Development of biocatalysts immobilized on coal ash-derived Ni-zeolite for facilitating 4-chlorophenol degradation. (July 2020)

• Record Type: Journal Article
• Authors: Lim, Yejee; Yu, Jimin; Park, Sungyoon; Kim, Minsoo; Chen, Siyu; Bakri, Nurul Aziemah Binti; Sabri, Nur Izzati Auni Binti Mohd; Bae, Sungjun; Kim, Han S.
• Is Part Of: Bioresource technology. Volume 307(2020)
• Publication Date: 2020-07
• Subjects: Enzyme immobilization -- 4-Chlorophenol -- Oxydoreductase -- Coal fly ash -- Synthetic zeolite; Biomass -- Periodicals; Biomass energy -- Periodicals; Bioremediation -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Bioénergie -- Périodiques; Déchets agricoles -- Périodiques; Déchets industriels -- Périodiques; Déchets organiques -- Périodiques; Déchets (Combustible) -- Périodiques; 662.88
• DOI: 10.1016/j.biortech.2020.123201
• Languages: English
• ISSNs: 0960-8524

Abstract

Graphical abstract: Highlights: Coal fly ash-derived Ni-zeolite was developed as an enzyme support. The enzyme immobilization yield was 77.5%. Immobilized CphC-I catalyzes the initial step of 4-CP biodegradation. The activity of immobilized CphC-I was 7.98 U/g Ni-zeolite. vmax = 0.20 mM/min, KM = 0.44 mM, and kcat / KM = 0.02 mM −1. min −1 . Abstract: A new type of biocatalyst was developed to facilitate the biochemical decomposition of 4-chlorophenol (4-CP) in this study. Oxydoreductases that catalyze the initial steps of 4-CP biodegradation were immobilized on a synthetic inorganic enzyme support. Type-X zeolite, a high-surface area support, was synthesized from coal fly ash, on which nickel ions were plated by impregnation (Ni-zeolite), followed by the effective immobilization (77.5% immobilization yield) of recombinant monooxygenase (CphC-I), dioxygenase (CphA-I), and flavin reductase (Fre) isolated from Pseudarthrobacter chlorophenolicus A6 and Escherichia coli K-12, respectively. The retained catalytic activity of the enzymes immobilized on Ni-zeolite was as high as 64% of the value for the corresponding free enzymes. The Michaelis–Menten kinetic parameters vmax and KM of the immobilized enzymes were determined to be 0.20 mM·min −1 and 0.44 mM, respectively. These results are expected to provide useful information with respect to the development of novel enzymatic treatments for phenolic hydrocarbon contaminants.