Isolation, one-step affinity purification, and characterization of a polyextremotolerant laccase from the halophilic bacterium Aquisalibacillus elongatus and its application in the delignification of sugar beet pulp. (April 2017)

• Record Type: Journal Article
• Authors: Rezaei, Shahla; Shahverdi, Ahmad Reza; Faramarzi, Mohammad Ali
• Is Part Of: Bioresource technology. Volume 230(2017)
• Page Start: 67
• Page End: 75
• Publication Date: 2017-04
• Subjects: Aquisalibacillus elongatus -- Halophilic laccase -- Affinity chromatography -- Delignification -- Ionic liquid; 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.2017.01.036
• Languages: English
• ISSNs: 0960-8524

Abstract

Graphical abstract: Highlights: A laccase producing halophile Aquisalibacillus elongatus was bio-prospected. Rapid and efficient purification was achieved using a synthetic affinity resin. Purified laccase was an extremely stable against pH, temperature, and additives. The laccase had exceptionally specificity to a wide range of potential substrates. Enzymatic hydrolysis in [BMIM][PF6 ] yielded 78.4% delignification within 12 h. Abstract: The aim of the present work was to study the ability of a halophilic bacterial laccase to efficient delignification in extreme conditions. Here, a highly stable extracellular laccase showing ligninolytic activity from halophilic Aquisalibacillus elongatus is described. The laccase production was strongly influenced by NaCl and CuSO4 and under optimal conditions reached 4.8 U mL −1 . The monomeric enzyme of 75 kDa was purified by a synthetic affinity column with 68.2% yield and 99.8-fold purification. The enzyme showed some valuable features viz. stability against a wide range of organic solvents, salts, metals, inhibitors, and surfactants and specificity to a wide spectrum of substrates diverse in structure and redox potential. It retained more than 50% of the original activity at 25–75 °C and pH 5.0–10.0. Furthermore, the enzyme was found to be effective in the delignification of sugar beet pulp in an ionic liquid that makes it useful for industrial applications.