Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 131, Issue 18, Pages 6549-6553Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja900786z
Keywords
-
Categories
Funding
- Ministry of Education, Science, Sports, and Culture [20106011]
- [18200033]
- Grants-in-Aid for Scientific Research [20106011] Funding Source: KAKEN
Ask authors/readers for more resources
Proteins have evolved to acquire highly specialized biological functions and are ideal for various applications in both medicine and biotechnology, although denaturation is one of the major problems in protein chemistry. Here, we show a novel strategy for the regulation and preservation of the enzymatic activity. even after heat treatment by the complex formation with a cationic smart copolymer, poly(N,N-diethylaminoethyl methacrylate)-graft-poly(ethylene glycol) (PEAMA-g-PEG). PEAMA-g-PEG suppressed the enzymatic activity of lysozyme completely without any conformational change, indicating complex formation and the capping of the active site of lysozyme by PEAMA-g-PEG. The addition of an anionic polymer, poly(acrylic acid) (PAAc), recovered the inhibited enzymatic activity of the lysozyme/PEAMA-g-PEG complex completely. Surprisingly, even after heating the lysozyme with PEAMA-g-PEG for 20 min at 98 degrees C, the addition of PAAc recovered 80% enzymatic activity of lysozyme. Circular dichroism (CD) spectral analysis clearly indicated that the irreversible inactivation of lysozyme induced by the heat treatment was suppressed by the complex formation with PEAMA-g-PEG.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available