ROLE OF pH IN GEL FORMATION OF WASHED CHICKEN MUSCLE AT LOW IONIC STRENGTH

Chang, Hsin-Sui; Feng, Yuming; Hultin, Herbert O.

doi:10.1111/j.1745-4514.2001.tb00751.x

Cited by 23 publications

(16 citation statements)

References 30 publications

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“…It has been described that this feature is species dependent (Perez-Mateos and Lanier 2006) and that it is enhanced by the pH-shifting method. It has been suggested (Chang et al 2001;Wright and Lanier 2005) that the more thorough disruption of muscle structure by acid or alkaline processing may play a key role in better distributing proteins for heat-induced gel formation which reduces the need for salt to accomplish the same effect. Kristinsson and Hultin (2003a) found that acid-and alkali-treated cod myofibrillar proteins gelled at lower temperatures than native proteins.…”

Section: Gel Qualitymentioning

confidence: 97%

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

Nolsøe

Undeland

2008

Food Bioprocess Technol

206

151

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The acid and alkaline solubilization processes for isolating muscle protein from ground fish raw materials are investigated by scrutinizing the literature. Following an introduction to the processes, with some underlying chemistry, patents related to the acid and alkaline solubilization process are described together with previously patented methods for processing of protein isolates. Focus is then placed on comparing a range of factors important in fish muscle protein isolation between the acid and alkaline solubilization processes, and classic washing-based surimi technology. The factors addressed were: protein yield, gel quality, color, lipid reduction, lipid oxidation, microbial stability, and frozen storage stability. A long series of studies made with different fish/shellfish species have been used for this purpose. Certain results are summarized in table form (protein yields, gel strength, and whiteness), others only in text form. From this part of the review, it is obvious that the acid process often has certain advantages (e.g., protein yield) and the alkaline process other ones (gel strength, whiteness, lipid removal, lipid oxidation, and total microbial count). Thus, the choice of method depends on the application. It is clear that most species respond differently to acid and alkaline solubilization, which is why the two methods are initially compared. In a section about new processing attempts, the use of the acid and alkaline methodology for isolating proteins from whole fish/shellfish and fish by-products is reviewed together with attempts to recover waste water proteins and attempts to modify the process. Tentative uses of the new protein isolates, e.g., as coatings, protein brines, and emulsifiers are finally described together with some conclusions and future opportunities for the acid and alkaline processes.

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Section: Gel Qualitymentioning

confidence: 97%

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

Nolsøe

Undeland

2008

Food Bioprocess Technol

206

151

View full text Add to dashboard Cite

show abstract

“…Gelling properties of the MPs depend upon pH (Chang and others 2001a; Lesiów and Xiong 2001a). At the isoelectric point (pI), proteins have a net charge of zero and retain the least amount of water.…”

Section: Phmentioning

confidence: 99%

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Sun

Holley

2010

Comp Rev Food Sci Food Safe

399

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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“…Recent trends indicate many consumers are interested in reducing their sodium intake. Thus, the salt content of surimi seafood deserves considerable attention (Chang and others 2001).…”

Section: Introductionmentioning

confidence: 99%

Negative Roles of Salt in Gelation Properties of Fish Protein Isolate

Kim

Park

2008

Journal of Food Science

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Salt effect on gelling properties of fish protein isolate (FPI) prepared by acid- and alkali-aided extraction was investigated. Acid- or alkali-extracted FPI formed significantly better gel texture with 0% NaCl than with 3% NaCl. Texture properties of acid- or alkali-extracted FPI decreased as NaCl content increased, especially at 2% to 3% salt. Contrarily, salt significantly promoted texture qualities of conventional surimi gels. The effect was highlighted when they were subjected to low temperature setting. The myofibrillar proteins in FPI were not solubilized when NaCl was added, perhaps due to protein aggregation caused by acid or alkali extraction. FPI solubility, however, was not closely related to their texture properties. Cold setting did not promote texture properties of FPI gels as much as conventional surimi gels. Acid-extracted gels gave the best color properties.

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ROLE OF pH IN GEL FORMATION OF WASHED CHICKEN MUSCLE AT LOW IONIC STRENGTH

Cited by 23 publications

References 30 publications

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Negative Roles of Salt in Gelation Properties of Fish Protein Isolate

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