Premium
Chemical interaction between the immobilized enzymes on Cu‐MCM41 determinated by EPR
Author(s) -
Rosaleshernandez Martha cecilia,
TerresRojas Eduardo,
RamirezRosales Daniel,
Kispert Lowell
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.682.4
Subject(s) - electron paramagnetic resonance , chemistry , molecular sieve , substrate (aquarium) , enzyme , peroxidase , mcm 41 , mesoporous material , catalysis , organic chemistry , physics , oceanography , nuclear magnetic resonance , geology
MCM‐41 is a member of a family of mesoporous molecular sieves, it has been used for the proteins immobilizations such as cytochrome c, papina, tripsina, cytochrome P‐450 and peroxidase. The incorporation of different transition metal ions such as Al +3 , Cu +2 , Ti +4 y V into the framework of MCM‐41 changes their physico‐chemical properties such as the electron transfer efficiency between embedded molecules and the material MCM‐41 However, the importance of these metals over the material surface during the enzyme immobilization process has been not studied enough which could be of great importance. Therefore, the main of this work is to immobilize peroxidase, acetilcholinesterase and cytocrome P‐450 2B4 on Cu‐MCM‐41 in order to evaluate their catalytic activity and the interaction between the enzymes and Cu +2 by using EPR studies. The EPR results showed that copper reacts with NH 3 groups from aminoacids of the enzyme such as Lysin and Arginine which are found in its surface and this allow to immobilize the enzyme as an uni‐directional manner allow to the optimal substrate access and product egress.