Preparation of immobilized NAD glycohydrolase from Neurospora crassa conidia by hydrophobic interaction--characteristics of the enzyme derivative.
作者： M. Pace , D. Agnellim , P. G. Pietta , A. Cocilovo , L. Bonizzi
DOI: 10.1080/10826068408070640
关键词: Hydrolase 、 Hydrophobic effect 、 Sepharose 、 Ionic strength 、 NAD+ kinase 、 Neurospora crassa 、 Stereochemistry 、 NAD+ nucleosidase 、 Chemistry 、 Enzyme
摘要: Abstract NAD glycohydrolase from Neurospora crassa conidia has been immobilized by hydrophobic interaction on Sepharose beads coated with propyl residues through CNBr activation. The bond resulted stable under a wide range of conditions (ionic strength, temperature, pH). As result immobilization the pH optimum for catalytic activity shifted about 0.2 unit in acidic direction, to lie between 7.5 and 7.3. stability enzymatic was largely enhanced effect but K value towards NAD+ increased compared that free enzyme (1×10−3 2×10−4 M respectively).
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