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

Iwasaki, Tomohito; Yamamoto, Katsuhiro

doi:10.1016/j.ijbiomac.2003.08.005

Cited by 28 publications

(9 citation statements)

References 24 publications

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“…The promotion of the reactive SH content indicated that the pressure changed the myosin conformation, with the exposure of SH inside the head portion. Iwasaki & Yamamoto () reported that during the compression process, the structure of myosin was collapsed, resulting in the formation of small‐sized aggregates. But in the decompression process, small‐sized aggregates of myosin grew to large aggregates.…”

Section: Resultsmentioning

confidence: 99%

High‐pressure processing‐induced conformational changes during heating affect water holding capacity of myosin gel

Wang

Chen

Zou

et al. 2016

Int J of Food Sci Tech

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Summary This study aimed to investigate the effects of high‐pressure processing (HPP) (0.1‐400 MPa for 9 min) on the water holding capacity (WHC) of heat‐induced rabbit myosin gel and structural changes during thermal treatment (25–75 °C). HPP at 100 MPa significantly increased the WHC (P < 0.05) and formed more regular and homogeneous three‐dimensional network. Myosin tails at 100 MPa unfolded completely during the thermal treatment, which was beneficial to form a high WHC gel network. However, myosin pressurised at 200 MPa and above formed a weak gel. Their heads were already aggregated before heating, preventing from subsequent thermal denaturation and aggregation. With the temperature increasing, unfolding of myosin tails was not sufficient for a filamentous network formation. These results suggested that HPP could modify the myosin structure and affect the gel formation during heating. The 100 MPa was the optimum pressure level for the WHC of rabbit myosin gel.

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Section: Resultsmentioning

confidence: 99%

High‐pressure processing‐induced conformational changes during heating affect water holding capacity of myosin gel

Wang

Chen

Zou

et al. 2016

Int J of Food Sci Tech

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“…The hydrophobicity of myosin increases with heating, resulting in polymerization and gelation (Wicker and Knopp ). In the case of gelation caused by high hydrostatic pressure, the hydrophobicity of myosin also increases with pressure (Yamamoto and others ; Iwasaki and Yamamoto ). We found lower hydrophobicity of HMM in low ionic strength solution containing l ‐histidine than in high ionic strength solution (Figure ).…”

Section: Resultsmentioning

confidence: 99%

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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“…Loss of M‐line was shown to affect the thick filament resulting in release of myosin (Iwasaki et al., 2006; Jung et al., 2000b). Iwasaki and Yamamoto (2002, 2003) observed that the myosin tail (S2) dissociated to single peptide chains and the head (S1), being the most pressure‐sensitive part, was deformed (see : in Figure 3). It is noted in these studies that the subfragments, S1 and S2, were extracted from rabbit muscle prior to HPP treatment.…”

Section: Molecular Impacts Of Hpp To Meat Systemsmentioning

confidence: 99%

High‐pressure processing of meat: Molecular impacts and industrial applications

Bolumar

Orlien

Sikes

et al. 2020

Comp Rev Food Sci Food Safe

104

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High‐pressure processing (HPP) has been the most adopted nonthermal processing technology in the food industry with a current ever‐growing implementation, and meat products represent about a quarter of the HPP foods. The intensive research conducted in the last decades has described the molecular impacts of HPP on microorganisms and endogenous meat components such as structural proteins, enzyme activities, myoglobin and meat color chemistry, and lipids, resulting in the characterization of the mechanisms responsible for most of the texture, color, and oxidative changes observed when meat is submitted to HPP. These molecular mechanisms with major effect on the safety and quality of muscle foods are comprehensively reviewed. The understanding of the high pressure–induced molecular impacts has permitted a directed use of the HPP technology, and nowadays, HPP is applied as a cold pasteurization method to inactive vegetative spoilage and pathogenic microorganisms in ready‐to‐eat cold cuts and to extend shelf life, allowing the reduction of food waste and the gain of market boundaries in a globalized economy. Yet, other applications of HPP have been explored in detail, namely, its use for meat tenderization and for structure formation in the manufacturing of processed meats, though these two practices have scarcely been taken up by industry. This review condenses the most pertinent‐related knowledge that can unlock the utilization of these two mainstream transformation processes of meat and facilitate the development of healthier clean label processed meats and a rapid method for achieving sous vide tenderness. Finally, scientific and technological challenges still to be overcome are discussed in order to leverage the development of innovative applications using HPP technology for the future meat industry.

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

Cited by 28 publications

References 24 publications

High‐pressure processing‐induced conformational changes during heating affect water holding capacity of myosin gel

High‐pressure processing‐induced conformational changes during heating affect water holding capacity of myosin gel

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

High‐pressure processing of meat: Molecular impacts and industrial applications

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