Host: The Society of Chemical Engineers, Japan
Hexagonal mesoporous SBA-15-type molecular sieves with pore sizes in the range of 4.5-9.3nm have been prepared using non-ionic block copolymers. The immobilization of enzyme trypsin on SBA-15 was investigated. The amount of trypsin adsorbed in the SBA-15 was found to be related to the pore size of the SBA-15. The samples of immobilized trypsin were active for the hydrolysis of N-α-benzoyl-DL-arginine-4-nitroaniline (BAPNA). The hydrolysis activity increased with the increase of the amount of trypsin adsorbed. The relative activity, which is defined as the ratio of the activity by the immobilized enzyme to that by native enzyme, showed maximum with respect to the pore size.
