학술논문
An Investigation into the Stability Source of Collagen Fiber Modified Using Cr(III): An Adsorption Isotherm Study
Document Type
Academic Journal
Source
Molecules (Basel). January 2024, Vol. 29 Issue 2
Subject
Language
English
ISSN
1420-3049
Abstract
Author(s): Jiheng Li [1]; Wenjun Long [2]; Liangqiong Peng (corresponding author) [1,*]; Lijun Guo [2]; Wenhua Zhang (corresponding author) [1,2,*] 1. Introduction Putrescible animal skins can be readily converted into [...]
The enhanced hydrothermal stability of leather, imparted by little Cr(III), has traditionally been ascribed to strong coordinate bonds. However, this explanation falls short when considering that the heat-induced shrinking of collagen fiber is predominantly driven by rupturing weak H-bonds. This study explored the stability source via adsorption thermodynamics using collagen fiber as an adsorbent. Eleven isotherm models were fitted with the equilibrium dataset. Nine of these models aptly described Cr(III) adsorption based on the physical interpretations of model parameters and error functions. The adsorption equilibrium constants from six models could be transformed into dimensionless thermodynamic equilibrium constants. Based on the higher R[sup.2] of the van’t Hoff equation, thermodynamic parameters (∆G°, ∆H°, ∆S°) from the Fritz–Shluender isotherm model revealed that the adsorption process typifies endothermic and spontaneous chemisorption, emphasizing entropy increase as the primary driver of Cr(III) bonding with collagen. Thus, the release of bound H[sub.2]O from collagen is identified as the stability source of collagen fiber modified by Cr(III). This research not only clarifies the selection and applicability of the isotherm model in a specific aqueous system but also identifies entropy, rather than enthalpy, as the principal stability source of Cr-leather. These insights facilitate the development of novel methods to obtain stable collagen-based material.
The enhanced hydrothermal stability of leather, imparted by little Cr(III), has traditionally been ascribed to strong coordinate bonds. However, this explanation falls short when considering that the heat-induced shrinking of collagen fiber is predominantly driven by rupturing weak H-bonds. This study explored the stability source via adsorption thermodynamics using collagen fiber as an adsorbent. Eleven isotherm models were fitted with the equilibrium dataset. Nine of these models aptly described Cr(III) adsorption based on the physical interpretations of model parameters and error functions. The adsorption equilibrium constants from six models could be transformed into dimensionless thermodynamic equilibrium constants. Based on the higher R[sup.2] of the van’t Hoff equation, thermodynamic parameters (∆G°, ∆H°, ∆S°) from the Fritz–Shluender isotherm model revealed that the adsorption process typifies endothermic and spontaneous chemisorption, emphasizing entropy increase as the primary driver of Cr(III) bonding with collagen. Thus, the release of bound H[sub.2]O from collagen is identified as the stability source of collagen fiber modified by Cr(III). This research not only clarifies the selection and applicability of the isotherm model in a specific aqueous system but also identifies entropy, rather than enthalpy, as the principal stability source of Cr-leather. These insights facilitate the development of novel methods to obtain stable collagen-based material.