Increase of storage shelf life of locally produced salted/dried fish by redrying and/or packeting

Experiments were undertaken to prolong the storage life of salted/dried fish by re-drying and/or packing. The storage life under normal conditions is 51 days; re-drying the fish at 50°C for 12 hours extends the storage life only by 7 days. However, re-drying and packing gizzard shad (Gonialosa manminna ) in polyethylene maintains the fish in excellent conditions for well over 87 days. The use of air tight bags for storing good quality salted dried fish is recommended.

The storage of red snapper (Lutjanus spp.) in ice, chilled sea water and chilled fresh water

The results are given of trials conducted to determine the effect on quality of holding fish (Lutjanus species) in chilled freshwater and also to compare the quality loss of fish stored in chilled seawater and chilled freshwater and in ice. No adverse effects were observed when storing in chilled freshwater apart from loss of external appearance after 6 days storage; taste panel tests showed acceptable conditions up to 15 days. Chilled seawater is unsuitable for storage as it spoils the intake of salt from the medium, making the flesh unpalatable.

Genetic diversity of Yunnan local pig breeds inferred from blood protein electrophoresis

Protein electrophoresis was used to examine the blood protein polymorphism in Yunnan local pig breeds, i.e., the Saba pig, Dahe pig, and Diannan small-ear pig breeds, Of 38 genetic loci surveyed 9 were found to be polymorphic. The percentage of polymorphic loci (P) varies from 0.1875 to 0.2121, and the mean individual heterozygosity (H) varies front 0.0712 to 0.1027 in three pig breeds. The results indicate that blood protein polymorphism in Yunnan pig breeds is high. Yunnan local pig breeds have a wealth of genetic diversity at the level of blood proteins.

Changes in lipids of mussel during storage

Proximate composition, lipid and fatty acid components of dried mussel and changes in lipids during 1 year storage were studied. Male mussel contained lower fat contents and higher contents of polyunsaturated fatty acids of C20:5n-3, and C22:6n-3. High percentages of Cl6:1, Cl7:1, Cl8:3n-3, C20:3n-8 existed in NL and C!6:0, C18:0, Cl8:1n-9, C20:2n-6, C20:5n- 3, C22:6n-3 were very rich in PL. Triglycerides phosphatidylcholine, cholesterol were major components of mussel lipids. Free fatty acids (FFA) increased greatly and phospholipids decreased during storage, saturated fatty acids showed an increase trend and polyunsaturated fatty adds decreased differently. Dried mussels were vacuum packed and air packed and packaging methods had a great influence on the oxidation of mussellip,ids, indicating preference of vacuum packaging.

Minimize frequency fluctuations of isolated power system with wind farm by using superconducting magnetic energy storage

Wind power generation as one of the most popular renewable energy applications is absorbing more and more attention all over the world. However, output power fluctuations of wind farm due to random variations of wind speed can cause network frequency and voltage flicker in power systems. The power quality consequently declines, particularly in an isolated power system such as the power system in a remote community or a small island. This paper proposes an application of superconducting magnetic energy storage (SMES) to minimize output fluctuations of an isolated power system with wind farm. The isolated power system is fed by a diesel generator and a wind generator consisting of a wind turbine and squirrel cage induction machine. The control strategy is detailed and the proposed system is evaluated by simulation in Matlab/Simulink.

In vitro phagocytic study of blood leucocytes and peritoneal macrophages of walking catfish Clarias batrachus ( Ham.) against Aeromonas hydrophila and Escherichia coli.

In observation of in vitro phagocytic activity against Aeromonas hydrophila isolate 34k (a virulent form) and Escherichia coli (an avirulent bacteria) of neutrophil- and monocyte-like cells of walking catfish Clarias batrachus showed phagocytosis. N eutrophils and monocytes phagocytized the avirulent form of bacterial isolate more than the virulent one. Other blood leucocytes did not show phagocytosis. Peritoneal macrophage of the fish were separated by glycogen elicitation and the macrophages were being adhered on plastic cover slips for studying their in vitro phagocytic activity. Most of the cells were alive after adherence and showed phagocytosis against the virulent and avirulent bacteria. The percent phagocytosis and phagocytic index were higher against the avirulent E. coli than the virulent A. hydrophila.

