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Muscle Proteins (muscle + protein)
Kinds of Muscle Proteins Terms modified by Muscle Proteins Selected AbstractsEFFECT OF VARIOUS ANTIOXIDANTS ON THE OXIDATIVE STABILITY OF ACID AND ALKALI SOLUBILIZED MUSCLE PROTEIN ISOLATESJOURNAL OF FOOD BIOCHEMISTRY, Issue 2 2009SIVAKUMAR RAGHAVAN ABSTRACT Protein isolates prepared from cod (Gadus morhua) myofibrillar proteins using acid or alkali solubilization are susceptible to oxidative rancidity. Oxidation could be delayed by the exogenous addition of antioxidants. The objective of this research was to compare the efficacy of antioxidants such as ,-tocopherol, butylated hydroxyanisole (BHA) and propyl gallate, to inhibit oxidation in acid- and alkali- solubilized cod protein isolates. Oxidation was catalyzed using cod hemolysate. Oxidation of lipids was monitored by the measurement of thiobarbituric acid reactive substances and painty odor. Results showed that protein isolates prepared using the acid process was significantly (P < 0.05) more susceptible to lipid oxidation than alkali-solubilized protein isolates. Regardless of pH treatments, the efficacy of various antioxidants decreased in the order propyl gallate > BHA > ,-tocopherol. PRACTICAL APPLICATIONS Research has shown that seafood available for human consumption is rapidly getting depleted and that many fish species may become extinct in the next half-century or so. Acid and alkali solubilization methods are recent but well-known techniques used for preparing protein isolates from under-utilized aquatic species and the by-products of seafood industry. Although numerous researchers have studied the use of acid and alkali processes on several sources of seafood, almost no research has been done on the use of antioxidants to protect protein isolates from lipid oxidation. In our research, we have studied the effect of various antioxidants on the oxidative stability of acid- and alkali-solubilized fish myofibrillar proteins. The results from this work will enable the seafood industry to properly identify the process and the type of antioxidants required for making muscle food products with increased oxidative stability. [source] ROLE OF INITIAL MUSCLE pH ON THE SOLUBILITY OF FISH MUSCLE PROTEINS IN WATERJOURNAL OF FOOD BIOCHEMISTRY, Issue 4 2004STEPHEN D. KELLEHER The solubility of the myofibrillar and cytoskeletal proteins in water was determined for the muscle tissue often species offish. The flesh of six white-muscled fish had pH's at the time of processing above pH 6.6 and greater than 80% of their myofibrillar/cytoskeletal proteins were soluble in water. The flesh of three pelagic species and a shark had pH values when processed below 6.6 and the water solubility of their myofibrillar and cytoskeletal proteins was less than 40%. When the washed minced muscle of one of the white-fleshed species, cod, was exposed to low pH, the solubility of its myofibrillar and cytoskeletal proteins decreased substantially. The water solubility of the cod myofibrillar and cytoskeletal proteins could be reestablished by washing the acid-treated cod flesh with neutral salt solutions. It is suggested that pH values below 6.6 modify certain proteins which prevent the water-extractability of the rest of the myofibrillar and cytoskeletal proteins from being expressed. [source] Role of Reduced Ionic Strength and Low pH in Gelation of Chicken Breast Muscle ProteinJOURNAL OF FOOD SCIENCE, Issue 1 2005S. Ke And ABSTRACT: Elastic gels with a high moisture content of 88% were prepared at an acidic pH and low ionic strength. The relationship among pH, ionic strength, water-holding capacity, and fold score of gels was investigated. A decrease of pH from 4.1 to 3.7 or below increased gel elasticity and significantly decreased water loss under pressure (P < 0.05). In the presence of sodium chloride, gels made at pH 3.5 to 3.7 had decreased elasticity and increased water loss under pressure. Prior freezing increased the water loss of gels under pressure. Gels made with phosphoric acid and hydrochloric acid lost less water under pressure than those made with citric acid. The percentage loss of water from cylindrical gels was inversely related to the height of the cylinders, suggesting that surface effects were involved. These results suggest that net positive charges on the protein molecules at low pH produced electrostatic repulsion, which was a major driving force for water uptake in the low-salt gels. [source] Characterization and Functionality of Frozen Muscle Protein in Volador (Illexcoindetii), Pota (Todaropsis eblanae), and Octopus (Eledone cirrhosa)JOURNAL OF FOOD SCIENCE, Issue 7 2003C. Ruiz-Capillas ABSTRACT: Three species of cephalopods: volador (Illex coindetii), pota (Todaropsis eblanae), and octopus (Eledone cirrhosa) were