Effect of quality of Surimi on cross-linking reaction of myosin heavy chain during setting.

Numakura, Tadahiro; Seki, Nobuo; Kimura, Ikuo; Toyoda, Kyohei; Fujita, Takao; Takama, Kōzō; Arai, Ken‐ichi

doi:10.2331/suisan.53.633

Cited by 14 publications

(4 citation statements)

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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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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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“…Addition of cysteine or sodium bisulfite to the mince produced from frozen fish results in the recovery of reactive and total sulflydryl groups and improves the gel strength of the minced fish products (Lan et al, 1987). Denaturation and interactions between the heavy chains reduce gel-forming capacity and lower the surimi quality (Numakura et al, 1987).…”

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confidence: 99%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

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: The changes in protein structure associated with the preparation and frozen storage of surimi were investigated. Raw surimi was prepared by repeatedly washing Alaska pollock flesh with chilled water. The product was either slowly frozen or underwent rapid freezing using liquid air; in either case it was then subjected to frozen storage at ‐20 °C for 24 mo. Fourier transform infrared/attenuated total reflectance (FTIR/ATR) spectroscopy showed that during preparation of surimi, the a‐helix content increased with increased number of washing cycles. Differential scanning calorimetry (DSC) revealed a shift in the thermal transition of actin to a higher temperature during surimi preparation. Electrophoresis, FTIR/ATR spectroscopy, and DSC results revealed a loss of myofibrillar proteins from surimi after 3 washing cycles, suggesting that 3 washing cycles were adequate to prepare surimi. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) showed relatively minor changes in protein subunit structure with some loss of the myosin light chains (MLC); myosin heavy chain (MHC), actin, and tropomyosin were found to be relatively stable. Native‐PAGE showed no major changes in surimi after 24 mo storage at ‐20 °C. FTIR/ ATR spectroscopy indicated a significant decrease in a‐helix relative to p‐sheet structure in surimi after 2 y of storage at ‐20 °C. The loss of α‐helical content was more significant in slowly frozen surimi compared with rapid‐frozen surimi samples. DSC results revealed a shift in the thermal transition of actin to lower temperatures during frozen storage of surimi.

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“…Actually, commercially available surimi‐based, thermal gel products are produced by a 2‐step heating procedure which consists of the 1st step at moderately high temperatures at around 40 °C and the 2nd step at around 80 °C. The former step is called setting (suwari), where myosin heavy chains, the largest subunit of the myosin molecule, are bound covalently by the action of a tissue‐type transglutaminase (TGase), forming a gel network holding massive water (Niwa and Miyake ; Niwa and others ; Numakura and others ; Nishimoto and others ; Numakura and others ; Numakura and others ; Seki and others ; Kimura and others ). The tissue‐type TGase catalyzes the cross‐linking between γ‐carboxyamide group of glutamine residue and primary amine of lysine residue in the presence of Ca 2+ , thereby facilitating the increase of elasticity of fish meat thermal gels (Folk ; Joseph and others ; Wan and others ; Wan and others , ).…”

Section: Introductionmentioning

confidence: 99%

The Pepsin Digestibility of Thermal Gel Products Made from White Croaker (Pennahia argentata) Muscle in Associating with Myosin Polymerization Levels

Ueki

Wan

Watabe

2014

Journal of Food Science

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Thermal gels were made from white croaker (Pennahia argentata) surimi at various polymerization levels of myosin heavy chains induced by suwari treatment at 38 °C for various time periods and subsequently heated at 85 °C for 20 min. Myosin heavy chain polymerization levels were also achieved in the presence of microbial transglutaminase (MTG) added at various concentrations in the surimi. The breaking strength and breaking strain rate were markedly increased during suwari treatment up to 60 min in accordance with the increased levels of myosin heavy chain polymerization. MTG enhanced myosin heavy chain polymerization during suwari treatment for 15 and 30 min, resulting in the increase of breaking strength. The solubilization in 8 M urea and pepsin digestibility of these gels as well as angiotensin I-converting enzyme (ACE) inhibitory activity of their pepsin digests were decreased with the increased levels of myosin heavy chain polymerization. These results suggest that myosin heavy chain polymerization affects not only rheological properties of thermal gels but also their functional properties for human health.

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Effect of quality of Surimi on cross-linking reaction of myosin heavy chain during setting.

Cited by 14 publications

References 0 publications

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

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

Protein Structural Changes During Preparation and Storage of Surimi

The Pepsin Digestibility of Thermal Gel Products Made from White Croaker (Pennahia argentata) Muscle in Associating with Myosin Polymerization Levels

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