Adsorption of pepsin in octadecylamine matrix at air-water interface

Biophysical Chemistry
Tapanendu KamilyaG B Talapatra

Abstract

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.

References

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Sep 20, 2006·Langmuir : the ACS Journal of Surfaces and Colloids·Luciano CaseliOsvaldo N Oliveira
Feb 3, 2007·The Journal of Physical Chemistry. B·Tapanendu KamilyaG B Talapatra
Apr 10, 2007·Colloids and Surfaces. B, Biointerfaces·Tapanendu KamilyaG B Talapatra
Aug 19, 2007·Biochimica Et Biophysica Acta·Andreas Barth
Mar 27, 2009·The Journal of Physical Chemistry. B·Tapanendu KamilyaG B Talapatra
Jun 9, 2009·Colloids and Surfaces. B, Biointerfaces·Prabir PalG B Talapatra

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Citations

May 4, 2010·The Journal of Physical Chemistry. B·Mrityunjoy MahatoG B Talapatra
Dec 9, 2009·The Journal of Physical Chemistry. B·Mrityunjoy MahatoG B Talapatra
Jun 17, 2011·The Journal of Physical Chemistry. B·Bidisha TahG B Talapatra

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