classified according to sex, stage of sexual development, and anatomical zone for characterization and functionality of their muscle proteins. The 3 species exhibited very similar levels of total protein. Octopus mantles and arms contained the least proline and the most hydroxyproline. The highest solubility values in immature pota coincided with the lowest apparent viscosity and emulsifying capacity values. The highest insolubility values observed in octopus coincided with the highest viscosity and emulsifying capacity values. However, in volador which exhibited an intermediate solubility, viscosity was very high and emulsifying capacity was very low. [source] Protein requirement for maintenance and maximum growth of two-banded seabream (Diplodus vulgaris) juvenilesAQUACULTURE NUTRITION, Issue 1 2009R.O.A. OZÓRIO Abstract The effects of various dietary protein levels on growth performance, whole body composition and nutrient utilization were studied in two-banded sea bream (Diplodus vulgaris), a candidate species for aquaculture. Fish (initial weight 6.1 g) were fed to satiety six iso-energetic diets, containing 5%, 12.5%, 25%, 35%, 45% or 55% of crude protein during 72 days. Fish fed 35% and 45% protein attained better growth and feed utilization than the other groups (P < 0.05). Daily growth index and feed conversion ratio were the poorest for fish fed 5% and 12.5% protein (P < 0.001), while the 25% and 55% protein groups had intermediate performance. Lipid retention increased significantly from 13.7% to 30.1% (P < 0.0001) and protein retention decreased from 35.5% to 21.3% (P < 0.01) with increasing protein levels from 12.5% to 45%. Muscle protein, lipid and energy concentrations were not significantly affected by dietary protein level. The estimated protein requirement for maintenance and maximum growth of two-banded seabream growing from 6 to 20 g were 7.5% and 35.7%, respectively. Protein requirements as calculated from body protein gain were 2.3 and 6.5 g of protein intake per kilogram body weight per day. [source] Proteomic analysis of proteins associated with body mass and length in yellow perch, Perca flavescensPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 11 2008John Mark Reddish Abstract The goal of commercial yellow perch aquaculture is to increase muscle mass which leads to increased profitability. The accumulation and degradation of muscle-specific gene products underlies the variability in body mass (BM) and length observed in pond-cultured yellow perch. Our objective was to apply a combination of statistical and proteomic technologies to identify intact and/or proteolytic fragments of muscle specific gene products involved in muscle growth in yellow perch. Seventy yellow perch randomly selected at 10, 12, 16, 20, and 26,wk of age were euthanized; BM and length were measured and a muscle sample taken. Muscle proteins were resolved using 5,20% gradient SDS-PAGE, stained with SYPRO® Ruby and analyzed using TotalLabÔ software. Data were analyzed using stepwise multiple regression with the dependent variables, BM and length and proportional OD of each band in a sample as a potential regressor. Eight bands associated with BM (R2,=,0.84) and nine bands with length (R2,=,0.85) were detected. Protein sequencing by nano-LC/MS/MS identified 20 proteins/peptides associated with BM and length. These results contribute the identification of gene products and/or proteolytic fragments associated with muscle growth in yellow perch. [source] Effect of amino acid and glucose administration following exercise on the turnover of muscle protein in the hindlimb femoral region of ThoroughbredsEQUINE VETERINARY JOURNAL, Issue S36 2006A. MATSUI Summary Reasons for performing study: In man, muscle protein synthesis is accelerated by administering amino acids (AA) and glucose (Glu), because increased availability of amino acids and increased insulin secretion, is known to have a protein anabolic effect. However, in the horse, the effect on muscle hypertrophy of such nutrition management following exercise is unknown. Objectives: To determine the effect of AA and Glu administration following exercise on muscle protein turnover in horses. We hypothesise that administration of AA and Glu after exercise effects muscle hypertrophy in horses, as already shown in man and other animals. Methods: Measurements of the rate of synthesis (Rs) and rate of degradation (Rd) of muscle protein in the hindlimb femoral region of thoroughbred horses were conducted using the isotope dilution method to assess the differences between the artery and iliac vein. Six adult Thoroughbreds received a continuous infusion of L-[ring- 2H5]-phenylalanine during the study, the stable period for plasma isotope concentrations (60 min), resting periods (60 min), treadmill exercise (15 min) and