Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength.
Adjustment of pH from 6.4 to neutrality improved gelling ability and water-holding capacity of twice water-washed, minced chicken-breast muscle significantly at physiological ionic strength, at which the majority of the myofibrillar proteins, including myosin, are not soluble. A strain value of 2.2 was obtained at neutral pH. Myofibrils were the main components of the gel network at both pH 6.4 and 7.0; however, the myofibrillar distribution varied with the pH value. At pH 6.4, myofibrils formed a network of localized aggregates leaving large voids between, whereas at neutral pH, an evenly distributed network of myofibrils was formed. In addition, at neutral pH, a network of fine strands was found within the network of myofibrils. The network was much less developed at pH 6.4. The thin and thick filaments within each myofibrillar structure were disorganized at both pH values. The intramyofibrillar spaces were larger at neutral pH than at pH 6.4. It was proposed that adjustment of pH to neutrality increased electrostatic repulsion leading to a more even distribution of the myofibrillar proteins, a key factor responsible for the improved gel strength and water-holding capacity.
Feng
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Massachusetts Agricultural Experiment Station, Department of Food Science, University of Massachusetts/Amherst, Marine Station, Gloucester, Massachusetts 01930, USA. ummarine@tiac.net
Hultin
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HO
D000818:Animals; D002645:Chickens / Q000378:metabolism*; D005511:Food Handling; D005782:Gels / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008460:Meat; D009124:Muscle Proteins; D018482:Muscle, Skeletal / Q000737:chemistry* / Q000378:metabolism; D012212:Rheology; D012995:Solubility; D013997:Time Factors; D014867:Water
D005782:Gels; D009124:Muscle Proteins; D014867:Water