Effect of heat treatment on the enzymatic stability of grass carp skin collagen and its ability to form fibrils in vitro.
BACKGROUND
The molecular configuration, molecular weight distribution and thermal transition enthalpy (ΔH) of grass carp skin (GCS) collagens after heat treatment under different conditions were measured using circular dichroism, gel filtration chromatography and differential scanning calorimetry (DSC). The enzymatic stability of collagen was evaluated using different enzymes, while the ability to form fibrils in vitro was assessed by morphological observation of collagen fibrils and turbidity testing.


RESULTS
The ΔH values, in-solution molecular aggregation and the stability to enzymatic hydrolysis of GCS collagen decreased irreversibly and progressively with the duration of heat treatment at 33 °C, which was the onset endothermic temperature obtained from the DSC curve. A strong positive linear correlation between the enzymatic sensitivity of collagen and the degree of thermal denaturation was found. A decrease in fibril diameter and D-periodicity length with denaturation could also be observed in the SEM and TEM images.


CONCLUSION
The onset endothermic temperature (To ) rather than the denaturation temperature (Td ) is the threshold temperature for configurational stability of GCS collagen in acidic solution, and the biological properties would obviously change if the collagen was heat treated at this temperature.
['Yang|Huan|H|', 'Wang|Haibo|H|', 'Zhao|Yan|Y|', 'Wang|Haiyin|H|', 'Zhang|Hanjun|H|']
D000143:Acids D000818:Animals D001672:Biocompatible Materials D002152:Calorimetry, Differential Scanning D002347:Carps D002942:Circular Dichroism D003094:Collagen D004798:Enzymes D005109:Extracellular Matrix D029941:Fish Proteins D006358:Hot Temperature D006868:Hydrolysis D066298:In Vitro Techniques D011489:Protein Denaturation D012867:Skin D012996:Solutions D013816:Thermodynamics
heat treatment enzymatic stability grass carp collagen self-assembly