Hydrostatic Pressure-induced Aggregation of Myosin Molecules in 0.5<scp>M</scp>KCl at pH 6.0

Yamamoto, Katsuhiro; Hayashi, Saihou; Yasui, Tsutomu

doi:10.1271/bbb.57.383

Cited by 65 publications

(31 citation statements)

References 3 publications

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“…Pressurization may cause denaturation and/or aggregation (Okamoto et al, 1990;Yamamoto et al, 1993;Mandava et al, 1994;Cheah and Ledward, 1996), which could limit heat gelation in meat batters so that samples are less hard (Carballo et al, 1996a). Such effect should presumably be associated with a decrease in water/fat binding properties, but the opposite behavior was observed in our results (Tables 2 and 3).…”

Section: Texture Profile Analysismentioning

confidence: 48%

High‐pressure‐cooked Low‐fat Pork and Chicken Batters as Affected by Salt Levels and Cooking Temperature

Jiménez‐Colmenero

Fernández

Carballo

et al. 1998

Journal of Food Science

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The application of high pressure (200 and 400 MPa, 30 min) favored water and fat binding properties of chicken and pork batters even at low ionic strength. Textural properties of meat batters (particularly hardness and chewiness, and to a lesser extent springiness and cohesiveness) were influenced by cooking temperature. High pressures influenced the texture of batters, so that pressurized samples were less hard, cohesive, springy or chewy than nonpressurized samples; this effect was not related to on salt concentration. High pressure treatment limited the formation of gel structures, which probably was associated with its preserving effect against thermal denaturation of meat proteins.

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Section: Texture Profile Analysismentioning

confidence: 48%

High‐pressure‐cooked Low‐fat Pork and Chicken Batters as Affected by Salt Levels and Cooking Temperature

Jiménez‐Colmenero

Fernández

Carballo

et al. 1998

Journal of Food Science

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“…In the native state, myosin polymers are bound by their tails to form filamentous aggregates. Pressure could dissociate this aggregation and promote a new type of aggregation linked with exposure of the hydrophobic core localised in the head of myosin, according to the mechanism described by Yamamoto et al 6 This change in aggregation type could modify the complex shape of myosin aggregates but not the relative molecular weight of aggregates.…”

Section: Modification Of Tertiary Structure Of Proteins By High Pressurementioning

confidence: 99%

Effect of high‐pressure processing on myofibrillar protein structure

Chapleau

Mangavel²,

Compoint³

et al. 2003

J Sci Food Agric

108

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Modification of myofibrillar proteins induced by high-pressure processing has been investigated at pressures ranging from 50 to 600 MPa for 10 min at 20 • C. Analysis by spectroscopic methods and circular dichroism of myofibrillar proteins in phosphate buffer pH 6.0 containing 0.6 M KCl showed no changes in the secondary structure of proteins. However, study of protein conformation by quasielastic light scattering and gel filtration chromatography proved the emergence of aggregation after treatment at pressures higher than 300 MPa. This aggregation was accompanied by enhanced binding of anilino-1-naphthalene-8-sulphonic acid, which indicated an increase in hydrophobic bonding of myofibrillar proteins. Modification of the tertiary and quaternary structures of proteins may induce a molten globule state.

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“…We had reported morphological and physicochemical properties of pressure treated myosin [12][13][14]. However, the structure of myosin under pressure is not clearly known, so we investigated the pressure-induced structural changes of myosin by the in situ measurement of turbidity as well as the ANS fluorescence intensity of myosin under pressure.…”

Section: Discussionmentioning

confidence: 99%

“…The turbidity of myosin filaments in 0.1 M KCl at pH 7.0 decreases under relatively low pressure [11]. The aggregation of myosin monomer in 0.5 M KCl at pH 6.0 occurs through head-to-head interactions among myosin molecules by pressure treatment [12,13]. Myosin filaments in 0.1 M KCl at pH 6.0 form a gel in response to pressure treatments at 210 MPa for 10 min [14].…”

Section: Introductionmentioning

confidence: 99%

“…Myosin filaments in 0.1 M KCl at pH 6.0 form a gel in response to pressure treatments at 210 MPa for 10 min [14]. We have already reported the mechanism of pressure-induced gelation of myosin filaments [12][13][14]. The pressure-induced gelation of myosin occurs only by head-to-head interactions and tail-to-tail interaction, which takes part in heat-induced gelation, is not involved.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Changes in rabbit skeletal myosin and its subfragments under high hydrostatic pressure

Iwasaki

Yamamoto

2003

International Journal of Biological Macromolecules

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Hydrostatic Pressure-induced Aggregation of Myosin Molecules in 0.5MKCl at pH 6.0

Cited by 65 publications

References 3 publications

High‐pressure‐cooked Low‐fat Pork and Chicken Batters as Affected by Salt Levels and Cooking Temperature

High‐pressure‐cooked Low‐fat Pork and Chicken Batters as Affected by Salt Levels and Cooking Temperature

Effect of high‐pressure processing on myofibrillar protein structure

Changes in rabbit skeletal myosin and its subfragments under high hydrostatic pressure

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