Effect of Hydrostatic Pressure on Molecular Conformation of Tilapia (Orechromis niloticus) Myosin

Change in tilapia myosin molecular conformation due to pressurization at 50 to 200 MPa for 0 to 60 min was investigated. After a 50-MPa treatment, tilapia myosins slightly decreased their total sulfhydryl contents and exposed their hydrophobic residues. Experimental results indicated that 100- and 1...

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Bibliographic Details
Published in:Journal of food science 2003-05, Vol.68 (4), p.1192-1195
Main Authors: Ko, W.C, Jao, C.L, Hsu, K.C
Format: Article
Language:English
Subjects:
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
Ca-ATPase
Ca2-transporting ATPase
disulfide bonds
Fish
Food industries
Food science
Fundamental and applied biological sciences. Psychology
hydrophobic bonding
hydrophobicity
hydrostatic pressure
molecular conformation
myosin
Orechromis niloticus
sulfhydryl group
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Summary:Change in tilapia myosin molecular conformation due to pressurization at 50 to 200 MPa for 0 to 60 min was investigated. After a 50-MPa treatment, tilapia myosins slightly decreased their total sulfhydryl contents and exposed their hydrophobic residues. Experimental results indicated that 100- and 150-MPa treatments caused an apparent unfolding of myosins and a 1-fold increase of their surface hydrophobicity (S(o)). Myosins mainly formed intermolecular disulfide bonds with pressures of 100 to 200 MPa. In addition, increasing pressures altered the myosin conformation and decreased its Ca-ATPase activity. Myosin apparently unfolded and formed disulfide bonds and hydrophobic interactions with pressurizing at 150 MPa.
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.2003.tb09623.x