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

Benjakul, Soottawat; Visessanguan, Wonnop; Ishizaki, Shoichiro; Tanaka, Munehiko

doi:10.1111/j.1365-2621.2001.tb15207.x

Cited by 143 publications

(94 citation statements)

References 33 publications

(10 reference statements)

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“…2. Myofibril contains myosin and actin as major proteins which are naturally associated with troponin and tropomyosin (Benjakul et al 2001). Electrophoretic profile of myofibrils reveal that bands of major polypeptides like myosin heavy chain (*200 kD), alpha-actinin (around 97.4 kD), actin (*42-44 kD), tropomyosin (*36 kD) were intact and no fragmentation was observed.…”

Section: Electrophoresismentioning

confidence: 99%

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Effect of ultrasonication on secondary structure and heat induced gelation of chicken myofibrils

Saleem

Ahmad

2016

J Food Sci Technol

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Ultrasonication has been suggested as a new promising technique to improve the quality of meat and other meat products. In this study ultrasonication at low frequency (20 kHz) was carried out to investigate the effect on structural and biochemical properties of myofibril proteins. The possible implications between ultrasonicationinduced structural changes and gelation properties were also investigated. Structural changes were investigated by ATPase activity, SDS-PAGE, circular dichroism and fluorescence spectroscopy. Microstructural changes in heat induced gels were observed by SEM and water holding capacity was determined by centrifugation. Ultrasonic treatment for 30 min significantly reduced the Ca 2? -ATPase activity. Moreover significant change in structure of proteins at secondary level, as indicated by marked decrease in a-helicity, was observed. Marginal change in fluorescence at 10 min was followed by significant increase at 20 and 30 min reflecting exposure of hydrophobic residues on surface during unfolding. Microstructural analyses of gels showed marked improvement in regular three dimensional network at 20 and 30 min of sonication. WHC at 20 min and 30 min were significantly higher than control. Our results suggest that ultrasonication at low frequency (20 kHz) can prove beneficial for improving functional properties of meat and meat products.

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Section: Electrophoresismentioning

confidence: 99%

“…Structural changes under ultrasonication, as indicated by CD spectra and hydrophobicity profile, leads to increased exposure of hydrophobic residues. The exposure of hydrophobic residues and their mutual interactions have been suggested to determine properties of the protein gels (Chan et al 1992;Benjakul et al 2001). …”

Section: Water Holding Capacity (Whc)mentioning

confidence: 99%

Effect of ultrasonication on secondary structure and heat induced gelation of chicken myofibrils

Saleem

Ahmad

2016

J Food Sci Technol

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“…Improvement of surimi gel quality (gel strength) has been one of the major thrusts in surimi gel products. Gel forming ability of surimi depends on both intrinsic and extrinsic factors, including species (Lee 1984), physic and chemical properties of muscle proteins (Benjakul et al 2001), the presence of endogenous enzymes, e.g. proteinases and transglutaminase , and the conditions used in processing (Benjakul et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology

2013

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Surimi is a semi-processed washed fish mince protein concentrate mixed with cryoprotectants for frozen storage, which is the primary constituent of processed foods. Mechanically separated chicken meat (MSCM) is a common ingredient of comminuted sausages mainly due to its low price. The present work aimed to define the adequate parameters to obtain surimi-like material from MSCM using response surface methodology, and to characterize the chemical and textural properties of this product. The MSCM was utilized in the elaboration of surimi-like material using the bleaching method with sodium bicarbonate and sodium chloride solutions. For this purpose, the effect of process parameters viz: temperature (T=2, 7, and 12°C), time (t=5, 10, and 15 min/cycles) and washing solution:MSCM ratio (R=2:1, 4:1, and 6:1w/w) were evaluated using response surface methodology. The highest composite design averages obtained were 10.7 % for protein content, 1,003.4 g for breaking force, 645.8 g.cm for gel strength, 9.0 N for cutting strength, and 24.1 N.s for work of shearing at the optimum combination of processing conditions of 7°C, 10 min and 4:1 washing solution:MSCM ratio, corresponding to the central points of the proposed experimental design. The obtained models had high determination coefficients, explaining 95.85, 98.23, 98.41, and 96.08 % of total variability in protein content, cutting strength, breaking force, and work of shearing variabilities, respectively. According to the folding test the surimi-like material presented the same characteristics of a high quality surimi (FT=5).

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“…(Xiong, 2000;Reznick et al, 1992) The ice crystals that are formed pull water from the intracellular spaces into the intercellular spaces, leading to excessive moisture loss during thawing, which influences the sensory profile and the tenderness of meat (Ngapo et al, 1999). Multiple freeze-thaw cycles increase the loss of muscle moisture, as the damage to the ultrastructure of the meat fibers does not allow uptake of moisture into the intracellular spaces, leading to thawing loss, while freezing deteriorates meat quality due to osmotic removal of water, mechanical damage due to ice crystal formation, and lipid and protein oxidation (Benjakul et al, 2001;Xiong, 2000), thawing cause meat discoloration, thawing and cooking loss, and lipid oxidation (Xia et al, 2009). However, the main threat to the quality of frozen meat is the decrease of waterholding capacity (WHC), which is manifested as a loss of exudate (drip) upon thawing.…”

Section: Introductionmentioning

confidence: 99%

Effec t of Freeze-Thaw Cycles on Lipid Oxidation and Myowater in Broiler Chickens

Ali

Rajput

et al. 2016

Rev. Bras. Cienc. Avic.

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The present study was carried out to investigate the influence of freezing-thawing cycles (0, 2, 4 and 6) on lipid oxidation and myowater contents and distribution. Nine replicates of chicken breast meat samples were used for each cycle. Lipid oxidation was determined by measuring peroxide value, and malondialdehyde (MDA) concentrations, which reflect thiobarbituric acid reactive substance (TBARS). Color was determined with a digital colorimeter. Muscle moisture contents were determined by drip loss and thawing loss, water holding capacity, and nuclear magnetic resonance (NMR). The results showed that, as the number of freeze-thaw cycles increased, meat redness decreased and MDA and peroxide values increased. Drip loss and thawing loss tended to decreasing as the number of freeze-thaw cycles increased. Water holding capacity also decreased as a function of increasing freeze-thaw cycles. NMR relaxometry profile showed freeze-thaw cycles change the water distribution of meat subjected to multiple freeze-thaw cycles. In conclusion, multiple freezing and thawing rate (6 cycles) increased lipid oxidation, decreased myowater, and impaired the color of chicken meat.

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

Cited by 143 publications

References 33 publications

Effect of ultrasonication on secondary structure and heat induced gelation of chicken myofibrils

Effect of ultrasonication on secondary structure and heat induced gelation of chicken myofibrils

Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology

Effec t of Freeze-Thaw Cycles on Lipid Oxidation and Myowater in Broiler Chickens

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