recovery period (240 min). All horses were given 4 solutions (saline [Cont], 10% AA [10-AA], 10% Glu [10-Glu] and a mixture with 10% AA and 10% Glu [10-Mix]) over 120 min after exercise, and the Rs and Rd of muscle protein in the hindlimb measured. Results: The average Rs during the 75,120 min following administration of 10-Mix was significantly greater than for the other solutions (P<0.05). The second most effective solution was 10-AA, and there was no change in Rs after 10-Glu. Conclusions: Administration of AA following exercise accelerated Rs in the hindlimb femoral region, and this effect was enhanced when combined with glucose, because of increasing insulin secretion or a decreased requirement for AA for energy. Potential relevance: Further studies are required regarding the effect on muscle hypertrophy of supplementing amino acids and glucose in the feed of exercising horses. [source] The use of muscle protein for egg production in the Zebra Finch Taeniopygia guttataIBIS, Issue 2 2002Mat Cottam Pectoral muscle can be an important source of protein for birds. During egg formation Zebra Finches Taeniopygia guttata are able to compensate for nutritional inadequacies in their diet by utilization of the protein in their flight muscles. This analysis of flight muscle sarcoplasm supported earlier observations of protein depletion during egg production. However, SDS gel electrophoresis of the sarcoplasm produced no evidence to support a previous suggestion of the existence of a high molecular weight storage protein, and it is thought that the original observation may have arisen as an artefact of experimental methodology. During laying, protein removal from the sarcoplasm occurred over a range of different proteins and was not confined to any one specific protein band. Additionally, the protein band most reduced over the course of laying did not contain elevated levels of the amino acids most limiting to egg production. These results indicate that during laying, flight muscle sarcoplasm contributes towards the nutrient requirements of egg production from general protein reserves, rather than from a specific storage protein containing elevated levels of limiting amino acids. [source] Body protein does not vary despite seasonal changes in fat in the White Stork Ciconia ciconiaIBIS, Issue 1 2002Delphine Michard-Picamelot To understand how a large soaring bird, the White Stork Ciconia ciconia, copes with energy constraints, we compared changes in body mass in 14 captive adult storks with the body composition of 12 free-ranging adult storks found dead from accidents. The captive storks, already in an enclosure for several years, were fed ad libitum. They were weighed daily for 1.5,3.5 years using an automatic device. The bodies of the accidentally killed storks were analysed to determine total water, lipid, protein and ash contents, and to assess the biochemical composition of certain organs. Females were on average 20% lighter and 24% smaller than males, but the body mass of the sexes varied in parallel throughout the year. Body mass peaked in December and January (25,30% above minimal body mass), due essentially to large fat stores in subcutaneous and abdominal adipose tissues. Body mass and body lipid rapidly decreased from February to June, whether the storks reared chicks successfully or not, and remained minimal for a few days into July. In contrast to birds using flapping flight, no variation in body protein or pectoral muscle protein was observed while breeding, even though the moult occurred then, nor in August, before the time when wild storks migrate. An endogenous regulation of body fuels is discussed. [source] Molecular regulation of postsynaptic differentiation at the neuromuscular junctionIUBMB LIFE, Issue 11 2005Raghavan Madhavan Abstract The neuromuscular junction (NMJ) is a synapse that develops between a motor neuron and a muscle fiber. A defining feature of NMJ development in vertebrates is the re-distribution of muscle acetylcholine (ACh) receptors (AChRs) following innervation, which generates high-density AChR clusters at the postsynaptic membrane and disperses aneural AChR clusters formed in muscle before innervation. This process in vivo requires MuSK, a muscle-specific receptor tyrosine kinase that triggers AChR re-distribution when activated; rapsyn, a muscle protein that binds and clusters AChRs; agrin, a nerve-secreted heparan-sulfate proteoglycan that activates MuSK; and ACh, a neurotransmitter that stimulates muscle and also disperses aneural AChR clusters. Moreover, in cultured muscle cells, several additional muscle- and nerve-derived molecules induce, mediate or participate in AChR clustering and dispersal. In this review we discuss how regulation of AChR re-distribution by multiple factors ensures aggregation of AChRs exclusively