Premium
Effect of high‐pressure processing on myofibrillar protein structure
Author(s) -
Chapleau Nicolas,
Mangavel Cécile,
Compoint JeanPierre,
de LamballerieAnton Marie
Publication year - 2003
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1613
Subject(s) - myofibril , chemistry , circular dichroism , molten globule , size exclusion chromatography , protein secondary structure , protein aggregation , protein structure , protein tertiary structure , dynamic light scattering , phosphate , chromatography , biophysics , crystallography , biochemistry , chemical engineering , enzyme , nanoparticle , engineering , biology
Modification of myofibrillar proteins induced by high‐pressure processing has been investigated at pressures ranging from 50 to 600 MPa for 10 min at 20 °C. Analysis by spectroscopic methods and circular dichroism of myofibrillar proteins in phosphate buffer pH 6.0 containing 0.6 M 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. Copyright © 2003 Society of Chemical Industry