title: Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein.
abstract: The objective of the study was to examine how oxidatively induced protein cross-linking would influence the gelation properties of myofibrillar protein (MP) under meat processing conditions. MP suspensions in 0.6 M NaCl at pH 6 were treated with an iron-catalyzed oxidizing system (IOS: 10 microM FeCl(3), 0.1 mM ascorbic acid, 0.05 to 5 mM H(2)O(2)) or a H(2)O(2)-activated metmyoglobin oxidizing system (MOS: 0.01 to 0.1 mM metmyoglobin/H(2)O(2)) that produced hydroxyl radical and ferryl species, respectively. Both oxidizing systems promoted MP thermal gelation, which was evidenced by rapid protein-protein interaction and the enhancement in storage modulus (elasticity) of the gel network as revealed by dynamic rheological testing in the 20 to 74 degrees C temperature range. This gelation-enhancing effect was attributed to the shift of myosin aggregation in the early stage of heating from predominantly head-head association (nonoxidized control samples) to prevalently tail-tail cross-linking through disulfide bonds. However, both hardness and water-holding capacity of chilled gels tended to decline when MP was exposed to >or=1 mM H(2)O(2) in IOS and to all concentrations of metmyoglobin in MOS. Microscopic examination confirmed a more porous structure in oxidized gels when compared with nonoxidized protein gels. The results demonstrated that mild oxidation altered the mode of myosin aggregation in favor of an elastic gel network formation, but it did not improve or had a negative effect on water-binding properties of MP gels.
  
  
  CONCLUSIONS
  Mild oxidation promotes protein network formation and enhances gelation of myofibrillar protein under normal salt and pH conditions used in meat processing. This oxidative effect, which involves disulfide linkages, is somewhat similar to that in bakery product processing where oxidants are used to improve dough performance through gluten protein interaction.
authors.affiliation: Dept. of Animal and Food Sciences, Univ. of Kentucky, Lexington, KY 40546, USA. ylxiong@uky.edu
authors.forename: Youling L
authors.initials: YL
authors.lastname: Xiong
authors.forename: Suzanne P
authors.initials: SP
authors.lastname: Blanchard
authors.forename: Tooru
authors.initials: T
authors.lastname: Ooizumi
authors.forename: Yuanyuan
authors.initials: Y
authors.lastname: Ma
mesh_terms: D000818:Animals; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D005511:Food Handling; D005524:Food Technology; D005782:Gels / Q000378:metabolism*; D017665:Hydroxyl Radical / Q000378:metabolism*; D008786:Metmyoglobin / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D009210:Myofibrils / Q000378:metabolism*; D010084:Oxidation-Reduction; D011489:Protein Denaturation; D012212:Rheology / Q000379:methods; D013552:Swine
chemical_list: D003432:Cross-Linking Reagents; D005782:Gels; D008786:Metmyoglobin; D017665:Hydroxyl Radical