Journal
JOURNAL OF THE TAIWAN INSTITUTE OF CHEMICAL ENGINEERS
Volume 65, Issue -, Pages 1-7Publisher
ELSEVIER
DOI: 10.1016/j.jtice.2016.04.025
Keywords
Cerrena; Laccase; Cross-linked enzyme aggregates; NaCl; Remazol Brilliant Blue Reactive
Categories
Funding
- Natural Science Foundation of China [41306120]
- Oceanic Public Welfare Industry Special Research Project of China [201305015]
Ask authors/readers for more resources
White-rot fungus Cerrena sp. strain HYB07 produces laccase with high yields and strong decolorization ability. Cerrena laccase was immobilized by preparing Cross-linked enzyme aggregates (CLEAs), and ammonium sulfate and glutaraldehyde were the optimal precipitant and cross-linking agent, respectively. An activity recovery rate of 68.1% was obtained at pH 8 after precipitation with (NH4)(2)SO4 and cross linking with 30 mM glutaraldehyde for 311 at 25 degrees C. Immobilized Cerrena laccase demonstrated improved tolerance to NaCl, metal ions and organic solvents. NaCl was a mixed-type inhibitor of both free and immobilized laccases with 2, 2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) as the substrate, and the improvement of NaCl resistance by laccase immobilization was quantified kinetically. Laccase CLEAs had higher inhibition constants K-I and K-IS compared to free laccase, suggesting that the affinity of NaCl to laccase was attenuated by immobilization. Laccase CLEAs also displayed greater velocity and efficiency in Remazol Brilliant Blue Reactive decolorization in the presence of NaCl than free laccase. Greater differences in the half time (t(1/2)) of Remazol Brilliant Blue Reactive decolorization by free and immobilized laccases were observed with increasing NaCl concentrations. (C) 2016 Taiwan Institute of Chemical Engineers. Published by Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available