Effect of alcohol and pyrophosphate on non-proteolytic modori during thermal gelation of actomyosin sol

Carp actomyosin sol containing 90 mg protein/g in 0.5 M NaCl (or 1 M NaCl) at pH 7.0 was heated from 5 to 80 deg C at heating rate of 2 deg C/min. The non-proteolytic modori (gel weakening) which occurred characteristically during actomyosin gelation was detected at 53 deg C by measuring storage mod...

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Bibliographic Details
Published inNippon Suisan Gakkaishi Vol. 67; no. 4
Main Authors Ni, S. (Hokkaido Univ., Sapporo (Japan)), Nozawa, H, Seki, N
Format Journal Article
LanguageJapanese
Published 2001
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Summary:Carp actomyosin sol containing 90 mg protein/g in 0.5 M NaCl (or 1 M NaCl) at pH 7.0 was heated from 5 to 80 deg C at heating rate of 2 deg C/min. The non-proteolytic modori (gel weakening) which occurred characteristically during actomyosin gelation was detected at 53 deg C by measuring storage modulus (G') of the sol. The addition of ethanol and n-butanol to the sol did not suppress the non-proteolytic modori but shifted the modori temperature to 51 deg C and 42 deg C, respectively. Butanol greatly increased the G' and the breaking strength of actomyosin gel formed. The addition of pyrophosphate-Mg (PPi-Mg) dissociated actin and myosin from actomyosin, and changed the thermal gelation pattern of actomyosin sol to a myosin-like one. The change eliminated non-proteolytic modori, though PPi-Mg did not increase the G' or the breaking strength of thermally induced gel. PPi-Mg made no contribution to a great increase in the gel strength of actomyosin gel formed by a two step heating method including microbial transglutaminase-induced setting.
Bibliography:2001006279
Q02
Q05
ISSN:0021-5392
DOI:10.2331/suisan.67.735