Gel Strength Development During Heating of Surimi in Combination with Egg White or Whey Protein Concentrate

Burgarella, J. C.; Lanier, Tyre C.; Hamann, D. D.; Wu, M. C.

doi:10.1111/j.1365-2621.1985.tb10541.x

Cited by 37 publications

(22 citation statements)

References 7 publications

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“…To reduce cost, improve flavor, and/or enhance texture of meat products, a number of additives have been developed and used in meat products, including enzymes as well as protein and nonprotein additives. These functional protein additives have been examined: whey (Burgarella and others 1985a, 1985b; Weerasinghe and others 1996; Liu and others 2000), caseinate (Camou and Sebranek 1990), egg albumen (Burgarella and others 1985a, 1985b; Hamann and others 1990; Pietrasik and Li‐Chan 2002), soy (Kurth and Rogers 1984; Feng and others 2003; Ramírez‐Suárez and Xiong 2003), wheat gluten (Ramírez‐Suárez and others 2005), cereal proteins (Chang‐Lee and others 1990; Chung and Lee 1990), and blood plasma and globin proteins (Autio and Mietsch 1990; Park 1994; Kang and Lanier 1999; Lou and others 2000). In addition, these nonprotein additives have been used in surimi and other meat products especially restructured meats; starch (Chen and others 1993; Yoo and Lee 1993; Yoon and others 1997a, 1997b; Kong and others 1999a, 1999b, 2001) and hydrocolloids such as carrageenan, alginate, pectins, xanthan gum, locust bean gum, and guar gum (Gómez‐Guillén and others 1997; Montero and others 2001; Pérez‐Mateos and others 2001; Barrera and others 2002; Ramírez and others 2002; Verbeken and others 2005).…”

Section: Additivesmentioning

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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Section: Additivesmentioning

confidence: 99%

“…Burgarella and others (1985b) reported that egg white and whey protein substitutions interfered with fish protein gelation in surimi. The energy levels required to penetrate the fish + egg white and fish + whey gels were lower than those required for individual protein gels.…”

Section: Additivesmentioning

confidence: 99%

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Sun

Holley

2010

Comp Rev Food Sci Food Safe

405

244

View full text Add to dashboard Cite

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“…This was probably because these nonmuscle proteins interfered with gel formation by preventing actomyosin cross‐linking (Chung and Lee 1991). Burgarella et al. (1985) suggested that loss of gel strength with nonmuscle protein additives could be caused by “dilution” of myofibrillar protein.…”

mentioning

confidence: 99%

Effect of Chicken Plasma Protein and Some Protein Additives on Proteolysis and Gel-Forming Ability of Sardine (Sardinella Gibbosa) Surimi

Rawdkuen

Benjakul

Visessanguan

et al. 2007

J Food Processing Preservation

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The effect of chicken plasma protein (CPP) and various protein additives on autolysis and gel‐forming ability of sardine (Sardinella gibbosa) surimi was investigated. CPP and other protein additives showed inhibitory activity toward autolysis of sardine surimi incubated at 70C in a concentration‐dependent manner. Porcine plasma protein (PPP) and egg white (EW) were more effective in proteolysis prevention than CPP and other protein additives. Breaking force and deformation of both modori and kamaboko gels increased when CPP and other protein additives were added at levels up to 2% (P < 0.05). Nevertheless, PPP and EW showed a greater gel‐strengthening effect than CPP and other protein additives (P < 0.05). Addition of CPP and other plasma proteins resulted in decreased whiteness, especially with increasing amount (P < 0.05). However, no change in whiteness was observed with gels containing EW and soy protein isolate (SPI) (P > 0.05). Proteolysis of sardine surimi can be retarded by the addition of CPP and protein additives, leading to increased gel‐forming ability.

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“…Those researchers concluded that egg white does not interfere with the interaction between myosin molecules. Conversely, egg-white solutions added to surimi (Atlantic Croaker) were antagonistic to gel formation (Burgarella et al, 1985b). Clark et al (1983) identified an interference of gel network formation in model mixtures of agar and gelatin.…”

Section: Resultsmentioning

confidence: 98%

Effect of Washing and Adding Spray-Dried Egg White to Mechanically Deboned Chicken Meat on the Quality of Cooked Gels

1990

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Mechanically deboned chicken meat (MDCM) was washed using a two-step washing regimen, which yielded a reduced-fat and light-colored meat. Spray-dried egg white (SDEW) was added to unwashed and washed MDCM at four levels [.0%, 2.5%, 5.0%, 7.5% (wt/wt)], then cooked. Cooked gels were analyzed for cook yield (CY), proximate composition, reflectance color, and texture (gel torsion).The CY was significantly lower for washed versus unwashed gels. Adding SDEW significantly increased CY in MDCM gels. Moisture was significantly higher in washed than unwashed gels. Moisture was reduced and protein was increased by adding SDEW to the gels at the higher levels.Washed MDCM gels were significantly lighter in color (higher L*) and less red (lower a*) than unwashed gels at all levels of added SDEW. Values of L* and a* are those specified by the International Commission on Illumination. Less apparent but significant lightening effects were observed due to the addition of SDEW.Washed MDCM gels were stronger (higher stress) and in most cases more deformable (higher strain) than unwashed gels. Small increases in gel strength were observed at the highest levels of added SDEW. Strain significantly decreased at the 7.5% SDEW level in both washed and unwashed gels. (

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Gel Strength Development During Heating of Surimi in Combination with Egg White or Whey Protein Concentrate

Cited by 37 publications

References 7 publications

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Effect of Chicken Plasma Protein and Some Protein Additives on Proteolysis and Gel-Forming Ability of Sardine (Sardinella Gibbosa) Surimi

Effect of Washing and Adding Spray-Dried Egg White to Mechanically Deboned Chicken Meat on the Quality of Cooked Gels

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