1996
DOI: 10.2331/fishsci.62.73
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Effect of Cryoprotectants and a Reducing Reagent on the Stability of Actomyosin during Ice Storage

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Cited by 36 publications
(21 citation statements)
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“…34 SH a , another SH group, which is localised in the light meromyosin region of the myosin molecule, was reported to be involved in the oxidation of MHC and its dimer formation, leading to an increase in Mg 2 -EGTA activity. 17 Benjakul et al 14 reported an increase in Mg 2 -EGTA activity with a decrease in total SH content in Paci®c whiting actomyosin during iced storage. Oxidation of sulphhydryl groups of myosin has been considered to reduce Ca 2 sensitivity.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…34 SH a , another SH group, which is localised in the light meromyosin region of the myosin molecule, was reported to be involved in the oxidation of MHC and its dimer formation, leading to an increase in Mg 2 -EGTA activity. 17 Benjakul et al 14 reported an increase in Mg 2 -EGTA activity with a decrease in total SH content in Paci®c whiting actomyosin during iced storage. Oxidation of sulphhydryl groups of myosin has been considered to reduce Ca 2 sensitivity.…”
Section: Discussionmentioning
confidence: 99%
“…Total and surface SH contents were determined using 5,5'-dithio-bis(2-nitrobenzoic acid) (DTNB) according to the method of Ellman 16 as modi®ed by Sompongse et al 17 To 1.0 ml of actomyosin solution (0.4%), 9 ml of 0.2 M Tris-HCl buffer, pH 6.8, containing 8 M urea, 2% SDS and 10 mM EDTA, was added. To 4 ml of the mixture, 0.4 ml of 0.1% DTNB was added and incubated at 40°C for 25 min.…”
Section: Total and Surface Sh Determinationmentioning
confidence: 99%
“…Enzymatic proteolysis of fish meat during post mortem storage cause disruption of the structure of the myofibrillar proteins (Jasra et al, 2001;Verrez-Bagnis et al, 1999) and is thought to cause post-mortem softening, which is one of the most important quality attributes of fish muscle during cold storage. ( Munasinghe et al, 2005;Bonnal et al, 2001;VerrezBagnis et al, 2001;Sompongse et al, 1996). These studies show that the rate of proteolysis varies among species (Papa et al, 1996;.…”
Section: Protein Denaturationmentioning
confidence: 97%
“…The effect of different YAP additions on the content of salt-soluble myofibrillar protein in GCF during the storage time is shown in Figure 1( (Yongsawatdigul & Park, 2003). The formation of disulfide bonds caused by oxidation of sulfhydryl groups during storage may lower the dissolution amount as well (Sompongse, Itoh, & Obatake, 1996). Besides, myofibrillar protein may be hydrolyzed by endogenous protease or microbial metabolism (Matsukura, Okitani, Nishimuro, & Kato, 1981).…”
Section: Effect Of Yap On Content Of Salt-soluble Myofibrillar Proteinmentioning
confidence: 99%