Biochemical and conformational changes of myosin purified from Pacific sardine at various pHs

J. D. Park, J. Yongsawatdigul, Y. J. Choi, Jae W. Park

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Biochemical and conformational changes of purified sardine myosin were investigated at various pHs. The purity of myosin, as determined by SDS-PAGE, was approximately 94.6%. One major band at 205 kDa, corresponding to myosin heavy chain, and 3 light chains at 31, 24, and 23 kDa were observed on the SDS-PAGE gel. The greatest myosin protein solubility was observed at pH 7 and remained constant up to pH 11. Sardine myosin showed no solubility at pHs 2.5 to 5.0. Three endothermic peaks were obtained for samples prepared at pHs 7 and 10, while no peaks were shown for pH 2 samples, indicating chemical denaturation of myosin occurred before thermal treatment. The greatest Ca 2+-ATPase activity was observed at pH 7, while no activity was observed between pHs 2 and 5 and at pH 11. Total sulfhydryl content was not measured at pHs 2.5 to 4 while the greatest measure was obtained for samples at pH 5.5. Surface hydrophobicity was not detected from pHs 2.5 to 5.0; thereafter the content remained consistent through pH 11. Storage modulus, indicating the elastic element of myosin gels, was minimally affected at pH 2, indicating myosin was chemically denatured before the temperature sweep treatment. However, at pH 10, the thermal exposure of myosin, as evidenced by dynamic thermograms with deeper valleys at 40 to 60°C, was noted, indicating myosin was not damaged by adjustment to pH 10 and therefore was still able to undergo thermal gelation.

Original languageEnglish
JournalJournal of Food Science
Volume73
Issue number3
DOIs
Publication statusPublished - 2008 Apr 1
Externally publishedYes

Fingerprint

Sardinops sagax
Myosins
myosin
Hot Temperature
Solubility
Polyacrylamide Gel Electrophoresis
Gels
sardines
Myosin Heavy Chains
Elastic Modulus
Hydrophobic and Hydrophilic Interactions
gels
Adenosine Triphosphatases
heat
storage modulus
myosin heavy chains
protein solubility

ASJC Scopus subject areas

  • Food Science

Cite this

Biochemical and conformational changes of myosin purified from Pacific sardine at various pHs. / Park, J. D.; Yongsawatdigul, J.; Choi, Y. J.; Park, Jae W.

In: Journal of Food Science, Vol. 73, No. 3, 01.04.2008.

Research output: Contribution to journalArticle

Park, J. D. ; Yongsawatdigul, J. ; Choi, Y. J. ; Park, Jae W. / Biochemical and conformational changes of myosin purified from Pacific sardine at various pHs. In: Journal of Food Science. 2008 ; Vol. 73, No. 3.
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