Adsorption of pepsin in octadecylamine matrix at air-water interface.
The incorporation/entrapment of water-soluble surface-active enzyme, pepsin (PEP) within an insoluble cationic octadecylamine (ODA) monolayer is studied by Langmuir-Blodgett technique. The observation suggests that the incorporation of PEP is less preferable at compressed region (~30mN/m). The electrostatic interaction plays a significant role for the greater incorporation of PEP in cationic ODA monolayer. The surface pressure-area isotherms along with FE-SEM analysis indicates the squeezing out of PEP from the monolayer at higher surface pressure. This will assist to select the optimum surface pressure to obtain a good quality and well-ordered Langmuir monolayer. FTIR study of amide bands together with FE-SEM imaging of ODA-PEP mixed film indicates that ODA perturbs the PEP by the increment of beta-structure resulting into larger unfolding, intra, and intermolecular aggregates.
Kamilya
Tapanendu
T
Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
Pal
Prabir
P
Talapatra
G B
GB
D000327:Adsorption; D000388:Air; D000588:Amines / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry; D007700:Kinetics; D008855:Microscopy, Electron, Scanning; D010434:Pepsin A / Q000737:chemistry*; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D000588:Amines; D004800:Enzymes, Immobilized; D014867:Water; D010434:Pepsin A; C009317:stearylamine