Department of Experimental and Clinical Pharmacology, Medical College of Rzeszow University, The University of Rzeszow, 35-310 Rzeszow, Poland.
Department of Chemistry and Biochemistry, Brigham Young University, UT 84602, Provo, USA.
Int J Biol Macromol. 2020 Nov 15;163:833-841. doi: 10.1016/j.ijbiomac.2020.07.051. Epub 2020 Jul 9.
The study of the experimental and calculated heat capacity, C of fish collagen (silver carp) with contents of several additive components was presented. The experimental low-temperature heat capacity was measured in the temperature range of 1.85 to 302.8 K using a Quantum Design Physical Property Measurement System (PPMS) and the higher temperature C from 223.15 K to 382.15 K by Differential Scanning Calorimetry (DSC) method. For an interpretation of the experimental, low-temperature data, the vibrational heat capacity of the pure silver carp collagen was calculated based on the contribution of a sum of the vibrational heat capacity of 4248 amino acids. The vibrational heat capacity for each amino acids was taken from Advanced Thermal Analysis System (ATHAS) Data Bank for individual poly (amino acid) residues based on their group and skeletal vibrational spectra. Comparing of the experimental heat capacity of the collagen with additive components and the calculated vibrational heat capacity of the pure silver carp collagen shows that the differences range from around 10% at 100 K to 14% at 300 K temperature. Such thermal analysis can provide information about the contribution to C of unknown components or impurities in the investigated system.
本文介绍了含有几种添加剂成分的鱼胶原蛋白（白鲢）的实验和计算热容 C 的研究。使用 Quantum Design 物理性能测量系统（PPMS）在 1.85 至 302.8 K 的温度范围内测量了实验低温热容，使用差示扫描量热法（DSC）在 223.15 K 至 382.15 K 的较高温度下测量了 C。为了解释实验低温数据，基于 4248 个氨基酸的振动热容之和，计算了纯白鲢胶原蛋白的振动热容。根据其基团和骨架振动谱，从高级热分析系统（ATHAS）数据库中为每个氨基酸获取了用于单个聚（氨基酸）残基的振动热容。将含添加剂成分的胶原蛋白的实验热容与纯白鲢胶原蛋白的计算振动热容进行比较，结果表明，在 100 K 时，差异在 10%左右，在 300 K 时，差异在 14%左右。这种热分析可以提供有关未知成分或杂质对所研究系统 C 的贡献的信息。
