title: The effect of high pressure on the functional properties of pork myofibrillar proteins.
abstract: Complementary methodologies were used to analyse the pressure-induced modification and functionality of myofibrillar proteins from pork meat pressurised at 200, 400, 600, or 800 MPa (10 min, 5 or 20 °C). Pressure at 400 MPa was found to be the threshold for loss of solubility, and the structural proteins, myosin and actin, lost their native solubility due to aggregation. The results from the extraction of proteins with different reagents targeting the disruption of specific molecular interactions suggested that pressure-induced aggregation was caused mainly by hydrogen bonding during pressurisation and not hydrophobic interactions nor disulphide cross-links. Furthermore, the soluble proteins were exposed to remarkable structural changes already at 200 MPa and lost their native functionality. The modification of the proteins in pressurised meat affected the water binding sites of the myofibrillar proteins and, thereby, the interactions between proteins and water molecules, and distribution between myofibrillar and extra-myofibrillar compartments.
authors.affiliation: Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark.
authors.forename: Alberto
authors.initials: A
authors.lastname: Grossi
authors.affiliation: Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark.
authors.forename: Karsten
authors.initials: K
authors.lastname: Olsen
authors.affiliation: Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark.
authors.forename: Tomas
authors.initials: T
authors.lastname: Bolumar
authors.affiliation: Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark.
authors.forename: Åsmund
authors.initials: Å
authors.lastname: Rinnan
authors.affiliation: The Niels Bohr Institute, Faculty of Science, University of Copenhagen, Universitetsparken 5, DK-2100 København Ø, Denmark.
authors.forename: Lars H
authors.initials: LH
authors.lastname: Øgendal
authors.affiliation: Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark. Electronic address: vor@food.ku.dk.
authors.forename: Vibeke
authors.initials: V
authors.lastname: Orlien
mesh_terms: D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D006860:Hydrogen Bonding; D008460:Meat / Q000032:analysis*; D009124:Muscle Proteins / Q000737:chemistry*; D009218:Myosins; D011312:Pressure / Q000009:adverse effects*; D000069466:Red Meat; D012995:Solubility; D019265:Spectroscopy, Near-Infrared / Q000379:methods*; D013552:Swine; D014867:Water / Q000737:chemistry
chemical_list: D009124:Muscle Proteins; D014867:Water; D009218:Myosins
keywords: High pressure; LF-NMR; Myofibrillar proteins; NIR; Protein functionality; Protein structure modification; SDS PAGE; SEC-LS