Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
601281 | Colloids and Surfaces B: Biointerfaces | 2011 | 10 Pages |
Abstract
⺠The kinetic study of lipolysis of mixture of substrates TC8 and DiC12PC organized as mixed monolayers by TLL or PLA2 respectively, shows an increasing of the catalytic action of TLL, while the action of PLA2 in the molecular environment of the mixture of substrates TC8 and DiC12PC is not affected. ⺠The values of Qm' for pure TC8 and Qm for pure DiC12PC were compared with these obtained for the hydrolysis in the mixed TC8/DiC12PC monolayers under the action of each of enzymes (TLL or PLA2) or of both enzymes (TLL + PLA2). ⺠A mutual inhibition effect of the catalytic activities of both TLL and PLA2 enzymes during their simultaneous action on the mixed TC8/DiC12PC substrates was observed. ⺠The studied systems illustrate the role of interactions between the all participants of the interfacial catalytic act in a more complex catalytic system closer to the “in vivo” situation.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
K. Mircheva, Tz. Ivanova, I. Panaiotov, R. Verger,