Contribution of SS Bonds to the Elasticity of Actomyosin Gel in which Coexisting Transglutaminase was inactivated

Niwa, Eiji; Inuzuka, Kumiko; Nowsad, Alam Akm; Liu, Dajia; Kanoh, Satoshi

doi:10.2331/fishsci.61.438

Cited by 4 publications

(4 citation statements)

References 11 publications

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“…However, Niwa et al reported that suwari was observed during the setting of meat paste even under conditions when TGase activity was inhibited and when the oxidation of sulfhydryl groups occurred 22,23 . In the present experiment, set gels heated at 35°C or 40°C were not heated again at 80°C or 90°C to cook.…”

Section: Resultsmentioning

confidence: 53%

Inhibiting effect of polymerization and degradation of myosin heavy chain during preheating at 30oC and 50oC on the gel-forming ability of walleye pollack surimi

et al. 2001

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To confirm the contribution of polymerization and degradation of myosin heavy chain (MHC) during preheating to the gel‐forming ability of fish meat paste, walleye pollack surimi paste was preheated at 30°C and 50°C prior to heating at 80°C in the presence of various inhibitors. At 30°C, ethyleneglycol bis(2‐aminoethyl ether)‐N,N,N′,N′‐tetraacetic acid (EGTA) and ethylenediaminetetraacitic acid (EDTA) inhibited gel formation as well as the polymerization of MHC, whereas dithiothreitol (DTT) and leupeptin promoted gel formation, which was accompanied by the enhancement of MHC polymerization and decreased MHC degradation, respectively. At 50°C, leupeptin inhibited MHC degradation and improved gel strength, whereas EGTA, EDTA and DTT had no effect on MHC polymerization and degradation and did not affect gel formation. The results demonstrate that the gel strength of cooked gel (80°C) is not affected by preheating at 30°C and 50°C and does not inhibit polymerization and degradation. Results suggest that the gel strength of cooked gel is dependent on the polymerization and degradation of MHC during preheating.

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Section: Resultsmentioning

confidence: 53%

Inhibiting effect of polymerization and degradation of myosin heavy chain during preheating at 30oC and 50oC on the gel-forming ability of walleye pollack surimi

et al. 2001

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“…Other studies indicate that the sulfhydryl group content of walleye pollack surimi remains constant during incubation at 38°C, 11 and that intermolecular disulfide bonding is thought to be indispensable to the setting appearance of some species of fish meat 12 . Furthermore, it was reported that SH‐blocked actomyosin gel was weaker in gel strength than SH‐unblocked actomyosin gel at 40°C under conditions of no TGase activity 13 …”

Section: Introductionmentioning

confidence: 99%

“…12 Furthermore, it was reported that SHblocked actomyosin gel was weaker in gel strength than SH-unblocked actomyosin gel at 40∞C under conditions of no TGase activity. 13 However, it is not clear whether the increase in the gel strength of the final cooked gel that has undergone prolonged preheating is related to the formation of disulfide bonds through the oxidation of sulfhydryl groups other than cross-linking by TGase.…”

Section: Introductionmentioning

confidence: 99%

Contribution of the polymerization of protein by disulfide bonding to increased gel strength of walleye pollack surimi gel with preheating time

et al. 2001

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ABSTRACT:To clarify the contribution of polymerization of myosin heavy chain (MHC) by disulfide bonding to increased gel strength of cooked gel via preheating, the pastes of walleye pollack surimi (SS and C grades) were preheated at 25∞C and 40∞C for a variety of hours prior to heating at 80∞C for 20 min. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) patterns of cooked gels were analyzed with and without reducing the samples, which were solubilized in 8 M urea-2% SDS solution. The formation of polymers by disulfide bonding in cooked gels was almost constant in each of the SS and C grade surimi gels despite the period of preheating. Therefore, it was suggested that polymerization by disulfide bonding occurred during cooking at 80∞C and not during preheating.KEY WORDS: disulfide bond, gel formation, myosin heavy chain, suwari, walleye pollack surimi.

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“…Total free sulfhydryl groups (SH) content was determined by reacting with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) [23][24]. Meat samples were thawed, minced and dissolved in 20.0 mL urea-SDS solution (8.0 M urea, 3% SDS, 0.1 M phosphate, pH 7.4) by shaking at room temperature for 8 h. Then 1 mL of the protein solution was incubated with 0.3 mL DTNB reagent (10 mM DTNB in 0.1 M phosphate buffer, pH 7.4) at room temperature for 15 min.…”

Section: Sulfhydryl Group Contentmentioning

confidence: 99%

Carbonyl and sulfhydryl groups of chicken meat proteins after dietary modulation with selenium

2015

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Abstract:The objective of the study was to investigate the effects of selenium modulation on the alteration of carbonyl and sulfhydryl groups in proteins in chicken breast and leg meat. Selenium, in the form of sodium selenite and selenized yeast, was applied to broiler chicken at 0.26, 0.38 and 0.50 mg Se kg -1 . The alteration of protein carbonyl and sulfhydryl groups, as well as total antioxidative potential of breast and leg meat were analyzed in fresh, chilled and frozen material. Protein reactive groups were effectively protected against oxidatively induced changes (carbonyl groups formation) by dietary selenium supplementation, during frozen storage of both types of chicken muscles, either with white fibre domination (breast) or with red fibre domination (leg). The inorganic form of selenium was effective in decreasing the loss of protein sulfhydryl groups in muscles with red fibre domination during frozen storage. In conclusion, selenium compounds can be used in broiler nutrition as a protein antioxidizing agent, especially in perspective of the long storage of meat under freezing conditions.

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Contribution of SS Bonds to the Elasticity of Actomyosin Gel in which Coexisting Transglutaminase was inactivated

Cited by 4 publications

References 11 publications

Inhibiting effect of polymerization and degradation of myosin heavy chain during preheating at 30oC and 50oC on the gel-forming ability of walleye pollack surimi

Inhibiting effect of polymerization and degradation of myosin heavy chain during preheating at 30oC and 50oC on the gel-forming ability of walleye pollack surimi

Contribution of the polymerization of protein by disulfide bonding to increased gel strength of walleye pollack surimi gel with preheating time

Carbonyl and sulfhydryl groups of chicken meat proteins after dietary modulation with selenium

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