at NMJs. IUBMB Life, 57: 719-730, 2005 [source] Energy reserves during food deprivation and compensatory growth in juvenile roach: the importance of season and temperatureJOURNAL OF FISH BIOLOGY, Issue 1 2005P. L. M. Van Dijk The effect of 21 days of starvation, followed by a period of compensatory growth during refeeding, was studied in juvenile roach Rutilus rutilus during winter and summer, at 4, 20 and 27° C acclimation temperature and at a constant photoperiod (12L : 12D). Although light conditions were the same during summer and winter experiments and fish were acclimated to the same temperatures, there were significant differences in a range of variables between summer and winter. Generally winter fish were better prepared to face starvation than summer fish, especially when acclimated at a realistic cold season water temperature of 4° C. In winter, the cold acclimated fish had a two to three-fold larger relative liver size with an approximately double fractional lipid content, in comparison to summer animals at the same temperature. Their white muscle protein and glycogen concentration, but not their lipid content, were significantly higher. Season, independent of photoperiod or reproductive cycle, was therefore an important factor that determined the physiological status of the animal, and should generally be taken into account when fish are acclimated to different temperature regimes. There were no significant differences between seasons with respect to growth. Juvenile roach showed compensatory growth at all three acclimation temperatures with maximal rates of compensatory growth at 27° C. The replenishment of body energy stores, which were utilized during the starvation period, was responsible for the observed mass gain at 4° C. The contribution of the different energy resources (protein, glycogen and lipid) was dependent on acclimation temperature. In 20 and 27° C acclimated roach, the energetic needs during food deprivation were met by metabolizing white muscle energy stores. While the concentration of white muscle glycogen had decreased after the fasting period, the concentrations of white muscle lipid and protein remained more or less constant. The mobilization of protein and fat was revealed by the reduced size of the muscle after fasting, which was reflected in a decrease in condition factor. At 20° C, liver lipids and glycogen were mobilized, which caused a decrease both in the relative liver size and in the concentration of these substrates. Liver size was also decreased after fasting in the 4° C acclimated fish, but the substrate concentrations remained stable. This experimental group additionally utilized white muscle glycogen during food deprivation. Almost all measured variables were back at the control level within 7 days of refeeding. [source] Effect of Combining Proteolysis and Lactic Acid Bacterial Fermentation on the Characteristics of Minced MackerelJOURNAL OF FOOD SCIENCE, Issue 3 2005Li-Jung Yin ABSTRACT: To improve the quality of fish muscle, mackerel muscle protein was hydrolyzed by proteases from Aspergillus oryzae, and then fermented by lactic acid bacteria (LAB). The highest protease activities were obtained from A. oryzae after 72 h incubation at 25°C. Acidic protease activity was much higher than neutral and alkaline proteases. SDS-PAGE indicated the degradation of muscle proteins after 1 or 2 h hydrolysis by A. oryzae proteases at 50°C. During 48 h fermentation by Pediococcus pentosaceus L and S at 37°C, rapid growth of LAB, decline in pH, and suppression in the growth of microflora, Enterobacteriaceae, Staphylococcus, and Pseudomonas, occurred while increases in whiteness, nonprotein nitrogen, sensory quality, and free amino acids were observed. These data suggested that the acceptability of LAB -fermented mackerel hydrolysates could be substantially improved. [source] Antihypertensive Activities of Peptides Derived from Porcine Skeletal Muscle Myosin in Spontaneously Hypertensive RatsJOURNAL OF FOOD SCIENCE, Issue 1 2002Y. Nakashima ABSTRACT: Antihypertensive activities derived from porcine skeletal muscle proteins were investigated. Thermolysin hydrolysates of porcine muscle water-insoluble proteins demonstrated antihypertensive activities in spontaneously hypertensive rats when administrated in single oral doses. Hydrolysates of porcine myosin and peptides (Met-Asn-Pro-Pro-Lys, Ile-Thr-Thr-Asn-Pro, Met-Asn-Pro, Pro-Pro-Lys) with parts of the sequence of myosin showed antihypertensive activities. This is the first report of antihypertensive activities of peptides derived from muscle proteins of domestic animals. The hydrolysates of porcine muscle protein and their corresponding bioactive peptides might be utilized for physiologically functional foods. [source] Not All Injury-induced Muscle Proteolysis Is Due