Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals
(2007) Journal of Biotechnology — Vol. 132, n° 1, p. 23-31 (2007)
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- Authors
Agathos, Spiros N. 
- Abstract
- Laccase from the white rot fungus Coriolopsis polyzona was immobilized for the first time through the formation of cross-linked enzyme aggregates (CLEAs). Laccase CLEAs were produced by using 1000 g of polyethylene glycol per liter of enzyme solution as precipitant and 200 mu M of glutaraldehyde as a cross-linking agent. These CLEAs had a laccase activity of 148 U g(-1) and an activity recovery of 60.2% when using 2,2 '-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate. CLEAs formed by co-aggregation with bovine serum albumin (BSA) as a stabilizer showed lower laccase activity and affinity for ABTS than those without BSA. The CLEAs co-aggregated with BSA showed higher residual activity against a protease, NaN3, EDTA, methanol and acetone. The thermoresistance was higher for CLEAs than for free laccase and also higher for CLEAs co-aggregated with BSA than for simple CLEAs when tested at a pH of 3 and a temperature of 40 degrees C. Finally, laccase CLEAs were tested for their capacity to eliminate the known or suspected endocrine disrupting chemicals (EDCs) nonylphenol, bisphenol A and triclosan in a fluidized bed reactor. A 100-ml reactor with 0.5 mg of laccase CLEAs operated continuously at a hydraulic retention time of 150 min at room temperature and pH 5 could remove all three EDCs from a 5 mg l(-1) solution. (C) 2007 Elsevier B.V. All rights reserved.
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Cabana, H., Jones, J. P., & Agathos, S. N. (2007). Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. Journal of Biotechnology, 132(1), 23-31. https://doi.org/10.1016/jjbiotec.2007.07.948 (Original work published 2007)