Abstract
Ultra-fine bubbles (UFBs) have been used in successful applications in a wide variety of fields, such as healthcare, agriculture, fisheries, food engineering, and chemical engineering. In this study, we investigated the nucleation rate of protein crystals in the presence of UFBs. It was found that UFBs induced the nucleation of trypsin and lysozyme basic proteins and reduced that of glucose isomerase and α-lactalbumin acidic proteins. The results suggest that the nucleation of proteins is influenced by the presence of UFBs. This novel approach offers insights for a better understanding of the mechanism of protein nucleation, and it provides a wide variety of possibilities for protein crystallography.
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