Gelation of Proteins from Washed Muscle of Threadfin Bream (<i>Nemipterus japonicus</i>) under Mild Acidic Conditions

Chawla, S.P.; Venugopal, V.; Nair, P.M.

doi:10.1111/j.1365-2621.1996.tb14194.x

Cited by 65 publications

(55 citation statements)

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“…The final color of the surimi is due to the loss of lipids, blood, carotenoids and other pigments during the washings of the muscle (Chawla et al, 1996). Thus, Table 3 shows that both kinds of washings were equally efficient (p > 0.05) for the removal of colored substances, undesirable for the final color of the product.…”

Section: Color Analysismentioning

confidence: 99%

Washings and cryoprotectants for the production of Tilapia Surimi

et al. 2017

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This research aimed at studying the effects of different washing conditions (distilled water x distilled water + NaHCD 3 + NaCl) and cryoprotectants (NaCl + saccharose x sorbitol + sodium tripolyphosphate) for the production of tilapia surimi. The experiment used a factorial design 2 x 2 and the variables analyzed were proximate composition, non-nitrogen protein (NNP) removal, texture, color and yield. The protein and moisture contents of the surimi were influenced neither by washings nor by cryoprotectants, while the ash content was higher when NaCl + saccharose were used as the cryoprotectants and the yield was higher when only distilled water was used for the washings. Combining distilled water for the washings and NaCl + saccharose as the cryoprotectants provided the highest lipid and NNP removals. The different treatments produced surimi gels with similar colors and texture.

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Section: Color Analysismentioning

confidence: 99%

Washings and cryoprotectants for the production of Tilapia Surimi

et al. 2017

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“…The solubility of protein was determined according to the method of Roussel and Cheftel 7 as described by Chawla et al 8 Samples (1 g) were solubilised in 20 ml of various solvents: 0.6 mol kg À1 KCl (S1); 20 mmol kg À1 Tris-HCl buffer, pH 8.0 (S2); S2 containing 1% (w/v) SDS (S3); S2 containing 1% (w/v) SDS and 8 mol kg À1 urea (S4); S2 containing 1% (w/v) SDS, 8 mol kg À1 urea and 2% (v/v) b-mercaptoethanol (S5). Solubilised protein was precipitated using 50% (w/v) trichloroacetic acid.…”

Section: Solubility Studymentioning

confidence: 99%

Physicochemical and textural properties of dried squid as affected by alkaline treatments

Benjakul

Visessanguan

Tanaka

et al. 2000

J. Sci. Food Agric.

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“…Although most of muscle protein gels are formed using heat treatment, gelation of myofibrillar proteins can occur at lower pH values without heating (Chawla et al, 1996;Ngapo et al, 1996;Riebroya et al, 2009;Saunders, 1994; Minced muscle was homogenized in 5 volumes (w/v) of 20 mmol/L Tris-HCl buffer (pH 7.5) containing 0.1 mol/L KCl. The homogenate was centrifuged at 10000g for 10 min (4 ℃) in a centrifuge (Sigma Laborzentrifugen, Model 4K15, Osterode, Germany), and the precipitate was washed twice by suspending them in 5 volumes of the same isolation buffer following the same process as above.…”

Section: Introductionmentioning

confidence: 99%

“…Gelation is an important functional property of myofibrillar proteins, which is mainly responsible for the textural properties of surimibased products. Gel formation involves partial denaturation of protein followed by irreversible aggregation which results in a three dimensional network (Chawla et al, 1996;Sun et al, 2011;Venugopal et al, 1994). The gel formation of proteins is influenced by several factors, such as type of muscle, protein concentration, pH, ionic strength, temperature, and pressure (Sun et al, 2011;Totosaus et al, 2002).…”

mentioning

confidence: 99%

“…Electrophoresis was performed at a constant voltage of 110 V. After electrophoresis was completed, gels Venugopal et al, 1994;Venugopal et al, 2002;Xu et al, 2011;Xu et al, 2012). Acid-induced gelation was traditionally used to make fish meat gel products, which provided products less susceptible to microbial spoilage and improved storage stability (Chawla et al, 1996;Techaratanakrai et al, 2011). In addition, acid-induced gelation was important for textural development of fermented fish mince, which was widely consumed in parts of Southeast Asia (Riebroy et al, 2007; Riebroya et al, 2009;Xu et al, 2010).…”

