期刊
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
卷 84, 期 1, 页码 66-74出版社
WILEY
DOI: 10.1002/jsfa.1613
关键词
myofibrillar proteins; high pressure; protein structure
Modification of myofibrillar proteins induced by high-pressure processing has been investigated at pressures ranging from 50 to 600 MPa for 10 min at 20degreesC. Analysis by spectroscopic methods and circular dichroism of myofibrillar proteins in phosphate buffer pH 6.0 containing 0.6m KCl showed no changes in the secondary structure of proteins. However, study of protein conformation by quasielastic light scattering and gel filtration chromatography proved the emergence of aggregation after treatment at pressures higher than 300 MPa. This aggregation was accompanied by enhanced binding of anilino-1-naphthalene-8-sulphonic acid, which indicated an increase in hydrophobic bonding of myofibrillar proteins. Modification of the tertiary and quaternary structures of proteins may induce a molten globule state. (C) 2003 Society of Chemical Industry.
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