Abstract:
:The structural changes and aggregation properties of silver carp actomyosin acidified with d-gluconic acid-δ-lactone (GDL) were investigated. Results showed that silver carp actomyosin underwent aggregation and formation of precipitate as indicated by turbidity and centrifugation coupled electrophoresis analysis. Circular dichroism indicated that myosin rod unfolded during acidification, resulting in a gradual decrease in α-helical content. The changes in tertiary structure of actomyosin under acidic conditions were demonstrated by second-derivative UV spectra and intrinsic fluorescence. Tyrosine residues were exposed to the surface of proteins when pH was decreased to 5.5, and were buried inside the protein aggregates with further reduction in pH. In contrast, more tryptophan residues were exposed to the polar environment with decreasing pH. 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide crosslinking experiments showed that the intensity of myosin heavy chain (MHC) bands decreased sharply with decreasing pH and the actin bands decreased more slowly, suggesting that MHC is the major protein component involved in the non-covalent cross-linking and formation of aggregates during acidification of silver carp actomyosin.
journal_name
Food Chemjournal_title
Food chemistryauthors
Xu Y,Xia W,Jiang Qdoi
10.1016/j.foodchem.2012.02.216subject
Has Abstractpub_date
2012-09-15 00:00:00pages
1005-10issue
2eissn
0308-8146issn
1873-7072pii
S0308-8146(12)00438-4journal_volume
134pub_type
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