to Increased Activity of the Ubiquitin/Proteasome System: Evidence for Up-Regulation of Macrophage-associated Lysosomal Proteolysis in a Model of Local TraumaNUTRITION REVIEWS, Issue 1 2003Article first published online: 16 SEP 200 A characteristic response to injury is a dramatic loss of skeletal muscle protein owing to increased muscle protein breakdown. Over the past decade, numerous studies have indicated that up-regulaton of the ubiquitin-proteasome system is a common mechanism underlying such injury-induced muscle proteolysis. However, a recent study using a single-impact trauma to the gastrocnemius muscle found that, although the rate of muscle proteolysis was dramatically increased, the ubiquitin-proteasome system was not involved. Rather, an increase in lysosomal activity, through infiltration of the damaged tissue by mononuclear macrophages, is responsible for the high rates of protein breakdown. [source] Development of a method to assess binding of astaxanthin to Atlantic salmon Salmo salar L. muscle proteinsAQUACULTURE RESEARCH, Issue 4 2005Madhury R Saha Abstract Several methods were examined to characterize the binding between astaxanthin and salmon muscle protein(s) in order to provide tools for evaluation of the role of muscle proteins on astaxanthin retention in Atlantic salmon Salmo salar L. flesh. The methods included gel filtration chromatography, displacement of a hydrophobic probe and ultrafiltration. With gel filtration chromatography, aggregation of astaxanthin under the experimental conditions was a major problem for the separation of bound astaxanthin from free astaxanthin because the apparent molecular weight of aggregated astaxanthin or astaxanthin micelles was in the range of protein,astaxanthin complexes. Displacement of the fluorescent probe 8-anilino-1-naphthalenesulphonate (ANS) was not effective as astaxanthin quenched the fluorophore so that displacement could not be observed. An ultrafiltration method was developed using 200-mM sodium cholate for dispersion of astaxanthin aggregates. This allowed unbound astaxanthin to be separated from bound astaxanthin using a 30-kDa filter. After salmon muscle proteins were solubilized in different fractions by sequential extraction using low ionic strength solutions, the astaxanthin binding of different fractions was assessed using the ultrafiltration method. The significant difference (P<0.05) observed in the astaxanthin binding of the various fractions suggests an application of this assay to detect differences in affinity of proteins for astaxanthin. The results also suggest that proteins other than actomyosin or actin can bind astaxanthin in Atlantic salmon flesh. This method can be used for the identification of astaxanthin-binding proteins in salmon flesh and other tissues. [source] Tropomyosin expression and dynamics in developing avian embryonic musclesCYTOSKELETON, Issue 5 2008Jushuo Wang Abstract The expression of striated muscle proteins occurs early in the developing embryo in the somites and forming heart. A major component of the assembling myofibrils is the actin-binding protein tropomyosin. In vertebrates, there are four genes for tropomyosin (TM), each of which can be alternatively spliced. TPM1 can generate at least 10 different isoforms including the striated muscle-specific TPM1, and TPM1,. We have undertaken a detailed study of the expression of various TM isoforms in 2-day-old (stage HH 10,12; 33 h) heart and somites, the progenitor of future skeletal muscles. Both TPM1, and TPM1, are expressed transiently in embryonic heart while TPM1, is expressed in somites. Both RT-PCR and in situ hybridization data suggest that TPM1, is expressed in embryonic heart whereas TPM1, is expressed in embryonic heart, and also in the branchial arch region of somites, and in the somites. Photobleaching studies of Yellow Fluorescent Protein-TPM1, and -TPM1, expressed in cultured avian cardiomyocytes revealed that the dynamics of the two probes was the same in both premyofibrils and in mature myofibrils. This was in sharp contrast to skeletal muscle cells in which the fluorescent proteins were more dynamic in premyofibrils. We speculate that the differences in the two muscles is due to the appearance of nebulin in the skeletal myocytes premyofibrils transform into mature myofibrils. Cell Motil. Cytoskeleton 2008. © 2008 Wiley-Liss, Inc. [source] Population genetic studies of hilsa shad, Tenualosa ilisha (Hamilton), in Bangladesh waters: evidence for the existence of separate gene poolsFISHERIES MANAGEMENT & ECOLOGY, Issue 5 2000M. Rahman Hilsa shad, Tenualosa ilisha (Hamilton), in Bangladesh is found in inland rivers, estuaries and the marine environment, throughout the year, but the peak catch period is during upstream migration. Tissue (white muscle, liver, brain) samples (total 