Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine

Hayakawa, Tõru; Yoshida, Yuri; Yasui, Masanori; Ito, Toshiaki; Iwasaki, Tomohito; Wakamatsu, Jun‐ichi; Hattori, Akihito; Nishimura, Takanori

doi:10.1016/j.meatsci.2011.06.002

Cited by 64 publications

(55 citation statements)

References 15 publications

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“…These results indicate that there may exist an interaction between amino acids and SSMP, which affects the heat-induced gelation of SSMP, and thus having an influence on gel properties. The view is also supported by the fact that L-His affects rheological properties of myosin during heat-induced gelation, resulting in the formation of a fine network consisting of thin strands (Hayakawa et al, 2012).…”

Section: Introductionmentioning

confidence: 93%

“…Water holding capacity (WHC) and texture are the important properties of meat products (Hayakawa et al, 2012). The former affects mouthfeel and yield, and the latter imparts chewiness (Chen et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…The former affects mouthfeel and yield, and the latter imparts chewiness (Chen et al, 2014). Many efforts have been devoted to the improvement of WHC and texture of meat products (Hayakawa et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effects of l-Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle

Qin

Zhou

et al. 2015

LWT - Food Science and Technology

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Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of l-Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle

Qin

Zhou

et al. 2015

LWT - Food Science and Technology

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“…Theoretically, both Lys and Arg may have significant but different influences on chicken myosin gel. To date, a few papers have reported on the effects of histidine on the thermal gelling properties of the myosin system [16,17] and the effects of Arg on actomyosin [18] or the SSMP system. [19] However, information is lacking regarding the effects of Lys or Arg on the thermal gelling properties of the myosin system.…”

Section: Introductionmentioning

confidence: 99%

Gelling properties of myosin as affected by L-lysine and L-arginine by changing the main molecular forces and microstructure

Zheng

Lei

et al. 2017

International Journal of Food Properties

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This paper investigated the effects of L-lysine (Lys) and L-arginine (Arg) on the water-holding capacity (WHC) and hardness of myosin gel as well as the mechanism of these effects. The results showed that Lys, Arg, and KOH increased the WHC but decreased the hardness in all cases. At pH 6.32, the WHC increased in the order control < KOH < Lys ≈ Arg, while the hardness decreased in the order control > KOH > Lys > Arg. Lys shortened low field nuclear magnetic resonance spin-spin relaxation times (T 2 ), while Arg and KOH slightly affected T 2 . Lys, Arg, and KOH had different influences on the molecular forces in myosin gels and the distribution of myosin size. Lys formed a gel with porous clusters, while Arg generated a gel with fine caves. Therefore, both Lys and Arg changed the microstructure of myosin gel by changing the distribution of the myosin size as well as the molecular forces that form and/or maintain myosin gel, ultimately contributing to the differences in the WHC, hardness, and T 2 .ARTICLE HISTORY

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“…In the presence of l ‐histidine, myosin molecules disperse as monomers and are solubilized in neutral and low ionic strength solutions. Moreover, we found that myosin in low ionic strength solution containing l ‐histidine formed a transparent gel after heating and that the heat‐induced gel had a fine network structure (Hayakawa and others ). The heat‐induced gelation structures of soluble myosin in low ionic strength solution containing l ‐histidine are similar to that of heavy meromyosin (HMM), a subfragment of myosin consisting of a globular head (S1) and a helical tail (S2), in high ionic strength solution (Ishioroshi and others ; Hayakawa and others ).…”

Section: Introductionmentioning

confidence: 95%

Role of Heavy Meromyosin in Heat‐Induced Gelation in Low Ionic Strength Solution Containing l‐Histidine

Hayakawa

Yoshida

Yasui

et al. 2015

Journal of Food Science

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The gelation of myosin has a very important role in meat products. We have already shown that myosin in low ionic strength solution containing L-histidine forms a transparent gel after heating. To clarify the mechanism of this unique gelation, we investigated the changes in the nature of myosin subfragments during heating in solutions with low and high ionic strengths with and without L-histidine. The hydrophobicity of myosin and heavy meromyosin (HMM) in low ionic strength solution containing L-histidine was lower than in high ionic strength solution. The SH contents of myosin and HMM in low ionic strength solution containing l-histidine did not change during the heating process, whereas in high ionic strength solution they decreased slightly. The heat-induced globular masses of HMM in low ionic strength solution containing L-histidine were smaller than those in high ionic strength solution. These findings suggested that the polymerization of HMM molecules by heating was suppressed in low ionic strength solution containing L-histidine, resulting in formation of the unique gel.

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Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine

Cited by 64 publications

References 15 publications

Effects of l-Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle

Effects of l-Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle

Gelling properties of myosin as affected by L-lysine and L-arginine by changing the main molecular forces and microstructure

Role of Heavy Meromyosin in Heat‐Induced Gelation in Low Ionic Strength Solution Containing l‐Histidine

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