title: Gelation properties of myofibrillar protein under malondialdehyde-induced oxidative stress.
abstract: BACKGROUND
  The structure of myofibrillar protein (MP) can be readily altered by oxidation, leading to the unfolding of MP structure, which further promotes protein-protein interactions, and thus influences the MP gelling properties. The objective of the study was to investigate the effect of malondialdehyde-induced oxidative stress on the gelation properties of myofibrillar protein (MP). Structural changes of the oxidised MPs were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. The oxidative stability of the MP gels as indicated by lipid hydroperoxide was also determined.
  
  
  RESULTS
  With the addition of an MDA concentration less than 10 mmol L-1, the MP gels showed an improved elasticity, gel strength, water holding capacity, and oxidative stability. Nevertheless, higher MDA concentration (25-50 mmol L-1) significantly reduced the gel quality, probably due to the formation of excessive covalent bonds in the system.
  
  
  CONCLUSIONS
  Results suggested that protein aggregation occurred in the oxidised system. Myosin was involved in gel formation through non-disulfide covalent bond. © 2016 Society of Chemical Industry.
authors.affiliation: State Key Laboratory of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu, China.
authors.forename: Lin
authors.initials: L
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu, China.|Jiangsu Province Key Laboratory of Advanced Food Manufacturing Equipment and Technology, Jiangnan University, China.
authors.forename: Min
authors.initials: M
authors.lastname: Zhang
authors.affiliation: School of Public Health, Curtin University, Bentley, Western Australia, WA 6102, Australia.
authors.forename: Zhongxiang
authors.initials: Z
authors.lastname: Fang
authors.affiliation: School of Agriculture and Food Sciences, University of Queensland, Brisbane, QLD, Australia.
authors.forename: Bhesh
authors.initials: B
authors.lastname: Bhandari
mesh_terms: D000818:Animals; D002347:Carps; D029941:Fish Proteins / Q000737:chemistry*; D005782:Gels / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008315:Malondialdehyde / Q000737:chemistry*; D009124:Muscle Proteins / Q000737:chemistry*; D009210:Myofibrils / Q000737:chemistry*; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D012212:Rheology
chemical_list: D029941:Fish Proteins; D005782:Gels; D009124:Muscle Proteins; D008315:Malondialdehyde
keywords: gelation; malondialdehyde; myofibrillar protein; protein oxidation