Dynamic rheological behaviour and biochemical properties of rabbit skeletal actomyosin during storage at 0° C

Ikeuchi, Yoshihide; Tanji, H.; Kakimoto, Takaaki; Suzuki, Atsushi

doi:10.1002/jsfa.2740650112

Cited by 6 publications

(8 citation statements)

References 36 publications

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“…4). Overall changes in storage modulus of chicken surimi during heating to 80ЊC were similar to changes in rigidity modulus of minced turkey muscle and rabbit skeletal actomyosin reported by Montejano et al (1984) and Ikeuchi et al (1994).…”

Section: Resultssupporting

confidence: 82%

Heat‐Induced Gelation Properties of Surimi From Mechanically Separated Chicken

Smyth

O’Neill

1997

Journal of Food Science

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Chicken surimi was prepared from fresh mechanically separated chicken meat using a sodium bicarbonate washing process. The heat-induced gelation properties were assessed under different conditions of pH, temperature, heating rate, protein and sodium tripolyphosphate (TPP) concentrations. Surimi gel strength increased (p Ͻ 0.05) after: reducing pH from 6.4 to 6.0, increasing temperature from 40ЊC to 80ЊC, reducing heating rate from 5ЊC/min to 1ЊC/min, increasing protein concentration from 4% (w/w) to 8% (w/w) or addition of 0.3% (w/w) TPP. Freeze thaw stability studies revealed that the gel strength of surimi decreased (p Ͻ 0.05) when subjected to frozen storage at Ϫ18ЊC.

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Section: Resultssupporting

confidence: 82%

Heat‐Induced Gelation Properties of Surimi From Mechanically Separated Chicken

Smyth

O’Neill

1997

Journal of Food Science

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“…2B). In the NAM system, no significant decrease in Ca 2 + -ATPase activity was observed during storage, 11) which is different from the result shown in this figure. This difference between NAM and RAM may have arisen from the difference in state of the myosin molecules in their complexes.…”

Section: Biochemical and Physicochemical Measurementscontrasting

confidence: 99%

“…1, 4A and 4B). In a previous paper, 11) we have reported that the peak at around 52°C clearly remained in NAM stored in 0.5 M KCl at pH 6.0 for 15 days. This indicates that the actin in NAM had been fairly well stabilized during storage.…”

Section: Dynamic Rheological Measurementsmentioning

confidence: 61%

Thermal Gelation Profile Changes in Reconstituted Actomyosin due to Storage under a High Salt Concentration and Low Temperature

Tanji¹,

Ikeuchi

Yoshizawa

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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Changes in the heat-induced gelation properties of reconstituted rabbit skeletal actomyosin stored under a high salt concentration at pH 6.0 and O°C were investigated at different weight ratios of actin to myosin by using dynamic rheological and biochemical measurements. The addition of actin resulted in a pronounced peak maximum at about 50°C and an accompanying temporary reduction in the range at about 50°C to 60°C. The more the initial actin concentration was increased, the greater was the area of the peak/shoulder. However, this area was markedly diminished with increasing storage time. As a result, the dynamic rheological pattern was transformed from an actomyosin type into a myosin type. The relationship between the G' value at 80°C and the actin/myosin weight ratio was curvilinear, with a peak at the ratio of 0.05, immediately after storage was started. This profile changed during storage, depending on the extent to denaturation of actin and myosin in the reconstituted actomyosin (RAM). The G' value of actomyosin in 0.5 M KCI with a small actin/myosin ratio of 0.05 decreased to one-half of its initial value after 7 days of storage, whereas the G' value with a large actin/myosin ratio of 0.225 increased by about 1.6 times. In 1.5 M KCI, aU the G" values declined to the level with myosin alone after 7 days of storage. The time-course plots of the remaining actin concentration in RAM at different weight ratios of actin to myosin after being treated with 0.5 M or 1.5 M KCI showed a decrease in the actin content with increasing storage time, and an increase in the KCI concentration to 1.5 M KCI promoted the denaturation of actin in RAM faster than with 0.5 M KCt The surface hydrophobicity of each RAM sample progressively increased with increasing storage time, while little significant increase in the sulfhydryl (SH) content during storage was observed. It is concluded that changes in the heat-induced gelation properties of actomyosin during storage are largely attributable to the denaturation of actin rather than to the denaturation of myosin or to quantitative changes in the SH content and hydrophobicity.Key words: thermal gelation; denaturation; myosin; actin; actomyosin In an earlier work by Yasui et al. on the heat-induced gelation mechanism of muscle proteins, only two proteins, myosin and actin, were recognized as being essential for the development of gelation properties in meat products. 1.2) According to their theory, myosin is the major factor involved in the heat-induced gelation of meat proteins, and its amount and nature bear a close relationship with the binding capacity of the resulting products. Actin alone does not exhibit any gelling ability, 1.3) but has a synergetic effect on a myosin gel. 1.2) Namely, a small amount of actin, which forms an F-actomyosin complex in the system, reinforces the myosin gel's strength, probably by functioning as a cross-linker with free myosin during the heatinduced gelation process at high ionic strength. The maximum gel strength is obtained at a 2.7 myosin to ...

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“…2) The authors have recently obtained experimental data suggesting that TM was responsible for stabilizing actin in natural actomyosin. 3) This finding made us aware of the importance of TM on actin filament properties in meat treated with salt (i.e., for curing).…”

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confidence: 99%

“…While the participation of T~v1 in the stability of actin can be imagined, it has not yet been definitively verified that the gel formability of natural actomyosin is affected by a change in the interaction between TM and actin during salt treatment. 3) To obtain more information about the stability of Factin in a natural actomyosin system during storage, we investigated the effect of TM on the denaturation of actin with or without heavy meromyosin (HMM) under various salt concentrations at pH 7.5 and O°C by using DNase I inhibition assay. The obtained results provide sufficient evidence that TM could effectively depress the denaturation of actin alone or actin with HMM at a comparatively low KCI concentration ranging from 0.1 to 0.5 M.…”

mentioning

confidence: 99%