β-Galactosidase Langmuir Monolayer at Air/X-gal Subphase Interface

Abstract

This article investigates the surface chemistry properties of the β-galactosidase monolayer at the air-subphase interface at the vicinity of its substrate, X-gal. We have demonstrated that the β-galactosidase in the monolayer form remained active and performed hydrolysis of the X-gal in the subphase. We investigated the β-galactosidase Langmuir monolayer in absence and presence of X-gal in the subphase of varying concentration of X-gal with the sodium chloride solution. It was found that the limiting molecular area as well as the collapse surface pressure kept on decreasing with the increasing concentration of X-gal. In accordance to the data obtained from the isotherm it was also found that β-galactosidase forms a stable monolayer that does not aggregate at the air-subphase interface. The stability of the monolayer at the air-subphase interface was studied by using compression-decompression cycles with and without X-gal at varying concentration and different surface pressures. The infrared reflection-absorption spectroscopy (IRRAS) and Brewster angle microscopy (BAM) of β-galactosidase Langmuir monolayer was also investigated for pure and mixed β-galactosidase at the air-subphase.

Carbon Dots: Diverse Preparation, Application, and Perspective in Surface Chemistry

“…Previously, we studied the surface properties of an enzyme, β-galactosidase, at the air−water interface. 80 We were interested in the surface properties of the conjugate of the β-galactosidase and CDs. We used the Langmuir monolayer technique to comprehend the surface properties of the conjugated enzyme.…”

“…The conjugation of NPs with protein/enzyme molecules, in recent years, to achieve unique properties has attracted many researchers, but the conjugation of CDs with enzymes has not been performed so far. Previously, we studied the surface properties of an enzyme, β-galactosidase, at the air–water interface . We were interested in the surface properties of the conjugate of the β-galactosidase and CDs.…”

Conjugation of Carbon Dots with β-Galactosidase Enzyme: Surface Chemistry and Use in Biosensing

“…This can be explained in such a way that the free residual amount of CDs were desorbed in the subphase as the CDs are highly hydrophilic. Furthermore, CDs bonded with enzyme in the conjugate monolayer also remained immersed on the subphase as only hydrophobic component of the analyte remains projected in the air at the air/subphase interface [32].…”

Interfacial Behavior of Fumonisin B1 Toxin and Its Degradation on the Membrane

“…21 Surface chemistry study is a powerful tool to mimic the interaction of the analyte with the cell membrane. 22 Further, the surface chemistry study approach via the Langmuir monolayer technique facilitates the study of cell adhesion and its implications. This is very important as most mammalian cells are adherent.…”

“…Fungal pathogens have a variety of adhesins that can interact with native cell proteins and glycoproteins . Surface chemistry study is a powerful tool to mimic the interaction of the analyte with the cell membrane . Further, the surface chemistry study approach via the Langmuir monolayer technique facilitates the study of cell adhesion and its implications.…”