Amidase activity of phosphonate analogue imprinted chymotrypsin mimics in shape-selective, substrate-specific and enantioselective amidolysis of L-phenylalanine-p-nitroanilides

作者：Mathew Divya; Thomas Benny; Devaky K S^*

来源：Journal of Molecular Catalysis A: Chemical , 2016, 415: 65-73.

DOI：10.1016/j.molcata.2016.01.029

• Molecularly imprinted enzyme mimics
• Amidase activity
• Transition state analog
• Shape-selective amidolysis
• Catalytic efficiency
• Michaelis-Menten kinetics
• Enantioselectivity
• Imprinting efficiency
• Memorized cavity

Focusing on chymotrypsin mimics, highly crosslinked enzyme mimics are synthesized by molecular imprinting technique for the amidolysis of p-nitroanilide of phenylalanine, using phenyl-1-(N-benzyloxycarbonylamino)-2-(phenyl)ethyl phosphonate the transition state analog of amidolysis as the template, N-methacryloyl-L-histidine, N-methacryloyl-L-aspartic acid, and N-methacryloyl-L-serine as the functional monomers and EGDMA as the crosslinking agent. The amidase activity of the enzyme mimics follows pseudo first order kinetics. The transition state analog provides a tetrahedral geometry complementary to the transition state intermediate, which is responsible for the catalytic activity of the imprinted enzyme mimics. The enzyme mimics show stereospecificity and substrate selectivity in the amidolysis of phenylalanine p-nitroanilide. The proper orientation of the reactive functionalities in the super crosslinked macroporous polymer matrix for selective binding of the substrate through H-bonding is responsible for the high imprinting efficiency and substrate specificity of the imprinted polymer catalysts. Low cost, ease of preparation, high thermal stability, reusability and higher shelf life make the polymer catalysts better chymotrypsin mimics.

• 出版日期2016-5-1