Effects of Temperature, Actin-myosin Ratio, pH, and Salt and Protein Concentrations on Heat-induced Gelling of Cardiac Myosin and Reconstituted Actomyosin

Samejima, Kunihiko; Oka, Yukio; Yamamoto, Katsuhiro; Asghar, Ali; Yasui, Tsutomu

doi:10.1080/00021369.1986.10867689

Cited by 15 publications

(20 citation statements)

References 12 publications

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“…ofibrils (Samejima et al, 1992) but differed from reports for porcine cardiac myosin which had a maximal gel strength at pH 5.4 (Samejima et al, 1986). The +A0 washed myofibrils formed stronger gels than control myofibrils (-AO) at pH > 5.8 but not at pH ~5.7, suggesting possible modification of ionic interactions due to oxidation.…”

Section: Discussioncontrasting

confidence: 56%

Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Xiong

Decker

Robe

et al. 1993

Journal of Food Science

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Oxidation inhibition during washing, as it affects gelling properties and binding strength of beef heart myofibrillar protein, was investigated. Crude myofibrils isolated by repeated washing in the presence of propyl gallate, ascorbate and tripolyphosphate had a lower TBA value and formed stronger gels (puncture and compression strengths) in the pH range G-7.0 and in 0.6M NaCl than the control myofibrils. Inhibition of oxidation increased tensile stress of myofibrillar gels and enhanced bind strength in restructured meat. Functionality of myofibrillar protein could be protected by antioxidants used in the washing process.

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Section: Discussioncontrasting

confidence: 56%

Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Xiong

Decker

Robe

et al. 1993

Journal of Food Science

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“…The mechanisms of gel formation of myosin, actin and actomyosin have become clear through extensive studies (Samejima et al, 1969(Samejima et al, , 1988Ishioroshi et al, 1980Ishioroshi et al, , 1982Yasui et al, 1982;Asghar et al, 1984;Fretheim et al, 1986). Generally, myosin alone forms excellent gels.…”

Section: Introductionmentioning

confidence: 99%

Changes in Protein Solubility and Gelation Properties of Chicken Myofibrils during Storage

Xiong

Brekke

1989

Journal of Food Science

107

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The effect of storage on protein solubility and heat-induced gelation properties of chicken hen breast and leg myofibrils was investigated. Myofibrils suspended in 0.6M NaC1, pH 6.0, showed increasing protein solubility, viscosity, gel strength and water holding capacity with storage at 4°C. However, the effect of storage was most dramatic only during the initial 10 hr for all of the parameters studied. The relative distribution of the proteins comprising the salt soluble protein (SSP) extract changed during storage. Although storage had little effect on breast SSP, it was detrimental to leg SSP gelation. Breast myofibril suspensions, for all storage times, contained a greater amount of SSP and had better gelation properties than leg myofibril suspensions.

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“…Another reason for a decrease in breaking force by blending surimi and FPI may be because the ratio of surimi and FPI was not optimum. Samejima, Oka, Yamamoto, Asghar, and Yasui () showed lower gel strength when adding actin to myosin, whereas Yasui, Ishioroshi, and Samejima () illustrated a positive effect of actin on gel formation with an optimal ratio of actin and myosin. This suggested that the ability of protein to form gels depends on a favorable balance of attractive and repulsive forces and different protein structures.…”

Section: Resultsmentioning

confidence: 99%

Optimal blending of differently refined fish proteins based on their functional properties

Kobayashi

Park

2017

J Food Process Preserv

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Two different mixtures (Alaska pollock surimi with grass carp fish protein isolate (FPI) and grass carp surimi with grass carp FPI) were investigated for their compatibility and functionalities. As the proportion of FPI increased, it was observed surface hydrophobicity and surface reactive sulfhydryl (SRSH) content increased significantly, indicating the degree of fish protein unfolding prior to gelation was much higher than surimi alone. Comparable results were shown as measured by storage modulus (G 0 ) in oscillatory dynamic rheology, demonstrating the gelling temperature was reduced when the proportion of FPI increased. Effects of mixing surimi and FPI on gel functionality (hardness, cohesiveness, and whiteness) exhibited a linear pattern when the proportion of surimi was larger than or equal to that of FPI. However, there were no linear relationships when the proportion of FPI exceeded that of surimi. Practical applicationsCommercial surimi has been successfully used in the Western world over 30 years. Unlike surimi which is a refined fish myofibrillar protein composite, fish protein isolate (FPI) is a refined composite of myofibrillar protein and sarcoplasmic protein. The former is made by avoiding any chemical/ physical denaturation, while the latter can be made by inducing chemical denaturation and renaturation with pH shift. Even though FPI is not currently available in a commercial scale, it has a great potential to replace all or a part of surimi for the manufacture of fish protein gel products. This study reveals how to optimally mixed these two differently refined fish proteins based on their functional properties. The results suggested that blending surimi and FPI may be feasible only when the proportion of FPI does not exceed 50%.

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Effects of Temperature, Actin-myosin Ratio, pH, and Salt and Protein Concentrations on Heat-induced Gelling of Cardiac Myosin and Reconstituted Actomyosin

Cited by 15 publications

References 12 publications

Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Changes in Protein Solubility and Gelation Properties of Chicken Myofibrils during Storage

Optimal blending of differently refined fish proteins based on their functional properties

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