Microperoxidase-11(MP-11) has been immobilized for the first time in hybrid periodic mesoporous organosilica (PMO) materials and in a nano-crystalline metal organic framework (MOF). Microperoxidase-11 was physically absorbed from solution into the periodic mesoporous organosilica MBS and functionalized derivatives of MBS as well as in the 3-dimensional [Cu(OOC-C 6 H 4 -C 6 H 4 -COO)AE½ C 6 H 12 N 2 ] n metal organic framework. The conversion of Amplex Ò UltraRed and methylene blue to their respective oxidation products by immobilized MP-11 was determined.

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In this study we explored the efficiency of the additive methyl-beta-cyclodextrin (M beta CD) to enhance the activity and enantioselectivity of the serine protease subtilisin Carlsberg in organic solvents. These two parameters, measured for different transesterification reactions and in several solvents, are compared with results obtained by using two additional preparations of the same enzyme: lyophilized powder and cross-linked enzyme crystals (CLEC). The results suggest that co-lyophilization of subtilisin with M beta CD preserves the enzyme's active site tertiary structure rendering a highly active and enantioselective catalyst.

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