ISOLATION AND PROPERTIES OF A BLOOD-COAGULATION FACTOR-X ACTIVATOR FROM THE VENOM OF KING COBRA (OPHIOPHAGUS HANNAH)

A specific blood coagulation factor X activator was purified from the venom of Ophiophagus hannah by gel filtration and two steps of FPLC Mono-Q column ion-exchange chromatography. It showed a single protein band both in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and alkaline polyacrylamide gel electrophoresis. The mol. wt was estimated to be 62,000 in non-reducing conditions and 64,500 in reducing conditions by SDS-PAGE. The isoelectric point was found to be pH 5.6. The enzyme had weak amidolytic activities toward CBS 65-25, but it showed no activities on S-2266, S-2302, thrombin substrate S-2238, plasmin substrate S-2251 or factor Xa substrate S-2222. It had no arginine esterase activity toward substrate benzoylarginine ethylester (BAEE). The enzyme activated factor X in vitro and the effect was absolutely Ca2+ dependent, with a Hill coefficient of 6.83. It could not activate prothrombin nor had any effect on fibrinogen and thus appeared to act specifically on factor X. The procoagulant activity of the enzyme was almost completely inhibited by serine protease inhibitors like PMSF, TPCK and soybean trypsin inhibitor; partially inhibited by L-cysteine. Metal chelator EDTA did not inhibit its procoagulant activity. These results suggest that the factor X activator from O. hannah venom is a serine protease.

AN ACTIVATOR OF BLOOD-COAGULATION FACTOR-X FROM THE VENOM OF BUNGARUS-FASCIATUS

A specific activator of blood coagulation factor X was purified from the venom of Bungarus fasciatus by gel filtration and by ion-exchange chromatography on a Mono-Q column (FPLC). It consisted of a single polypeptide chain, with a mel. wt of 70,000 in reducing and non-reducing conditions. The enzyme had an amidolytic activity towards the chromogenic substrates S-2266 and S-2302 but it did not hydrolyse S-2238, S2251 or S-2222, which are specific substrates for thrombin, plasmin and factor Xa, respectively. The enzyme activated factor X in vitro and the effect was Ca2+ dependent with a Hill coefficient of 7.9. As with physiological activators, the venom activator cleaves the heavy chain of factor X, producing the activated factor Xa alpha. The purified factor X activator from B. fasciatus venom did not activate prothrombin, nor did it cleave or clot purified fibrinogen. The amidolytic activity and the factor X activation activity of the factor X activator from B. fasciatus venom were readily inhibited by serine protease inhibitors such as diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), benzamidine and by soybean trypsin inhibitor but not by EDTA. These observations suggest that the factor X activator from B. fasciatus venom is a serine protease. It therefore differs from those of activators obtained from Vipera russelli and Bothrops atrox venoms, which are metalloproteinases.

Effects of Pallas' viper (Agkistrodon halys pallas) venom on blood coagulation and characterization of a prothrombin activator

The action of Pallas' viper (Agkistrodon halys pallas) venom on blood coagulation was examined in vitro and a strong anticoagulant effect was observed. This action was abolished after treatment with a specific inhibitor of phospholipase A(2) activity (p-bromophenacyl bromide), revealing a procoagulant action in low concentrations of treated venom (around 1 mu g/ml). The effect of the venom an haemostasis was further characterized by measuring its ability to activate purified blood coagulation factors. It is concluded that A. halys pallas venom contains prothrombin activation activity. A prothrombin activator (aharin) was purified from the venom by Sephadex G-75 gel filtration and ion-exchange chromatography on a Mono-Q column. It consisted of a single polypeptide chain, with a mol. wt of 63,000. Purified aharin possessed no amidolytic activity on chromogenic substrates. It did not act on other blood coagulation factors, such as factor X and plasminogen, nor did it cleave or clot purified fibrinogen. The prothrombin activation activity of aharin was readily inhibited by ethylenediamine tetracetic acid (a metal chelator), but specific serine protease inhibitors such as diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride had no effect on it. These observations suggest that, like those prothrombin activators from Echis carinatus and Bothrops atrox venoms, the prothrombin activator from A. halys pallas venom is a metalloproteinase. (C) 1998 Elsevier Science Ltd. All rights reserved.

Cloning and characterization of a blood coagulation factor IX-binding protein from the venom of Trimeresurus stejnegeri

A blood coagulation factor IX-binding protein (TSV-FIX-BP) was isolated from the snake venom of Trimeresurus stejnegeri. On SDS-polyacrylamide gel electrophoresis, TSV-FIX-BP showed a single band with an apparent molecular weight of 23,000 under non-reducing conditions. and two distinct bands with apparent molecular weights of 14,800 and 14,000 under reducing conditions. cDNA clones containing the coding sequences of TSV-FIX-BP were isolated and sequenced to determine the structure of the precusors of TSV-FIX-BP subunits. The deduced amino acid sequences of two subunits of TSV-FIX-BP were confirmed by N-terminal protein sequencing and trypsin-digested peptide mass fingerprinting. TSV-FIX-BP was a nonenzymatic C-type lectin-like anti-coagulant. The anti-coagulant activity of TSV-FIX-BP was mainly caused by its dose dependent interaction with blood coagulation factor IX but not with blood coagulation factor X. (C) 2003 Elsevier Science Ltd. All rights reserved.