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confidence: 99%

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Acid-induced Gel Formation of Silver Carp (Hypophthalmichthys molitrix) Myofibrils as Affected by Salt Concentration

Jiang

Xia

2013

FSTR

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The influence of salt concentration on acid-induced gel formation and gel properties of silver carp myofibrils was investigated. Results showed that silver carp myofibrils were slightly soluble regardless of salt concentration in the presence of D-gluconic acid-δ-lactone (GDL). The increase of myofibrils solubility in the absence of GDL was mainly caused by the dissociation of myosin and actin, as evidenced by SDS-PAGE. Myosin and actin were the major protein components involved in acid-induced aggregation of silver carp myofibrils. Ca 2+ -ATPase activity and surface reactive sulphydryl (SH) contents of myofibrils with GDL addition were much lower than those in the absence of GDL. Significant decrease in total SH content of silver carp myofibrils in the present of GDL at salt concentration of 0.3 mol/L NaCl was observed, suggesting the contribution of disulphide bonds to the acid-induced gel formation. The gel properties of acidinduced silver carp myofibril gel were highly dependent upon salt concentration, and acidified myofibril gel with high gel strength could be obtained with addition of 1.7% − 2% NaCl.Keywords: silver carp, myofibrils, acid-induced gelation, salt concentration, influence *To whom correspondence should be addressed. E-mail: xuys@jiangnan.edu.cn (Y. Xu), xiaws@jiangnan.edu.cn (W. Xia) IntroductionMyofibrillar proteins (MP), accounting for about 55% to 60% of the total muscle protein, are generally referred as salt soluble protein (Sun and Holley, 2011). Gelation is an important functional property of myofibrillar proteins, which is mainly responsible for the textural properties of surimibased products. Gel formation involves partial denaturation of protein followed by irreversible aggregation which results in a three dimensional network (Chawla et al., 1996;Sun et al., 2011;Venugopal et al., 1994). The gel formation of proteins is influenced by several factors, such as type of muscle, protein concentration, pH, ionic strength, temperature, and pressure (Sun et al., 2011;Totosaus et al., 2002). Among these factors, pH and ionic strength are two important factors that can affect the dissociation state and charge distribution of protein amino acid residues in the solution and can alter the protein intermolecular electrostatic interactions, and thus affect the protein molecular structure and gel properties (Lin and Park, 1998). The nature and extent of gelation is highly pH-and salt-sensitive due to the importance of electrostatic interactions of myofibrils (Kristinsson and Hultin, 2003a).It is well known that salt concentration is one of the key factors in determining the gel formation of muscle protein and the physical properties of the gel. Increasing ionic strength was reported to decrease the electrostatic repulsive forces partially via charge screening at a given pH (Kristinsson and Hultin, 2003b). Sodium chloride is the salt commonly used in restructured meat products. High concentration (2% to 3%) of sodium chloride is usually added to fish mince to solubilize the myofibrillar proteins in...

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Gelation of Proteins from Washed Muscle of Threadfin Bream (Nemipterus japonicus) under Mild Acidic Conditions

Cited by 65 publications

References 23 publications

Washings and cryoprotectants for the production of Tilapia Surimi

Washings and cryoprotectants for the production of Tilapia Surimi

Physicochemical and textural properties of dried squid as affected by alkaline treatments

Acid-induced Gel Formation of Silver Carp (Hypophthalmichthys molitrix) Myofibrils as Affected by Salt Concentration

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