Dynamic rheological studies on salt-soluble proteins from three porcine muscles

Robe, Gerald H.; Xiong, Youling L.

doi:10.1016/s0268-005x(09)80165-3

Cited by 21 publications

(14 citation statements)

References 26 publications

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“…Samples used for viscometric measurement were diluted to 10 mg/mL with 50 mM phosphate buffer (pH 6.0) containing 0.6 M NaC1. Shear stress and apparent viscosity were determined as described by Robe and Xiong (1993) using a Model VORBohlinrheometer (BohlinInstruments, Inc., Cranbury, NJ).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein.

Wan¹,

Xiong²,

Decker³

1993

J. Agric. Food Chem.

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The effect of antioxidative treatments during bovine cardiac myofibril isolation on rheological and gelling properties of the myofibrillar protein was examined. Minced beef heart muscle was washed four times in 25 mM phosphate buffer (pH 7.0) without (control wash) or with combined antioxidants (0.02% propyl gallate, 0.2 % sodium ascorbate, and 0.2 ' % sodium tripolyphosphate). Washing with antioxidants inhibited oxidation in fresh myofibrillar pellets and in pellets stored for up to 8 days. The antioxidant treatment increased the shear stress and viscosity of protein suspensions by 20-100%. Both control and antioxidant-washed myofibrillar proteins exhibited complex dynamic viscoelastic characteristics during thermal gelation, but the antioxidant-washed protein showed greater storage and loss moduli than the control within 50-60 "C. An extrusion test indicated that the antioxidant-treated, freshly isolated protein formed stronger gels than the control. Thus, the functionality of myofibrillar protein can be protected by the inclusion of antioxidants in the muscle washing process.

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Section: Methodsmentioning

confidence: 99%

Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein.

Wan¹,

Xiong²,

Decker³

1993

J. Agric. Food Chem.

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“…Trout and Schmidt (1986) showed that binding ability of restructured beef rolls increased with the addition of di‐ or tripolyphosphates. Robe and Xiong (1993), on the other hand, found that storage modulus G′ of porcine muscle SSP decreased with the addition of 0.25% to 0.6% pyro‐ and tri‐polyphosphate. Torley and Young (1995) indicated that final rigidity and elasticity of salted beef homogenates were the same in the presence or absence of pyrophosphates.…”

Section: Additivesmentioning

confidence: 97%

“…The source and type of muscle can also influence gelation properties. The thermal gelation properties of myofibrillar protein have been extensively studied in different species including chicken (Smith and others 1988; Xiong 1992; Liu and Xiong 1996; Lesiów and Xiong 2003), beef (Fretheim and others 1986), pork (Robe and Xiong 1993; Lan and others 1995a, 1995b), rabbit (Boyer and others 1996a, 1996b), turkey (Barbut 1997), fish (Hennigar and others 1989; Chan and others 1992), shrimp (Chawla and others 1996), and squid (Paredi and others 1999). Cofrades and others (1997) investigated thermal gelation properties of chicken, pork, and hake actomyosin and observed no significant difference in the maximum gel strength among the 3 species despite the fact that pH, NaCl level, and protein concentration were different in each case.…”

Section: Type and Source Of Musclementioning

confidence: 99%

“…There have been a number of studies which examined the effects of muscle type within specific species. Using dynamic rheological testing, Robe and Xiong (1993) examined SSP extracted from porcine longissimus dorsi (LD) as well as from serratus ventralis (SV) and vastus intermedius (VI) muscles and found that the storage modulus (G′) was affected by muscle type, with VI exhibiting consistently stronger gels compared to those from SV and LD. Westphalen and others (2006) found that among semimembranosus (SM) myofibrils, LD, and psoas major (PM) porcine muscles SM produced the strongest gels and LD produced the weakest.…”

Section: Type and Source Of Musclementioning

confidence: 99%

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Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Sun

Holley

2010

Comp Rev Food Sci Food Safe

405

244

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Considerable research has been done to better understand the basis for gel formation by myofibrillar proteins (MPs) in effort to manufacture acceptable processed meats with lower cost and more desirable nutritional characteristics. Results from research available indicate that there is no substitute for the myofibrillar protein myosin in gel formation by proteins from a wide variety of animal and fish species. This report consolidates information on determinants of protein gel formation, examining types of muscles and fibers, the species influence, and interactions of the MPs actin and myosin with each other and with fat, gelatin, starch, hydrocolloids, some protein soy, whey, and nonprotein additives such as phosphates and acidifiers, and the influences of pH, ionic strength, rates of heating, and its absence, protein oxidation, as well as the use of transglutaminase and high hydrostatic pressure. It is of interest that myosin alone will form acceptable gels. Gel formation by MPs is optimized at pH 6, an ionic strength of 0.6 M, and at 60 to 70 °C. The observations that collagen‐derived gelatin can reduce the rubbery texture of low‐fat products and that solubilization of MPs is not always essential for gel formation, and the observation that good gels can be formed in the absence of salt, are exciting developments that should be considered as pressure mounts to continue to reduce fat and salt in the diet.

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“…Trout and Schmidt (1986) showed increased binding ability (cooking yield and tensile strength) in restructured beef rolls with di-or tripolyphosphates. Robe and Xiong (1993) found that shear stress (G') of salt-soluble proteins of porcine muscle decreased with tripolyphosphate. Torley and Young (1995) reported that final rigidity and elasticity (energy loss) of salted beef homogenates were the same in the presence or absence of pyrophosphate.…”

Section: Discussionmentioning

confidence: 99%

Gelation of Beef Heart Surimi as Affected by Antioxidants

Srinivasan

Xiong

1996

Journal of Food Science

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Oxidation of proteins (carbonyls) and lipids (TBARS) in beef heart surimi-like materials during preparation and storage (2ЊC) was inhibited by propyl gallate (0.02%) or ␣-tocopherol (0.2%). Inhibition of oxidation did not affect surimi gel property (storage modulus, G'). Storage promoted oxidation of proteins in 0.2% ascorbate-washed mince, leading to increases in peak (Ϸ55ЊC) and final (70ЊC) G' of thermally induced surimi gel. Protein carbonyls in stored surimi and its sol (salted), as well as TBARS of the sol, strongly correlated with both peak and final G' of gels. Incorporation of tripolyphosphate into washed mince promoted gelation whether the surimi-like material was oxidized or not.

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Dynamic rheological studies on salt-soluble proteins from three porcine muscles

Cited by 21 publications

References 26 publications

Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein.

Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein.

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Gelation of Beef Heart Surimi as Affected by Antioxidants

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