640 specimens) were collected from three different localities, representing marine, brackish and fresh water, during the monsoon in the summer of the years 1993,1996 to identify genetic markers and study the population structure of this species. The samples were analysed by starch gel electrophoresis and isoelectric focusing, and stained for 15 enzymes and general muscle proteins. Only phosphoglucomutase, aspartate amino transferase, esterase and unidentified muscle proteins were found to be polymorphic. The allele frequencies for the samples collected in the marine environment deviated from corresponding samples from freshwater and estuarine localities, indicating that hilsa shad in Bangladesh waters comprise more than one gene pool. [source] Influence of dietary composition on growth and energy reserves in tench (Tinca tinca)JOURNAL OF APPLIED ICHTHYOLOGY, Issue 1 2001N. De Pedro The effects of different protein, lipid and carbohydrate diets on growth and energy storage in tench, Tinca tinca L., were studied. Over a 2-month period fish were fed four different diets: control, protein-enriched, carbohydrate-enriched and lipid-enriched. The best growth rates were obtained with the control and protein-enriched diets; the carbohydrate diet produced the worst results (lowest specific growth rate, weight gain, nutritional index and hepatosomatic index). These results suggest that it is not advisable to reduce dietary fish protein below 35%, and that it is not possible to obtain a protein-sparing effect of either lipids or carbohydrates, at least in our experimental conditions. The high-protein diet resulted in the storage of energy excess as muscle proteins and hepatic glycogen. Tench fed the high-carbohydrate diet stored carbohydrates as muscle glycogen and reduced plasma triglycerides. Finally, both liver and muscle lipid content were in positive correlation to dietary lipid. [source] ATPASE ACTIVITY, SURFACE HYDROPHOBICITY, SULFHYDRYL CONTENT AND PROTEIN DEGRADATION IN REFRIGERATED SEABASS MUSCLE IN MODIFIED ATMOSPHERE PACKAGINGJOURNAL OF FOOD BIOCHEMISTRY, Issue 1 2004PAYAP MASNIYOM The effect of modified atmosphere packaging (80% CO2, 10% O2, 10% N2) on ATPase activity, surface hydrophobicity, sulfhydryl content and degradation of proteins in seabass muscle during storage at 4C was investigated. No changes in Ca2+ -, Mg2+ -, Mg2+ -Ca2+ -ATPase activities of natural actomyosin (NAM) in seabass slices kept under MAP were observed throughout the storage for up to 21 days (P > 0.05). However, a slightly increased Mg2+ -EGTA-ATPase was found. For seabass slices stored under air atmosphere, Ca2+ -ATPase activity decreased, whereas Mg2+ -EGTA-ATPase activity increased (P < 0.05) with a concomitant loss in Ca2+ -sensitivity. Lower decreases in total sulfhydryl content but higher increases in surface hydrophobicity were observed in samples stored under MAP, compared to those kept under air atmosphere. No marked autolytic degradation in samples kept under MAP was observed throughout the storage as monitored by no changes in myosin heavy chain, free ,-amino acid and trichloroacetic acid soluble peptide. Conversely, a considerable degradation was found in samples kept under air atmosphere, especially after 9 days of storage. Therefore, MAP is a promising means to retard the changes in muscle proteins, especially degradation. [source] CHARACTERISTICS OF MUSCLE FROM TWO SPECIES OF BIGEYE SNAPPER, PRIACANTHUS TAYENUS AND PRIACANTHUS MACRACANTHUSJOURNAL OF FOOD BIOCHEMISTRY, Issue 4 2002SOOTTWAT BENJAKUL ABSTRACT Composition and some properties of muscle from two species of bigeye snapper, P. tayenus and P. macracanthus, were investigated. Both species had a similar composition with the same myofibrillar protein content. However, muscle proteins from P. tayenus had higher thermal stability than those from P. macracanthus, as indicated by the higher enthalpy for transitions as well as the lower inactivation rate constant (KD). Upon 15 days of iced storage, natural actomyosin Ca2* -ATP ase and Mg2+ -Ca2+ -ATPase activities decreased, whereas Mg2+ -EGTA-ATPase activity increased, suggesting the denaturation of myosin, actomyosin and troponin/tropomyosin complexes, respectively. Increased surface hydrophobicity and decreased sulfhydryl groups indicated the denaturation possibly occurred via hydrophobic interaction and disulfide formation. Heading and eviscerating offish retarded the denaturation and physicochemical changes of proteins during iced storage. The results indicated that a rapid and proper post harvest handling was of importance to maintain the muscle quality of bigeye snapper. [source] Effect of Combining Proteolysis and Lactic Acid Bacterial Fermentation on the Characteristics of Minced MackerelJOURNAL OF FOOD SCIENCE, Issue 3 2005Li-Jung Yin ABSTRACT: To improve