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  • 2000-2004  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Hydrostatic pressures from 500 to 2000 atmospheres (atm) were applied at 0°C to determine the aggregation and viscoelastic properties of tilapia (Orechromis niloticus) myosin. Native myosins were present as long, linear, and single filaments. After a 500-atm treatment, these filaments unfolded and their volume decreased. Upon 1000-atm and 1500-atm treatments, myosins aggregated and formed inseparable network structures. Further, they transformed from viscous sol to elastic gels with a pressure of 500 to 1000 atm. At 2000 atm, the myosin formed irregular aggregates. This study reveals that at 500 atm, myosins unfolded; at 1000 atm, they aggregated, and beyond 1500 atm, they formed both a precipitate and gel.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 69 (2004), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Hydrostatic pressures (50 to 300 MPa) were applied at 0 °C for 50 min to determine the aggregation and viscoelastic properties of tilapia (Orechromis niloticus) myosin fragments: subfragment-1 (S-1) and rod. With pressure lower than 150-MPa treatment, S-1 underwent intermolecular interaction to increase its elastic properties. After a 200-MPa treatment, S-1 unfolded, aggregated, and decreased its solubility. A turbid solution was obtained after pressurization over 200 MPa. Further, S-1 transformed to a more elastic gel with pressure increasing. At 200 MPa, S-1 denatured entirely with no change of enthalpy detected by differential scanning calorimetry (DSC). However, all properties of rod did not change during pressurization. This study reveals that S-1 contributes the initiation of gel formation in myosin, and the role of rod is not clear. Keywords: hydrostatic pressure, S-1, rod, denaturation
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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