Though hydrophobic adhesives designed for underwater use are often sought after for their capacity to displace water from surfaces, their natural incompatibility with water can impede their application. Adhesive systems based on water can enhance wetting properties, reduce toxicity, and show responsive physical behavior to aqueous environments. In the case of protein-based adhesives, basic aqueous salts can significantly influence the forces at play between proteins and surfaces, both intra- and intermolecularly. This study examines the impact of four primary salts present in seawater—NaCl, KCl, MgCl2, and CaCl2—on underwater curing adhesives derived from two agricultural byproduct proteins: bovine serum albumin and bovine lactalbumin. Our findings reveal that salts can markedly affect the adhesion properties of protein-based adhesives, boosting bond strength at moderate salt levels while diminishing it at elevated concentrations. Experimental results indicate that high ionic strengths accelerate gelation, resulting in weaker materials with lower adhesion, whereas moderate salt concentrations slow down protein aggregation, yielding stiffer materials with enhanced bond strengths. The incorporation of silica fillers enhanced the bond strength of salt-infused gels but reduced the bond strength of bovine serum albumin gels. Generally, salts that reinforced the structural integrity of native proteins contributed to the formation of stiffer gel networks but often reduced adhesion compared to salts that had destabilizing effects. By combining simple salts with protein-based adhesives, we illustrate the ability to manipulate nearly all aspects of adhesive curing and strength, serving as an effective strategy to enhance underwater adhesion.

S.K.S.C.NADARAJAN & BROR.
Salt company since 1942
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