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Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins
Author(s) -
Wang Zhaoming,
He Zhifei,
Gan Xiao,
Li Hongjun
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13878
Subject(s) - chemistry , myofibril , circular dichroism , sodium dodecyl sulfate , gel electrophoresis , polyacrylamide gel electrophoresis , radical , protein aggregation , chromatography , sodium , biochemistry , enzyme , organic chemistry
Summary We investigated the effect of peroxyl radicals (ROO·), which are products of lipid peroxidation, on the structure and gel properties of myofibrillar proteins (MPs) isolated from rabbit meat. 2,2′‐Azobis(2‐amidinopropane) dihydrochloride (AAPH) was heated to stably derive ROO·. As the AAPH concentration increased, the protein carbonyl compounds significantly accumulated ( P < 0.05), and the total sulfhydryl content was significantly lost ( P < 0.05). Circular dichroism spectra, UV absorption spectra, intrinsic fluorescence spectra and surface hydrophobicity revealed that ROO· caused protein unfolding and conformational changes in MPs. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) analysis indicated that moderate (0–3 m m ) and relatively high (5 and 10 m m ) AAPH concentrations could lead to protein crosslinking and protein aggregation, respectively. These changes in protein structure could influence the gelling properties of MPs. Low‐level protein oxidation could increase gel strength and water holding capacity, whereas high‐level protein oxidation could reduce gel properties.