A significant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE. [source]