Effects Of Na+, Ca2+ And Ph Value On Thermal Denaturation Temperature Of Whale Shark Skin Collagen
Keywords
Collagen, Thermal Denaturation Temperature, Uv Absorption Spectrum, Aggregation Kinetics Curve, Differential Scanning Calorimetry Analysis
Abstract
The effects of different concentrations of Na+, Ca2+ and pH on the thermal denaturation temperature of whale shark skin type I collagen and whale shark skin type II collagen were systematically studied by differential scanning calorimetry (DSC). The characteristic ultraviolet absorption wavelength of type I collagen is located at 233.05nm, and the characteristic ultraviolet absorption wavelength of type II collagen is located at 232.90nm and 277.88nm. Studying the aggregation kinetics curve of collagen, it was found that the turbidity changes of whale shark type I collagen and whale shark type II collagen over time showed an S-shaped trend. The aggregation process can be divided into initial stage, growth stage and stabilizing stage. The thermal stability of whale shark type I collagen and whale shark type II collagen was characterized by a high-sensitivity differential calorimetry scanner. The thermal denaturation temperature of whale shark type I collagen is 40¡ãC, and the thermal denaturation temperature of whale shark type II collagen is 62¡ãC. Lower concentrations of Na+ and Ca2+ reduce the thermal denaturation temperature of type I collagen and type II collagen. This may be due to the addition of metal ions affecting the mutual repulsion of charged amino acid residues between collagen molecules, reducing the collagen denaturation temperature. Thermal stability of protein; higher concentrations of Na+ and Ca2+ continuously reduce the denaturation temperature of type I collagen and type II collagen. This may be due to the competition between metal ions and collagen molecules for water molecules, resulting in collagen instability. ; When the concentration of Na+ and Ca2+ metal ions continues to increase, the denaturation temperature of type I collagen and type II collagen increases due to salting out. After type I collagen is treated with strong acid and alkali, the endothermic denaturation peak of the protein becomes smaller or even disappears.
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Original research was done by Bao Bin, Wu Wenhui, Kang Junxia, Kang Yongfeng, Xie Jing, Chen Zhihua
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