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Molecularly Imprinted Polymer‐Assisted Refolding of Lysozyme
Author(s) -
Haruki Mitsuru,
Konnai Yoshihiro,
Shimada Ayumi,
Takeuchi Hirofumi
Publication year - 2007
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp070130c
Subject(s) - lysozyme , chemistry , acrylamide , methacrylate , yield (engineering) , methacrylic acid , chymotrypsinogen , molecularly imprinted polymer , polymer , folding (dsp implementation) , biochemistry , polymer chemistry , organic chemistry , trypsin , enzyme , monomer , chymotrypsin , materials science , selectivity , catalysis , metallurgy , electrical engineering , engineering
For production of active proteins using heterologous expression systems, refolding of proteins from inclusion bodies often creates a bottleneck due to its poor yield. In this study, we show that molecularly imprinted polymer (MIP) toward native lysozyme promotes the folding of chemically denatured lysozyme. The MIP, which was prepared with 1 M acrylamide, 1 M methacrylic acid, 1 M 2‐(dimethylamino)ethyl methacrylate, and 5 mg/mL lysozyme, successfully promoted the refolding of lysozyme, whereas the non‐imprinted polymer did not. The refolding yield of 90% was achieved when 15 mg of the MIP was added to 0.3 mg of the unfolded lysozyme. The parallel relationship between the refolding yield and the binding capacity of the MIP suggests that MIP promotes refolding through shifting the folding equilibrium toward the native form by binding the refolded protein.