A novel hydrophilic support, CoFoam, for enzyme immobilization

Lipases from different sources (porcine pancreas, Mucor miehei and Candida antarctica B) were covalently immobilized on a hydrophilic polyurethane composite (CoFoam). Their hydrolytic activities assayed with tributyrin were 0.55, 2.1 and 447 U g(-1), respectively. The activity of the C. antarctica B...

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Bibliographic Details
Published in:Biotechnology letters 2004-03, Vol.26 (6), p.473-477
Main Authors: VASUDEVAN, P. T, LOPEZ-CORTES, N, CASWELL, H, REYES-DUARTE, D, PLOU, F. J, BALLESTEROS, A, COMO, K, THOMSON, T
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Bioreactors
Biotechnology
Candida - chemistry
Candida antarctica
Catalysis
Enzyme Stability
Enzymes
Enzymes, Immobilized - chemistry
Flow rates
Fundamental and applied biological sciences. Psychology
Kinetics
Lipase - chemistry
Mucor - chemistry
Mucor miehei
Pancreas - chemistry
Polyurethanes - chemistry
Pressure
Substrate Specificity
Swine
Yeast
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Summary:Lipases from different sources (porcine pancreas, Mucor miehei and Candida antarctica B) were covalently immobilized on a hydrophilic polyurethane composite (CoFoam). Their hydrolytic activities assayed with tributyrin were 0.55, 2.1 and 447 U g(-1), respectively. The activity of the C. antarctica B composite in the synthesis of methyl oleate in hexane was 8.8 U g(-1) compared to 60.6 U g(-1) for commercial Novozyme 435. The advantage of the CoFoam composite lies in the low pressure drop in a packed-bed reactor at fairly large flow rates. For example, at flow rates of 10-12 l min(-1), the pressure drop over 15 cm is typically 3 kPa.
ISSN:0141-5492
1573-6776
DOI:10.1023/B:BILE.0000019553.26201.04