Growth and mortality of the narrowbarred Spanish Mackerel, Scomberomorus commerson (Lacepède), in Omani waters

Length composition data from quarterly catches of Omani narrowband Spanish mackerel, Scomberomorus commerson (Lacepède), landed between 1987 and 1995 were used to estimate the growth, mortality and exploitation parameters of the stock. Non-linear least square fitting provided a complete set of von Bertalanffy growth estimates: L _∞ = 173.6 cm fork length; K  = 0.28; and t ₀ = −0.86 years. There were no seasonal differences among the growth estimates. The instantaneous natural mortalities determined by three independent methods based on life-history parameters were 0.35, 0.64 and 0.77. Seasonal total mortalities were calculated by the length converted catch curve method for evaluating seasonal exploitation ratios ( E ). The E -values exceeded 0.4, indicating overexploitation during almost all the seasons studied. This was supported by the large reduction in the total landings of S . commerson from 27 762 t in 1988 to 3265 t in 1993.     

响应面法优化鲅鱼抗氧化肽发酵条件

为减少加工废弃物蛋白所造成的环境污染,提高水产品的利用率,探索了回收利用鲅鱼(Spanish mackerel)加工后富含蛋白质的废弃物,以寻找制备鲅鱼抗氧化肽的最佳生产条件。借助Design-Expert数据处理软件对苏云金芽孢杆菌Hy-4发酵产抗氧化肽的条件进行优化;在单因素试验的基础上,利用PlackettBurman试验设计法对影响发酵制备鲅鱼抗氧化肽的培养条件进行筛选。确定了影响发酵液总抗氧化活性的3个主要影响因素(P0.5)为发酵温度、培养基初始p H和料液比;在此基础上,利用最陡爬坡实验逼近3个关键因素的最大响应区域,再利用Box-Behnken试验设计及响应面分析法进行回归分析,通过求解回归方程得到产抗氧化肽的最优条件为:发酵时间48 h,发酵温度30℃,培养基初始p H 6.8,接种量2%,料液比1.45 g/50 m L,菌龄24 h。经过验证,发酵液总抗氧化活性达到537.73 U,较优化前提高了57.2%,与回归方程的预测值570.11 U相比,相对误差为5.7%,说明模型能够较好地预测菌株Hy-4发酵产抗氧化肽发酵液的总抗氧化性。     

The Influence of Cooking Parameters and Chilled Storage Time on Quality of Sous-Vide Atlantic Mackerel (Scomber scombrus)

The aim of the present study was to evaluate the effects of various sous-vide time–temperature regimes and their interactions on quality parameters of Atlantic mackerel (Scomber scombrus) during chilled storage. The mackerel ?llets were exposed to sous-vide treatment at 60, 75, and 90°C for 10, 15, and 20 min and further stored for 1, 3, and 7 days at 4 ± 1°C before analysis. Changes in pH, water content and cook loss, amount of water- and salt-soluble proteins, texture, and color parameters, as well as accumulation of lipid oxidation products in sous-vide-cooked mackerel were assessed. Sous-vide cooking time and temperature had the lowest contribution to the formation of primary and secondary products of lipid oxidation, as well as increase in yellowness of the fish flesh due to their accumulation; whereas duration of chilled storage led to a significant increase in oxidation and yellowness (p < 0.05). Duration of chilled storage also affected structural and textural properties of the fish muscle, leading to a decreased cook loss. At the same time, sous-vide cooking decreased the firmness of the fish muscle. Duration of chilled storage was found to have the highest significant effect (p < 0.001) on all physicochemical characteristics of sous-vide-cooked mackerel.     

Isolation,Purification, and Biochemical Characterization of Trypsin from Indian Mackerel (Rastralliger kanagurta)

Trypsin from viscera of Indian mackerel (Rastralliger kanagurta) was purified by ammonium sulphate precipitation and chromatographic techniques such as size exclusion, ion exchange, and affinity chromatography, with a 14.4-fold increase in specific activity and 18.7% recovery. The molecular weight of the trypsin was estimated to be approximately 26 kDa using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Purified trypsin showed amidase-specific activity which was determined using benzoyl-dl-arginine-p-nitroanilide (BAPNA). The optimum pH and temperature for isolated trypsin activity were 9.0 and 50°C, respectively. The purified trypsin was strongly inhibited by soybean trypsin inhibitor (SBTI) and N-p-tosyl-1-lysine chloromethyl ketone (TLCK). Purified trypsin showed almost 40% recovery at high NaCl concentration (30%). The N-terminal amino acid sequence of the first 10 amino acids of purified trypsin was IVGGYESQPH. The Michaelis-Menten constant (K_m) and catalytic constant (K_cat) of purified trypsin were 0.430 mM and 0.77 s^?1, respectively, determined using BAPNA as a substrate. Purified trypsin showed digestion of casein similar to bovine trypsin by the fluorometric method.