Publication: Covalent immobilization of a glucoamylase to bagasse dialdehyde cellulose
Issued Date
2001-12-31
Resource Type
ISSN
09593993
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2-s2.0-0035206729
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Mahidol University
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SCOPUS
Bibliographic Citation
World Journal of Microbiology and Biotechnology. Vol.17, No.7 (2001), 721-725
Suggested Citation
S. Varavinit, N. Chaokasem, S. Shobsngob Covalent immobilization of a glucoamylase to bagasse dialdehyde cellulose. World Journal of Microbiology and Biotechnology. Vol.17, No.7 (2001), 721-725. doi:10.1023/A:1012984802624 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/26423
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Title
Covalent immobilization of a glucoamylase to bagasse dialdehyde cellulose
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Abstract
Cellulose fibres from bagasse were oxidized by sodium periodate in sulphuric acid media at positions 2 and 3 of the anhydroglucose unit to produce dialdehyde cellulose. The aldehyde groups of the dialdehyde cellulose were able to react with amino groups of a glucoamylase to form covalent bonds and result in a dialdehyde cellulose immobilized enzyme. The optimum pH of this immobilized enzyme and free enzyme were in the range of 3.0-5.0 and 3.5-5.0, respectively. The optimum temperature for both the free and immobilized enzymes was 60-65°C. The relative remaining activity of the immobilized enzyme was 36% and its stability was very good, since it could be reused for over 30 cycles. Its activity decreased from the first to the seventh reuse cycles, due to the slow detachment of non-covalently bound enzyme. However, activity tended to stabilize after the seventh cycle of reuse, indicating very stable covalent binding between the enzyme and dialdehyde cellulose.