Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/69977
標題: Effect of hydrostatic pressure on molecular conformation of tilapia (Orechromis niloticus) myosin
作者: Ko, W.C.
Jao, C.L.
Hsu, K.C.
關鍵字: hydrostatic pressure
myosin
hydrophobicity
sulfhydryl group
Ca-ATPase
heat-induced gelation
thermal-denaturation
actomyosin
proteins
muscle
fish
stability
carp
fluorescence
aggregation
期刊/報告no:: Journal of Food Science, Volume 68, Issue 4, Page(s) 1192-1195.
摘要: 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 I-fold increase of their surface hydrophobicity (S(0)). 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.
URI: http://hdl.handle.net/11455/69977
ISSN: 0022-1147
文章連結: http://dx.doi.org/10.1111/j.1365-2621.2003.tb09623.x
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