Md. Bellal Hossain
Department of Nutrition and Food Engineering, Allied Health Science, Daffodil International University, Dhanmondi R/A, Dhaka-1207, Bangladesh

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Polymeric Switch on Lysozyme Activity: Role of Hydrophobic and Electrostatic Interactions Dr. Sumon Ganguli; Md. Bellal Hossain
The Journal of Pure and Applied Chemistry Research Vol 2, No 3 (2013)
Publisher : Chemistry Department, The University of Brawijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (377.351 KB) | DOI: 10.21776/ub.jpacr.2013.002.03.148

Abstract

Enzymes have attracted potential applications in both medicine and biotechnology. In our present study, we show a strategy for switching the enzymatic activity of lysozyme by the complex formation with a cationic smart copolymer. PAMA-g-PEG graft copolymers suppressed the enzymatic activity of lysozyme without any conformational change, indicating the formation of complex and covering the active site of lysozyme by copolymers. The addition of polyanion, poly(acrylic acid) (PAAc), recovered the suppressed enzymatic activity of the lysozyme/polymer complex efficiently. These finding suggest that that hydrophobic interaction coupled with electrostatic interactions has a great role for the complexation and decomplexation of the lysozyme/polymer complex. Circular dichroism (CD) spectral analysis indicated that the conformation of the enzymes maintained largely during the course of the complexation.