TY - JOUR
T1 - Catalytic activity of acetylcholinesterase immobilized on mesoporous molecular sieves
AU - Rosales-Hernández, M. C.
AU - Mendieta-Wejebe, J. E.
AU - Correa-Basurto, J.
AU - Vázquez-Alcántara, J. I.
AU - Terres-Rojas, E.
AU - Trujillo-Ferrara, J.
N1 - Funding Information:
The authors thank IMP, CONACYT, and COFAA-SIP/IPN for financial support to Laboratory of Characterization of Materials from IMP, Mexico.
PY - 2007/4/10
Y1 - 2007/4/10
N2 - MCM-41 and FSM-16 were used for enzyme immobilization on account of their good physical and chemical properties. In this work, the catalytic activity of acetylcholinesterase (AChE) immobilized on these materials was investigated, using neostigmina as AChE inhibitor. The results show that AChE was adsorbed on MCM-41 and on FSM-16-TIPB. AChE immobilized on the latter material maintained 70% of its activity and the material did not hydrolyze ACh (as MCM-41) by itself. Therefore, FSM-16-TIPB was the best material, considering also that when neostigmine was applied to AChE immobilized on FSM-16-TIPB, the activity of AChE decreased as occurs in its free from. Hence, this model could be useful in the evaluation of different kinds of AChE inhibitors, allowing the recycling of enzymes and making possible several assays and thereby, lowering cost.
AB - MCM-41 and FSM-16 were used for enzyme immobilization on account of their good physical and chemical properties. In this work, the catalytic activity of acetylcholinesterase (AChE) immobilized on these materials was investigated, using neostigmina as AChE inhibitor. The results show that AChE was adsorbed on MCM-41 and on FSM-16-TIPB. AChE immobilized on the latter material maintained 70% of its activity and the material did not hydrolyze ACh (as MCM-41) by itself. Therefore, FSM-16-TIPB was the best material, considering also that when neostigmine was applied to AChE immobilized on FSM-16-TIPB, the activity of AChE decreased as occurs in its free from. Hence, this model could be useful in the evaluation of different kinds of AChE inhibitors, allowing the recycling of enzymes and making possible several assays and thereby, lowering cost.
KW - AChE
KW - Catalytic activity
KW - FSM-16
KW - Immobilization
KW - MCM-41
UR - http://www.scopus.com/inward/record.url?scp=33847094251&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2006.11.004
DO - 10.1016/j.ijbiomac.2006.11.004
M3 - Artículo
C2 - 17208293
SN - 0141-8130
VL - 40
SP - 444
EP - 448
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
IS - 5
ER -