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Cellulase immobilization on Fe 3 O 4 and characterization
Author(s) -
Garcia Albert,
Oh Sangha,
Engler Cady R.
Publication year - 1989
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260330311
Subject(s) - cellulase , chemistry , enzyme , immobilized enzyme , molecular mass , ligand (biochemistry) , chromatography , enzyme assay , specific activity , nuclear chemistry , biochemistry , receptor
A successful procedure for attaching cellulase to 45 μm iron oxide particles with a high‐molecular‐weight (1000) ligand has been developed. Mass and activity balances were calculated for immobilized enzymes with different loadings. The highest specific activity of the immobilized enzyme was 5.9 mmol glucose/g bound protein/h. The efficacy of retaining enzymatic activity was 128%. The optimum pH was 5.5 compared to 4.0 of the free enzyme. The half‐life of the IMC was extended to 272 h compared to 0.77 h of the free enzyme.