TY - JOUR
T1 - Encapsulation of catalase into nanochannels of an inorganic composite membrane
AU - Itoh, Tetsuji
AU - Ishii, Ryo
AU - Hanaoka, Takaaki
AU - Hasegawa, Yasuhisa
AU - Mizuguchi, Junko
AU - Shiomi, Toru
AU - Shimomura, Takeshi
AU - Yamaguchi, Akira
AU - Kaneda, Hideaki
AU - NorioTeramae, [No Value]
AU - Mizukami, Fujio
PY - 2009/5
Y1 - 2009/5
N2 - Enzymes, especially those known as membrane proteins existing in plasma membranes, direct important and complicated reactions in living bodies. Thus, attempts have been made to extract such enzymes from living bodies, and immobilize and accumulate them on supports to effectively use their functions for catalysis [M. Hartmann, Chem. Mater. 17 (2005) 4577-4593]. However, enzymes extracted from living bodies tend to aggregate in the absence of detergents or at high concentrations, resulting in a loss of their activities [Y. Urabe, T. Shiomi, T. Itoh, A. Kawai, T. Tsunoda, F. Mizukami, K. Sakaguchi, ChemBioChem 8 (2007) 668-674]. We have, however, succeeded in assembling a highly durable membrane capable of high-density accumulation and providing a regular array of catalase by encapsulating it in mesoporous silica synthesized in the pores of an alumina membrane. The artificial biomembrane showed not only activity similar to that of the native catalase for the decomposition of H2O2 but also much higher stability; the catalase immobilized in the membrane still retained its original activity even after being employed 160 times in decomposing H2O2, whereas the native lost its activity after 40 cycles.
AB - Enzymes, especially those known as membrane proteins existing in plasma membranes, direct important and complicated reactions in living bodies. Thus, attempts have been made to extract such enzymes from living bodies, and immobilize and accumulate them on supports to effectively use their functions for catalysis [M. Hartmann, Chem. Mater. 17 (2005) 4577-4593]. However, enzymes extracted from living bodies tend to aggregate in the absence of detergents or at high concentrations, resulting in a loss of their activities [Y. Urabe, T. Shiomi, T. Itoh, A. Kawai, T. Tsunoda, F. Mizukami, K. Sakaguchi, ChemBioChem 8 (2007) 668-674]. We have, however, succeeded in assembling a highly durable membrane capable of high-density accumulation and providing a regular array of catalase by encapsulating it in mesoporous silica synthesized in the pores of an alumina membrane. The artificial biomembrane showed not only activity similar to that of the native catalase for the decomposition of H2O2 but also much higher stability; the catalase immobilized in the membrane still retained its original activity even after being employed 160 times in decomposing H2O2, whereas the native lost its activity after 40 cycles.
KW - Artificial biomembrane
KW - Catalase
KW - Mesoporous silica
KW - Porous alumina membrane
KW - Silica nanochannel
UR - http://www.scopus.com/inward/record.url?scp=68649096163&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=68649096163&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2008.08.014
DO - 10.1016/j.molcatb.2008.08.014
M3 - Article
AN - SCOPUS:68649096163
VL - 57
SP - 183
EP - 187
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
SN - 1381-1177
IS - 1-4
ER -