2006
DOI: 10.1111/j.1444-2906.2006.01284.x
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Thermally induced gelation of paramyosin from scallop adductor muscle

Abstract: Thermally induced gelation of paramyosin from scallop smooth adductor muscle was investigated by dynamic rheological measurements under various conditions. The paramyosin thermal gel was produced at pH 6.5 and 7.2 at temperatures above 30 ° C through a two-step increase in storage (G ′ ) and loss (G ′′ ) moduli; these values were higher than in gels produced from actomyosin at a high temperature. The thermal gel properties were very firm and brittle. In contrast, one main peak of G ′ was observed during gelati… Show more

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Cited by 11 publications
(2 citation statements)
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“…Although this could result from cleavage of the molecule during processing, this hypothesis was rejected because the MHC fibers were present in the other two fractions from the same sample of fin (Figure 2). PM fibers has also been related to behavior of muscle protein in food systems because, it is known that its presence in cephalopods muscle confers them with unique properties (Fukuda et al, 2006). We found the PM band (M r 97 kDa) in all fractions extracted, but mainly in the myofibrillar fraction, which is part of the pool of proteins extracted with high ionic strength buffer.…”
Section: Protein Fractions Determined By Sds-pagementioning
confidence: 64%
“…Although this could result from cleavage of the molecule during processing, this hypothesis was rejected because the MHC fibers were present in the other two fractions from the same sample of fin (Figure 2). PM fibers has also been related to behavior of muscle protein in food systems because, it is known that its presence in cephalopods muscle confers them with unique properties (Fukuda et al, 2006). We found the PM band (M r 97 kDa) in all fractions extracted, but mainly in the myofibrillar fraction, which is part of the pool of proteins extracted with high ionic strength buffer.…”
Section: Protein Fractions Determined By Sds-pagementioning
confidence: 64%
“…Gelation is an important functional property of fish muscle proteins (Niwa 1992; Fukuda and others 2006). Apart from fish muscle proteins, those of cephalopod such as octopus and squid have been reported to possess gelling properties (Nagashima and others 1992; Gomez‐Guillen and others 2002).…”
Section: Introductionmentioning
confidence: 99%