Change in myofibrillar protein of the salted meat paste from Alaska pollack and tilapia during the setting.

Katoh, Noboru; Hashimoto, Akihiko; Nozaki, Hisashi; Matsumoto, Tsutomu; Arai, Ken‐ichi

doi:10.2331/suisan.52.875

Cited by 2 publications

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“…This phenomenon is referred to as "suwari" or "setting" and can modify the texture of surimi-based products (Okada 1959;Shimizu et al 1981;Lanier 1986;Chan et al 1995). During the suwari process, formation of an insoluble aggregate and coincidental decrease of myosin heavy chain have been observed (Numakura et al 1985(Numakura et al , 1990Katoh et al 1986;Seki et al 1990Kamath et al 1992;Tsukamasa et al 1993;Chan et al 1995). In addition, significant activity of a Ca*+-dependent transglutaminase, which can catalyze formation of an &-(y-glutamy1)lysine isopeptide bond between lysyl and glutamyl residues on proteins have been detected in several fish muscles (Kimura et Kishi et al 1991; Kamath et al 1992; Sat0 et al.…”

Section: Introductionmentioning

confidence: 99%

Different Arrangement of ?-(?-Glutamyl)lysine Cross-Linking in Alaska Pollock (Theragra Chalcogramma) Surimi Proteins by Streptoverticillium and Endogenous Transglutaminases During Suwari Process

Satô

Tanaka

Kotaru

et al. 2001

J Food Biochemistry

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The objective of the present study is to compare the protein cross‐linking reaction in Alaska pollock surimi that is catalyzed by a commercially available microbial transglutaminase and by endogenous Alaska pollock transglutaminase. The endogenous transglutaminase was inhibited by EGTA and activated by CaCl2 The microbial transglutaminase was added to the salted surimi with and without EGTA and CaCl2. These surimi pastes were incubated at 25C up to 24 h followed by cooking at 90C. The resultant gels were fractionated into soluble and insoluble (aggregate) fractions by SDS‐urea extraction. Compositional analysis revealed that the aggregate consisted predominantly of cross‐linked myosin heavy chain. The distribution of ɛ‐(γ‐glutamyl)lysine isopeptide in the soluble and aggregate fractions andpeptide mapping analyses of the aggregate fraction demonstrate that the formation of isopeptide cross‐links in Alaska pollock surimi proteins during suwari process differs when catalyzed by the microbial transglutaminase and endogenous transglutaminase.

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Section: Introductionmentioning

confidence: 99%

Different Arrangement of ?-(?-Glutamyl)lysine Cross-Linking in Alaska Pollock (Theragra Chalcogramma) Surimi Proteins by Streptoverticillium and Endogenous Transglutaminases During Suwari Process

Satô

Tanaka

Kotaru

et al. 2001

J Food Biochemistry

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“…Differences in surface hydrophobicity and sulfhydryl group exposure have also been implicated (Niwa 1992; Wicker et al 1986Wicker et al , 1989Kim 1987). More recently, the changes in gel properties induced by setting have been associated with changes in myosin heavy chain (MHC) content (Numakura et al 1985(Numakura et al , 1987a(Numakura et al ,b,, 1989; Katoh et al 1986; Nishimoto et al 1987Nishimoto et al , 1988Saeki et al 1988). Decreases in MHC content during setting were attributed to nondisulfide cross-linking of MHC by a transglutaminase (Kimura et al 1991; Kishi et al 1991).…”

Section: Introductionmentioning

confidence: 99%

Nondisulfide Covalent Cross-Linking of Myosin Heavy Chain in "Setting" of Alaska Pollock and Atlantic Croaker Surimi

Kamath

Lanier

Foegeding

et al. 1992

J Food Biochemistry

121

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Myosin heavy chain (MHC) content of cooked gels of pollock and croaker surimi decreased during preincubation (“setting”) at temperatures ranging from 4–50C. Decreases in MHC content were attributed to either nondisulfide covalent cross‐linking or proteolysis. Depending upon which process dominated at a given temperature, formation of stronger or weaker gels occurred, respectively. Maximum production of cross‐linked polymers occurred at the optimum setting temperatures, i.e., at 25C for pollock surimi and 40C for croaker surimi. Subsequent cooking of these set gels at 90C decreased the amount of cross‐linked polymers formed at the optimum setting temperature. Addition of free lysine‐HCl inhibited formation of cross‐linked polymers of MHC during setting and the increase in cooked gel strength for both species. This supports published evidence that cross‐linking of MHC during setting may be of the ε‐amino‐(γ‐glutamyl) lysine I type, mediated by a transglutaminase enzyme.

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Change in myofibrillar protein of the salted meat paste from Alaska pollack and tilapia during the setting.

Cited by 2 publications

References 0 publications

Different Arrangement of ?-(?-Glutamyl)lysine Cross-Linking in Alaska Pollock (Theragra Chalcogramma) Surimi Proteins by Streptoverticillium and Endogenous Transglutaminases During Suwari Process

Different Arrangement of ?-(?-Glutamyl)lysine Cross-Linking in Alaska Pollock (Theragra Chalcogramma) Surimi Proteins by Streptoverticillium and Endogenous Transglutaminases During Suwari Process

Nondisulfide Covalent Cross-Linking of Myosin Heavy Chain in "Setting" of Alaska Pollock and Atlantic Croaker Surimi

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