| Summary: | 碩士 === 國立中央大學 === 化學工程與材料工程研究所 === 96 === Random protein immobilization usually suffers from serious loss of
the specific bioactivity of the immobilized protein. Oriented protein
immobilization of histidine tagged protein on metal chelating resin does
not guarantee 100% exposure of the active site. In this study, we develop
a new method for oriented immobilization. Design an affinity ligand
according to the characteristic and distribution of amino acids at the
opposite to the active site. The target protein is α-amylase from
Aspergillus oryzae, and the searched ligand is 3,3’,4,4’ -
Biphenyltetracarboxylic dianhydride (BPDA). We predict the possible
binding sites by using molecular dockikng. And at the experiments, we
attach BPDA to the surface of silica gel and via isotherm adsorb and
bioactivity assay show oriented immobilization owns superior specific
activity than random immobilization.
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