ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Thermal aggregation properties of duck breast and leg salt-soluble proteins (SSP) were studied at pH 5.50, 5.75 and 6.00. At pH 5.50, a major transition for breast was observed at 60.3°C and for leg at 41.8°C. At pH 5.75, major transitions at 44.6 and 43.2°C were obtained, respectively, for the breast and leg SSP. Three transitions at 46.0, 53.0 and 59.0°C were exhibited by breast SSP at pH 6.00, whereas only two major transitions at 47.4 and 54.0°C were identified in leg SSP. Changes in transition peak heights and shifts in transition temperatures as a result of pH changes indicated that, depending on fiber type, pH may enhance or suppress the aggregation behavior of specific constituents of the myosin/actomyosin complex, thereby altering the overall aggregation pattern of the protein preparation.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1992.tb06845.x
Permalink