Identification of Carbonylated Protein in Frozen Rainbow Trout (Oncorhynchus mykiss) Fillets and Development of Protein Oxidation during Frozen Storage
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- 作者：Inger V. H. Kjæ ; rsgå ; rd ; Mette R. N
p ; //pubs.acs.org/images/gifchars/oslash.gif" border="0">rrelykke ; Caroline P. Baron ; Flemming Jessen
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2006
- 出版时间：December 13, 2006
- 年：2006
- 卷：54
- 期：25
- 页码：9437 - 9446
- 全文大小：481K
- 年卷期：v.54,no.25(December 13, 2006)
- ISSN：1520-5118
文摘
Frozen storage of fish is known to enhance lipid oxidation, resulting in the development of anunpleasant rancid taste and odor. Frozen storage of fish is also known to reduce protein solubility,and proteins are expected to be oxidatively modified; however, these oxidative mechanisms are poorlyunderstood. Generally, protein oxidation leads to a wide range of modifications; the most studiedbeing the formation of carbonyl groups. The present work shows, by UV spectrophometricdetermination of protein carbonyl groups in rainbow trout muscle, that storage at -20 
C resulted ina 2-fold increase in protein carbonylation compared to storage at -30 or -80 C. Furthermore, low-salt-soluble proteins in fish that were either fresh or stored for 3 years at -80 C were found to havesimilar extents of carbonylation. Proteome analysis and two-dimensional immunoblotting of rainbowtrout low-salt- and high-salt-soluble proteins gave a detailed description of the protein carbonylationpattern. Several carbonylated proteins were identified by LC-MS/MS, such as nucleoside diphosphatekinase, adenylate kinase, pyruvate kinase, actin, creatine kinase, tropomyosin, myosin light chains1 and 2, and myosin heavy chain. Furthermore, the results showed a reduced solubility of nucleosidediphosphate kinase in fish stored at -20 C for 2 years compared to fish stored at -80 C. It wasobserved that low-abundant proteins could be relatively more carbonylated than high-abundantproteins, thereby indicating that some proteins are more susceptible to oxidation than others, due toeither their cellular localization, amino acid sequence, or biochemical function.
C resulted ina 2-fold increase in protein carbonylation compared to storage at -30 or -80 C. Furthermore, low-salt-soluble proteins in fish that were either fresh or stored for 3 years at -80 C were found to havesimilar extents of carbonylation. Proteome analysis and two-dimensional immunoblotting of rainbowtrout low-salt- and high-salt-soluble proteins gave a detailed description of the protein carbonylationpattern. Several carbonylated proteins were identified by LC-MS/MS, such as nucleoside diphosphatekinase, adenylate kinase, pyruvate kinase, actin, creatine kinase, tropomyosin, myosin light chains1 and 2, and myosin heavy chain. Furthermore, the results showed a reduced solubility of nucleosidediphosphate kinase in fish stored at -20 C for 2 years compared to fish stored at -80 C. It wasobserved that low-abundant proteins could be relatively more carbonylated than high-abundantproteins, thereby indicating that some proteins are more susceptible to oxidation than others, due toeither their cellular localization, amino acid sequence, or biochemical function.