Stabilization of Fish Protein-Based Adhesive by Reduction of Its Hygroscopicity.

Abstract

Protein-based fish adhesives have historically been used in various bonding applications; however, due to the protein's high affinity for water absorption, these adhesives become destabilized in high-moisture environments, resulting in reduced bondline strength and early failure. This limitation makes them unsuitable for industrial applications with higher demands. To address this issue, water-insoluble raw powder materials such as iron, copper, or zeolite were incorporated into natural fish adhesives. In this study, the hygroscopicity, dry matter content, thermal analysis (TGA/DSC), FT-IR spectroscopy, surface tension measurements, vapour permeability, and scanning electron microscope (SEM) of the modified adhesives were determined. In addition, the bonding properties of the modified adhesives were evaluated by the tensile shear strength of the lap joints, and mould growth was visually inspected. The resulting modified protein-based adhesives demonstrated improved stability in high humidity environments. Enhancing the hygroscopic properties of protein-based fish adhesives has the potential to unlock new opportunities and applications, providing a healthier and more environmentally sustainable alternative to petroleum-based adhesives.