Aggregation Behavior of Acylated Pepsin-Solubilized Collagen Based on Fluorescence Spectrum Technology

Abstract

The aggregation behavior of collagen-based materials plays an important role in their processing because it could affect their physicochemical properties. Based on the intrinsic fluorescence characteristic of tyrosine, fluorescence spectrum technology was used to investigate the aggregation state of the acylated collagen molecules in aqueous solution. The results showed that the aggregate degree of the acylated collagen was higher than that of the native collagen due to the hydrophobic interaction. With the increase of concentrations of the acylated collagen or at NaCl higher than 40 mmol/L, the aggregate degree of the acylated collagen molecules increased. When the pH was close to the isoelectric point of the acylated collagen, the hydrophobic interaction and the hydrogen bond helped to increase the aggregation degree. However, with the increase of temperature (10–70 ℃), the aggregation state of the acylated collagen decreased gradually due to the quenching, the molecular collision, and the broken of hydrogen bonds. Furthermore, two-dimensional correlation spectroscopy (2D-COS) showed that the response order was 360 > 305 nm at various acylated collagen and NaCl (>40 mmol/L) concentrations, while the response order was 305 > 360 nm when the pH value was increased from 5.0 to 9.0. Temperature-dependent 2D-COS showed there were four bands that occurred and the response order was listed as follows: 293 > 305 > 360 > 420 nm. In brief, the results might provide an important guide for molding processes of the acylated collagen.