Quality improvement of the thermal gel of horse mackerel by sodium citrate and its inhibition of the insoluble metalloproteinase

Jiang, Yan-Rong; Yoshida, Asami; Ohta, Megumi; Gao, Yi-Li; Noguchi, Erika; Kuwahara, Koichi; Hara, Kenji; Osatomi, Kiyoshi

doi:10.1007/s12562-022-01651-9

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“…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%

“…2−4 After the washing process, protease activity still remains in the myofibrillar fraction of some fish species, and myofibrilbound serine proteinase (MBSP) found in carp, lizard fish, and white croaker is reportedly an insoluble MIP. 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.…”

Section: Introductionmentioning

confidence: 99%

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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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