the quality of fish muscle, mackerel muscle protein was hydrolyzed by proteases from Aspergillus oryzae, and then fermented by lactic acid bacteria (LAB). The highest protease activities were obtained from A. oryzae after 72 h incubation at 25°C. Acidic protease activity was much higher than neutral and alkaline proteases. SDS-PAGE indicated the degradation of muscle proteins after 1 or 2 h hydrolysis by A. oryzae proteases at 50°C. During 48 h fermentation by Pediococcus pentosaceus L and S at 37°C, rapid growth of LAB, decline in pH, and suppression in the growth of microflora, Enterobacteriaceae, Staphylococcus, and Pseudomonas, occurred while increases in whiteness, nonprotein nitrogen, sensory quality, and free amino acids were observed. These data suggested that the acceptability of LAB -fermented mackerel hydrolysates could be substantially improved. [source] Characterization and Functionality of Frozen Muscle Protein in Volador (Illexcoindetii), Pota (Todaropsis eblanae), and Octopus (Eledone cirrhosa)JOURNAL OF FOOD SCIENCE, Issue 7 2003C. Ruiz-Capillas ABSTRACT: Three species of cephalopods: volador (Illex coindetii), pota (Todaropsis eblanae), and octopus (Eledone cirrhosa) were classified according to sex, stage of sexual development, and anatomical zone for characterization and functionality of their muscle proteins. The 3 species exhibited very similar levels of total protein. Octopus mantles and arms contained the least proline and the most hydroxyproline. The highest solubility values in immature pota coincided with the lowest apparent viscosity and emulsifying capacity values. The highest insolubility values observed in octopus coincided with the highest viscosity and emulsifying capacity values. However, in volador which exhibited an intermediate solubility, viscosity was very high and emulsifying capacity was very low. [source] Development of a Monoclonal Antibody for Grouper (Epinephelus marginatus) and Wreck Fish (Polyprion americanus) Authentication Using an Indirect ELISAJOURNAL OF FOOD SCIENCE, Issue 6 2003L. Asensio ABSTRACT: A monoclonal antibody generated against soluble muscle proteins from grouper (Epinephelus marginatus) has been used in 2 indirect ELISA formats (microtiter plates and immunostick tubes) for the rapid authentication of grouper and wreck fish (Polyprion americanus). This monoclonal antibody (1A4-MAb) was tested against native and heat-treated (cooked and sterilized) soluble muscle protein extracts from several commonly marketed fish species and only reacted with grouper and wreck fish samples. [source] Functional and Thermal Gelation Properties of Squid Mantle Proteins Affected by Chilled and Frozen StorageJOURNAL OF FOOD SCIENCE, Issue 6 2003M.C. Gómez-Guillén ABSTRACT: Fresh squid (Loligo vulgaris) mantles that underwent chilled and frozen storage were studied for their ability to form thermal gels as well as the effects of changes to the functional and chemical properties of the muscle proteins during storage. Assays of protein extractability in 5% NaCl, apparent viscosity, autolytic activity, and SDS-PAGE (of the soluble fraction) were carried out periodically. After 4 d of chilled storage, there was a significant drop in protein functionality that negatively affected the thermal gelation profile. The rate of proteolysis remained very high throughout frozen storage, however functional properties and thermal behavior remained very stable. [source] Role of pH and Ionic Strength on Water Relationships in Washed Minced Chicken-breast Muscle GelsJOURNAL OF FOOD SCIENCE, Issue 3 2003H.G. Kristinsson ABSTRACT The relationship between pH, ionic strength, and water balance of chicken-breast muscle gels was investigated. An increase in gel pH (pH 6.4 to 7.4) without added NaCl led to dramatic increases in water-holding capacity and water uptake (P < 0.05). Gels at 150 mM NaCl exhibited less ability to adsorb water than salt-free gels (P < 0.05 at pH 6.8 to 7.4) and had lower water-holding capacities (P < 0.05) and fold scores at and below pH 7. Varying salt concentration of the gel-bathing solutions had dramatic effect on the water uptake of the gels. The results show that strong water-absorbing gels can be produced at low ionic strengths and suggest that the negative charge of the muscle proteins is the driving force for water uptake and retention. [source] Biochemical and Conformation Changes of Actomyosin from Threadfin Bream Stored in IceJOURNAL OF FOOD SCIENCE, Issue 3 2002J. 