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Co-aggregation of Laccase and Nature Egg White: a Simple Method to Prepare Stable and Recyclable Biocatalyst

Jiang, Yanjun, Wang, Qi, He, Ying, Zhou, Liya, Gao, Jing
Applied biochemistry and biotechnology 2014 v.172 no.5 pp. 2496-2506
2,4-dichlorophenol, bovine serum albumin, crosslinking, egg albumen, glutaraldehyde, immobilized enzymes, laccase, temperature, thermal stability, trypsin, urea
Cross-linked enzyme aggregates (CLEAs) are a versatile and effective method for enzyme immobilization, which is exquisitely simple and amenable to rapid optimization. In this study, nature egg white, which is low cost, easily available, and nontoxic, was used as protein feeder to replace traditional protein feeder (bovine serum albumin, etc.) in the preparation of laccase CLEAs (CLEAs-egg). The effects of the various parameters—nature of the precipitant, temperature, glutaraldehyde concentration, and cross-linking time—on the activity recovery of the resulting CLEAs were studied. The laccase CLEAs-egg exhibited increased stability compared to the free and the laccase CLEAs without protein feeder. The thermal stability of CLEAs-egg was improved and showed 1.3- and 1.8-fold increase in activity at 40 and 60 °C after 5 h incubation, respectively. The stability of CLEAs-egg against denaturants (urea and GndHCl) and protease (trypsin) was also improved. Laccase CLEAs-egg was also demonstrated to be an active and stable biocatalyst in the removal of chlorophenol. After 30 h, 83.6 and 91.5 % of 4-chlorophenol and 2,4-dichlorophenol can be removed.