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Improvement of chloroperoxidase stability by covalent immobilization on chitosan membranes.
- Source :
-
Biotechnology letters [Biotechnol Lett] 2009 Aug; Vol. 31 (8), pp. 1269-72. Date of Electronic Publication: 2009 Apr 29. - Publication Year :
- 2009
-
Abstract
- Chloroperoxidase (CPO) from Caldariomyces fumago was optimally covalently immobilized on chitosan membranes pretreated with 0.8 M glutaraldehyde at pH 3.5 to give 3.18 mg CPO g(-1) support. Using monochlorodimedone (MCD) as assay substrate, the immobilized-CPO retained 40% activity at 50 degrees C after 40 min whereas free CPO retained only 0.02%. The residual activity for immobilized-CPO was 99 and 58% compared with 68 and 43% for free CPO in the presence of 1.5 M urea and 300 microM H(2)O(2), respectively, after 20 h.
- Subjects :
- Chloride Peroxidase chemistry
Chloride Peroxidase isolation & purification
Cyclohexanones metabolism
Enzyme Stability
Enzymes, Immobilized chemistry
Hot Temperature
Time Factors
Ascomycota enzymology
Chitosan metabolism
Chloride Peroxidase metabolism
Enzymes, Immobilized metabolism
Membranes enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1573-6776
- Volume :
- 31
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Biotechnology letters
- Publication Type :
- Academic Journal
- Accession number :
- 19404743
- Full Text :
- https://doi.org/10.1007/s10529-009-0009-2