Upgrading Laccase Production and Biochemical Properties: Strategies and Challenges

Abstract

Improving laccases continues to be crucial in novel biotechnological developments and industrial applications, where they are concerned. This review breaks down and explores the potential of the strategies (conventional and modern) that can be used for laccase enhancement (increased production and upgraded biochemical properties such as stability and catalytic efficiency). The challenges faced with these approaches are briefly discussed. We also shed light on how these strategies merge and give rise to new options and advances in this field of work. Additionally, this article seeks to serve as a guide for students and academic researchers interested in laccases. This document not only gives basic information on laccases, but also provides updated information on the state of the art of various technologies that are used in this line of investigation. It also gives the readers an idea of the areas extensively studied and the areas where there is still much left to be done. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:1015-1034, 2017.

Evaluation of laccase production by Ganoderma lucidum in submerged and solid‐state fermentation using different inducers

“…Laccases are enzymes produced by plants, bacteria, insects, and fungi. These enzymes have important characteristics, such as improved stability and high catalytic activity, but factors associated with productivity, diversity, and catalytic properties are not compatible with their industrial application in a viable way .…”

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

“…Due to their high catalytic efficiency and broad substrate specificity, laccases are used in various fields, including biopulping, delignification, biobleaching, environmental pollutants bioremediation, dye decolorization, etc. (Riva, 2006;Bertrand et al, 2017;Younes et al, 2019).…”

“…Fungi, especially white rot fungi, are the main laccase producers in nature, and the potential laccase producing strains be utilized in industrial application (Bertrand et al, 2017). Until now, many laccase-producing fungi have been studied and most of the fungi can produce several laccase isozymes (usually more than 10 isoenzymes in the same fungus strain) that showed different kinetic and physicochemical features, which makes it possible to seek new laccase isoenzymes and meets the demands in the industrial applications (Janusz et al, 2013;Zhuo et al, 2016;Zheng et al, 2017).…”

“…Until now, many laccase-producing fungi have been studied and most of the fungi can produce several laccase isozymes (usually more than 10 isoenzymes in the same fungus strain) that showed different kinetic and physicochemical features, which makes it possible to seek new laccase isoenzymes and meets the demands in the industrial applications (Janusz et al, 2013;Zhuo et al, 2016;Zheng et al, 2017). However, the expression of different laccase isoenzymes in the same strain depends on many factors such as the presence of inducers (especially Cu 2+ and phenolic compounds), the ratio of carbon and nitrogen, age of the culture and heat shock treatment (Baldrian, 2006;Piscitelli et al, 2011;Janusz et al, 2013;Zhuo et al, 2016;Bertrand et al, 2017). Untill now, few laccase isoenzymes have been isolated and characterized, usually one or two isoenzymes per fungus strain, and most of the laccases isoenzymes isolated so far are found sensitive to extreme conditions of temperature, pH, metal ions, etc.…”

A Modular Approach for Interlocking Enzymes in Whatman Paper

“…[17] Such factors hamper its application in biofuel cells, ethanol production, biosensors,t extile and food industries, and wastewater treatment. [18] Thus,w ed eveloped as imple, robust, and inexpensive method to stabilize laccase.…”