Abstract：
:As the most important tenderness related protein in mammal, there are few studies on how the nanoscale morphology of collagen I in tissues is related to traditional meat processing. The ultrastructure and mechanical characteristics of collagen fibers in tendon with different treatments have been explored in this study. Collagen fibers in homogenate group and acetic acid group were treated with ultrasound and thermal treatment. The nanoscale morphology of collagen fiber in homogenate group became granular at 60 °C and gelatin was formed at 70 °C. The collagen fibers extracted from acetic acid are unstable and easier to break under the same processing parameters, when compared with homogenated collagen fibers in both ultrasound and thermal treatment. The results suggested that acetic acid can disassemble the salt bond and Schiff-base in collagen, and the collagen fibers became loose but the triple helix structure remained integrity.
journal_name
Food Chemjournal_title
Food chemistryauthors
Wan Y,Gao Y,Shao J,Tumarbekova A,Zhang D,Zhu Jdoi
10.1016/j.foodchem.2020.128985subject
Has Abstractpub_date
2021-01-09 00:00:00pages
128985eissn
0308-8146issn
1873-7072pii
S0308-8146(20)32869-7journal_volume
347pub_type
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