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] Antihypertensive Activities of Peptides Derived from Porcine Skeletal Muscle Myosin in Spontaneously Hypertensive RatsJOURNAL OF FOOD SCIENCE, Issue 1 2002Y. Nakashima ABSTRACT: Antihypertensive activities derived from porcine skeletal muscle proteins were investigated. Thermolysin hydrolysates of porcine muscle water-insoluble proteins demonstrated antihypertensive activities in spontaneously hypertensive rats when administrated in single oral doses. Hydrolysates of porcine myosin and peptides (Met-Asn-Pro-Pro-Lys, Ile-Thr-Thr-Asn-Pro, Met-Asn-Pro, Pro-Pro-Lys) with parts of the sequence of myosin showed antihypertensive activities. This is the first report of antihypertensive activities of peptides derived from muscle proteins of domestic animals. The hydrolysates of porcine muscle protein and their corresponding bioactive peptides might be utilized for physiologically functional foods. [source] Protein Denaturation and Structural Damage During High-Pressure-Shift Freezing of Porcine and Bovine MuscleJOURNAL OF FOOD SCIENCE, Issue 6 2000F. Fernández-Martín ABSTRACT: Pork and beef muscles were subjected to 200 MPa and ,20 °C with or without water freezing. Both tissues responded to the treatment with similar behavior. Protein denaturation was greater when freezing occurred. Pressure-induced cold denaturation was complete for actin and very considerable for myosin and other muscle proteins. Connective proteins remained practically unaltered by pressurization and/or freezing. Structural changes in the muscle at sarcomere levels caused by pressurization were more severe when freezing occurred. Color, drip loss, and textural properties on the pressurized samples also revealed an additional deleterious influence of freezing. Pressurization alone and pressure-shift freezing resulted unsuitable for muscle preservation. [source] Viscosity and emulsifying capacity in pota and octopus muscle during frozen storageJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 11 2003C Ruiz-Capillas Abstract The functional quality of pota and octopus muscle during frozen storage for up to 12 months was evaluated periodically by determining viscosity and emulsifying capacity levels. In both species the effect on different anatomical locations (mantle and arms) in mature and young male and female individuals was studied. Apparent viscosity and emulsifying capacity levels were greater in octopus than in pota. While in pota a sharp decrease was observed in viscosity levels, falling to virtually nil, viscosity levels in octopus increased in the first 2 months and only slight decreases were observed at the end of storage. The change in emulsifying capacity, however, was quite similar in the two species, with not very sharp decreases. According to these results, emulsifying capacity measurement could be a suitable technique for showing the changes that occur in the muscle proteins of these species when they are stored frozen. No differences were observed by sex, but there were differences depending on the stage of maturity and anatomical location. Thus pota and octopus mantles present greater stability in frozen storage than the arms, and there is a tendency, although not always significant, that the mantles of young pota and octopus specimens are more stable in frozen storage than the mantles of adult individuals. Copyright © 2003 Society of Chemical Industry [source] Effect of lipid oxidation and frozen storage on muscle proteins of Atlantic mackerel (Scomber scombrus)JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 5 2002Suhur Saeed Abstract The effect of storage on the lipids and proteins in Atlantic mackerel stored for up to 24 months at ,20 and ,30,°C was studied. Traditional methods including the peroxide value, thiobarbituric acid-reactive substances (TBARS) and a reverse phase HPLC method were used to determine the primary and secondary lipid oxidation products. All tests showed an increase in lipid oxidation products with storage time and at a higher storage temperature of ,20,°C compared with samples stored at ,30,°C. Antioxidants had a significant effect (P,<,0.01) on the inhibition of lipid oxidation, as shown by the reduction in peroxide value and hydroxides, and malondialdehyde formation. Similarly, deterioration of protein structure and functionality in mackerel stored for 3, 6, 12 and 24 months was greater at ,20 than ,30,°C. ATPase activity in the myosin extract of Atlantic mackerel showed a significant decrease (P,<,0.01) with progressive frozen storage. Protein solubility in high salt concentration (0.6,M NaCl) decreased (P,<,0.01) during storage at both ,20 and ,30,°C but was greater at ,20,°C. Interestingly, antioxidants BHT, vitamin C and vitamin E protected the proteins against complete loss of ATPase activity and protein solubility to a significant level (P,<,0.01) for up to 1 year at ,20,°C compared with samples stored without antioxidants. This study confirms the deleterious effect of lipid oxidation products on protein structure and function in frozen fatty fish. © 2002 Society of Chemical Industry [source] | |||||||||||||||||||