Suitability of sodium lactate as cryoprotectant and its effect on gel forming ability and protein denaturation of croaker fish surimi during frozen storage

The effect of sodium lactate is compared with sucrose + sorbitol + sodium tri-poly phosphate as cryoprotectant on gel forming ability & protein denaturation of croaker surimi during frozen storage at -20±2°C for 90 days was evaluated. The quality of Croaker surimi with 6% (w/v) sodium lactate was examined in terms of biochemical parameters of muscle protein, thaw drip, gel strength and calcium ATPase activity :.omparing with those of surimi added with sucrose/sorbitol & without additive as control. Both the cryoprotectants minimized the negative effects of frozen storage on physico-chemical traits of myofibrillar proteins which was evident from the biochemical and sensory parameters. The residual Ca2+ ATPase activity and gel strength of surimi with sodium lactate were higher than those of control throughout 90 days of storage. Ca2+ A TPase activity and gel strength found a high positive correlation. From the results, it was found that sodium lactate was equally effective in preservation of croaker muscle protein native structure during frozen storage as the sucrose/ sorbitol and also less sweet without any risk of maillard browning.

Shelf life of dried products from small indigenous fish species under various packing and storage conditions

The overall quality of five SIS products was found in good condition up to 2 months storage on the basis of organoleptic, biochemical and bacteriological characteristics and all the products was excellent in sealed packed condition up to 45 days of storage. However, quality of the products stored in open air atmospheric temperature was found excellent for first 15 days. In an average the initial moisture content was in the range of 13.5 to 15.0% with highest moisture content in puti and lowest in chapila. At the end of the 60 days the moisture content reached to the range of 18.5 to 19.0% which was more or less near the recommended limit of 16% for dried fishery products. The moisture content beyond the recommended limit as the storage period increased further and at the end of 90 days the moisture content increased to the range of 22.9 to 24% when organoleptically the product quality became very poor. The changes in the value of total volatile base nitrogen (TVB-N), peroxide value (PO), moisture and aerobic plate count (APC) of solar tunnel dried products in sealed polythene packages were investigated during 60 days of storage. There was little or no differences in TVB-N, PO and bacterial load of each species packed under various polythene density. The initial TVB-N values were in the range of 10.30 to 12.40 mg/100g of the samples. TVB-N value increased slowly up to the end of the storage period and was to in the range of 46.20 to 57.00 mg/1 00 g of sample. Initially the peroxide values (P.O.) were in the range of 6.54 to 8.40 m.eq./kg oil of the samples. During 60 days of storage, P.O. values increased slowly and at the end of the storage period these values reached to the range of 22.00 to 25.30meq./kg of sample. The initial APC was in the range 5.3xl04-7.3x104 CFU/g. The bacterial load increased slowly and at the end of the 60 days storage period reached to the range 6.6x106 - 8.6x107 CFT/g.

Blood cells as targets of snake toxins

Snake venoms are mixtures of enzymes and peptides which exert toxicological effects by targeting their substrates or receptors upon envenomation. Snake venom proteins widely affect vascular system including circulating blood cells, coagulation factors, an

Toward an understanding of the molecular mechanism for successful blood feeding by coupling proteomics analysis with pharmacological testing of horsefly salivary glands

Horseflies are economically important blood-feeding arthropods and also a nuisance for humans and vectors for filariasis. They rely heavily on the pharmacological properties of their saliva to get a blood meal and suppress immune reactions of hosts. Little information is available on antihemostatic substances in horsefly salivary glands; especially no horsefly immune suppressants have been reported. By proteomics or peptidomics and coupling transcriptome analysis with pharmacological testing, several families of proteins or peptides, which act mainly on the hemostatic system or immune system of the host, were identified and characterized from 30,000 pairs salivary glands of the horsefly Tabanus yao (Diptera, Tabanidae). They are: (i) a novel family of inhibitors of platelet aggregation including two members, which possibly inhibit platelet aggregation by a novel mechanism and act on platelet membrane, (ii) a novel family of immunosuppressant peptides including 12 members, which can inhibit interferon-gamma production and increase interleukin-10 secretion, (iii) a serine protease inhibitor with 56 amino acid residues containing anticoagulant activity, (iv) a serine protease with anticoagulant activity, (v) a protease with fibrinogenolytic activity, (vi) three families of antimicrobial peptides including six members, (vii) a hyaluronidase, (viii) a vasodilator peptide, which is an isoform of vasotab identified from Hybomitra bimaculata, and interestingly (ix) two metallothioneins, which are the first metallothioneins reported from invertebrate salivary glands. The current work will facilitate the understanding of the molecular mechanisms of the ectoparasite-host relationship and help in identifying novel vaccine targets and novel leading pharmacological compounds.