Degradation of myofibrils in cultured yellowtail Seriola quinqueradiata burnt meat: effects of a myofibril-bound EDTA-sensitive protease

Liang, Xiao; Yoshida, Asami; Osatomi, Kiyoshi; Wang, Yajun; Cao, Min‐Jie; Hara, Kenji

doi:10.1007/s12562-011-0429-5

Cited by 7 publications

(4 citation statements)

References 38 publications

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“…HTST treatment compared to LTLT. The former (33 kDa) band was consistent with the expected size of tropomyosin (Daifuku et al, 2011), and the latter two bands (between 180 and 245 kDa and approximately 48 kDa) were tentatively identified as myosin and actin, respectively, based on their size (Liang et al, 2012).…”

Section: Fisheries and Aquatic Sciencessupporting

confidence: 54%

Effects of different heating conditions on protein composition in each muscle type of yellowtail (Seriola quinqueradiata)

Furuta¹,

Hamakawa²,

Ishibashi³

et al. 2022

Fish Aquat Sci

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To clarify the factors influencing the physical properties of fish after heat treatments, we investigated changes in the properties of proteins in the dorsal ordinary and dark muscle of yellowtail (Seriola quinqueradiata) heated under different conditions commonly used for the purposes of food hygiene. High-temperature/short-time heating (85℃ for 90 s and 75℃ for 60 s) affected the protein solubility more than low-temperature/long-time heating (63℃ for 30 min). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and differential scanning calorimetry showed that low-temperature/long-time heating reduced the degree of actin denaturation in fish compared with that by other heating conditions. In addition, collagen solubility was enhanced with low-temperature/long-time heating. Therefore, these results suggest that differences in the degree of actin and collagen denaturation are responsible for the enhanced meat tenderness and diminished meat shrinkage, resulting from low-temperature/ long-time heating.

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Section: Fisheries and Aquatic Sciencessupporting

confidence: 54%

Effects of different heating conditions on protein composition in each muscle type of yellowtail (Seriola quinqueradiata)

Furuta¹,

Hamakawa²,

Ishibashi³

et al. 2022

Fish Aquat Sci

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“…5−7 In our previous study, insoluble metalloproteinases responsible for the modori phenomenon were found in horse mackerel (Trachurus japonicus), 8 and a myofibril-bound EDTA-sensitive protease (MBESP), which causes the degradation of MHC, was identified in yellowtail muscle. 9 Under certain conditions, endogenous protease inhibitors (EPIs) in the soluble fraction inhibiting the modori phenomenon by suppressing target-oriented proteinases (such as sarcoplasmic proteins) in some fish meats showed the ability to inhibit serine-and cysteine-type proteases in walleye pollock surimi. 10,11 Moreover, the myofibril-bound serine proteinase inhibitor (MBSPI) purified from the skeletal muscle of lizard fish (Saurida wanieso) showed specific inhibition toward the MBSP.…”

Section: Introductionmentioning

confidence: 99%

“…After the washing process, protease activity still remains in the myofibrillar fraction of some fish species, and myofibril-bound serine proteinase (MBSP) found in carp, lizard fish, and white croaker is reportedly an insoluble MIP. − In our previous study, insoluble metalloproteinases responsible for the modori phenomenon were found in horse mackerel (Trachurus japonicus), and a myofibril-bound EDTA-sensitive protease (MBESP), which causes the degradation of MHC, was identified in yellowtail muscle …”

Section: Introductionmentioning

confidence: 99%

Identification of a Tissue Inhibitor of Metalloproteinase-2: An Endogenous Inhibitor of Modori-Inducing Insoluble Metalloproteinase from Yellowtail Seriola quinqueradiata Muscle

Jiang

Yoshida

Sun

et al. 2023

J. Agric. Food Chem.

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The existence of an endogenous protease inhibitor (EPI) was expected from the comparison of the gel properties between washed and nonwashed yellowtail surimi gels. A possible candidate, tissue inhibitor of metalloproteinase-2 (TIMP-2), was partially purified from the soluble fraction of yellowtail muscle, and an 18 kDa protein band was detected by sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions and western blot analysis. Its N-terminal amino acid sequence was determined as XSXSPAHPQQAF, with high homology to TIMP-2 from other fish species, suggesting that it was identified as yellowtail TIMP-2. Subsequently, full-length cDNA of two isoforms (TIMP-2a and TIMP-2b) was successfully cloned from yellowtail muscle. The N-terminal sequence of purified TIMP-2 completely corresponded to TIMP-2b. When the surimi gel quality decreased after spawning, the mRNA expression of TIMP-2b also decreased. Human TIMP-2 could inhibit autolysis of myofibrillar proteins from yellowtail muscle. Thus, TIMP-2b was considered the major EPI of the modori-inducing insoluble metalloproteinase in yellowtail muscle.

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“…Because of its fast natural growth rate, high nutritional quality, and delicious flavour and taste, it is regarded as a high value fish, and hence is cultivated in large quantities in the coastal areas of northern China (Wang et al ., 2005; Liu et al ., 2019; Shi et al ., 2019). Due to its commercial importance, in recent years researches on yellowtails have been on the rise (Mabuchi et al ., 2019; Furuta et al ., 2020; Tanimoto et al ., 2020), with focuses on its aquaculture (Sotoyama et al ., 2018), oil (Kim et al ., 2019), proteolysis of Myofibril (Xiao et al ., 2012), refrigeration storage stability of muscle (Tanimoto et al ., 2015), and fillet colour preservation frozen storage and post thawing (Hiraoka et al ., 2004). Yellowtail kingfish is mostly consumed uncooked as sashimi and sushi.…”

Section: Introductionmentioning

confidence: 99%

Characteristic stable structure of the myosin rod in dark muscle of yellowtail kingfish (Seriola aureovittata)

Liu

Wang

Huang

et al. 2022

Int J of Food Sci Tech

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Summary The dark muscle of yellowtail kingfish is regularly consumed as fresh sashimi alongside with the ordinary muscle. Thus, in this study, three types of ATPase activities, chymotryptic digestion patterns as well as thermal unfolding of various myosin domains were determined to reveal the denaturation characterisation of myosin in dark muscle and compare it with normal muscle. The thermal inactivation rate of dark muscle myosin Ca2+‐ATPase at 30°C (7.3 × 10−4, sec−1) was significantly (P < 0.05) greater than that of ordinary muscle (5.9 × 10−4, sec−1), while dark muscle myosin became more stable than ordinary muscle one once bound with F‐actin. On the other hand, the rod region especially light meromyosin region of the dark muscle myosin was much more stable than ordinary myosin. These results characterised that myosin in the dark muscle of yellowtail kingfish is constituted with less stable head and more stable rod regions than those in the ordinary muscle.

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Degradation of myofibrils in cultured yellowtail Seriola quinqueradiata burnt meat: effects of a myofibril-bound EDTA-sensitive protease

Cited by 7 publications

References 38 publications

Effects of different heating conditions on protein composition in each muscle type of yellowtail (Seriola quinqueradiata)

Effects of different heating conditions on protein composition in each muscle type of yellowtail (Seriola quinqueradiata)

Identification of a Tissue Inhibitor of Metalloproteinase-2: An Endogenous Inhibitor of Modori-Inducing Insoluble Metalloproteinase from Yellowtail Seriola quinqueradiata Muscle

Characteristic stable structure of the myosin rod in dark muscle of yellowtail kingfish (Seriola aureovittata)

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