The localization of activity of immobilzed L-asparaginase by covalent binding was studied by X-ray microanalysis. Asparagine and MgCl2 served as substrate and capture agent respectively. Substrate was catalysed by immobilized L-asparaginase to produce NH3, and NH3 was captured by MgCl2 to form precipitate MgNH4PO4. Precipitae was deposited on active site of immobilized L-asparaginase. The results show that the macroporous resins of immobilized L-asparaginase has greater enzyme activity, while distribution of activated enzyme was uniform. Most of activated enzyme was immobilized on the macroporous resins. The optimum condition of localization of activity of immobilized L-asparaginase was studied.
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