Biochemical study of type I collagen purified from skin of warm sea teleost Mahi mahi (Coryphaena hippurus), with a focus on thermal and physical stability
Monami Akita, Toshio Kono, Kento Lloyd, Toshiyuki Mitsui, Katsuji Morioka, Kohsuke Adachi
Journal of Food Chemistry
Acid‐ and pepsin‐soluble collagen were purified from the skin of mahi mahi (mmASC and mmPSC). The Pro+Hyp content of the latter (185/1,000 residues) was highest among all marine teleost fishes. Fourier transform infrared spectroscopy and Circular Dichroism (CD) analysis showed the typical structure of type I collagen. The ratio of positive over negative peak intensity calculated from the CD spectrum was approximately 1.19 in mmPSC, which is remarkably high, and indicates the stability of the triple helix. The denaturation temperatures (Td) of mmASC and mmPSC were the highest (29.5 and 28.8°C, respectively) among the marine teleost fishes previously studied. atomic force microscope and scanning electron microscope images showed that even after pretreatment, the fibrils presented their structure and fiber orientation. These results indicate the robustness of both collagens, which can be attributed to the high value of Pro+Hyp stabilizing the helix structure of the collagen molecule.
Circular dichroism, Protein structure, Thermal stability, Agriculture and environmental, Biochemistry