Springer Online Journal Archives 1860-2000
Process Engineering, Biotechnology, Nutrition Technology
Summary The ability of a recently developed affinity membrane to adsorb commercially prepared trypsin was investigated. Several buffered solutions of trypsin which varied in their initial concentrations from 62.5 mg/l to 1,000 mg/l, were passed through a stacked bed of seven membranes; dry wt 350 mgs. The adsorbed protein was eluted using acetic acid; 2.2 mgs to 5.3 mgs of trypsin was desorbed. The adsorption capacity tended to a maximum of 16 mg /g dry wt when the initial feed concentration of trypsin was 1 g/l. There was no loss in enzyme activity after desorption; 11,500 IU ± 500 IU.
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