Cellulase immobilization on Fe 3 O 4  and characterization | Zendy

Garcia Albert | Zendy; Oh Sangha | Zendy; Engler Cady R. | Zendy

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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.

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