Effects Of Amino Acid Composition And Solvent Environment On The Thermal Stability Of Freshwater Fish Collagen
Keywords
Collagen Thermal Stability Amino Acids Ionic Strengthcollagen Thermal Stability Amino Acids Ionic Strength
Abstract
This article explores the effects of amino acid composition, distribution and solvent environment on the thermal stability of fish-derived collagen protein. Using collagen from different fish species as experimental samples, the amino acid composition and thermal denaturation temperature of collagen were measured. Through correlation analysis, the main amino acid types and distribution indicators that affect the thermal denaturation temperature of collagen were clarified. The results show that the proline hydroxylation rate, basic amino acids, charged polar amino acids and total polar amino acid contents in collagen are positively correlated with the thermal denaturation temperature of collagen, while the contents of imino acids and non-polar amino acids are positively related to the thermal denaturation temperature of collagen. Denaturation temperature was negatively correlated (p<0.01). Using the stepwise multiple regression analysis method, a mathematical model of the correlation between the proline hydroxylation rate, charged polar amino acids and the thermal denaturation temperature of collagen was established. It has been verified that this model can better predict the quality of fish-derived collagen. Thermal denaturation temperature. On this basis, the influence of the solvent environment of collagen on its thermal stability was further studied. The results show that increasing the degree of infiltration of water molecules into collagen and the ionic strength of the system, or lowering the pH of the system will significantly reduce the thermal stability of collagen. Collagen was extracted from different species of grass carp and used to study amino acid compositions and thermal stability. The result of a correlation analysis between the amino acid compositions and denaturation temperatures of various collagens showed that the degree of hydroxylation of proline, the content of alkaline amino acids, polar amino acids with charge, and total polar amino acids were positively correlated with the denaturation temperature for collagen. However, the content of imino acids and nonpolar amino acids showed an inverse correlation with the denaturation temperature (p < 0.01). mathematical model of correlation between amino acid distribution and denaturation temperature of collagen was established by step-wise regression analysis using SAS software, which accurately forecasts the denaturation temperature of fish collagen. At the same time, the influence of solvent environment, including infiltration degree of water, pH, ionic strength, and ion species, on the thermal stability of fish collagen was investigated. The results showed that the thermal stability of fish collagen underwent a remarkable decrease with increase in the infiltration degree of water and ionic strength as well as a decrease in pH of the solvent. For further information of this article and research, feel free to contact our team for asssitance. Original research was done by Deng Mingxia
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