Ligninolytic Enzymes and Their Potential Applications

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About this Research Topic

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Background

Laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase are ligninolytic enzymes that have recently gained significant economic value in a variety of industries, including those in the textile, food, pulp and paper, pharmaceutical, and detergent industries, as well as nanoparticle-based biosensors, synthetic chemistry, cosmetics, soil bioremediation, and biodegradation of environmental phenolic pollutants, and the removal of endocrine disruptors. Due to the significant role that ligninolytic enzymes have played in biotechnological and environmental processes over the past few decades, ligninolytic microorganisms—which have the capacity to breakdown lignin—have attracted a great deal of attention during screening efforts. The global carbon cycle depends heavily on ligninolytic enzymes. Due to their employment in several processes, ligninolytic enzyme complexes are increasingly in demand for use in industry and biotechnology. The manufacture, purification, immobilization, characterization, and uses of ligninolytic enzymes in various industrial and biotechnological fields will all be covered in this topic.

Due to the limitations of physio-chemical processes, rising environmental concerns, regulatory constraints, and an expanding body of scientific knowledge, scientists are currently researching enzymatic approaches for creating green chemistry technologies. In particular, enzyme-assisted reactions are the subject of much research since they are often environmentally beneficial and have a wide range of possible applications. Recent attempts to alter enzymes chemically or biotechnologically may assist in increasing the activity and stability of the enzyme. Therefore, attempts to advance immobilization methods also need to be stepped up. Though several techniques have been created to immobilize enzymes, many of them have the significant flaw of rapidly deactivating the enzyme. With improved stability and activity than in free form, novel immobilization technologies have been devised to produce chemically bound immobilized enzymes. The ligninolytic enzymes (laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase) are being considered as potential eco-friendly enzymes to replace the conventional chemical and mechanical processes in a number of industries, including pulp and paper, textile, pharmaceutical, and nanoparticle-based biosensors. This is because of their diverse distributions and functions.

The present Research Topic's objective is to discuss innovative, promising, and recent developments in the field of microbial ligninolytic enzymes (including laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase). Only original research, short reviews, and review articles are acceptable. The following topics may be addressed in this research topic, but they are not restricted to them:

• Develop cutting-edge proteomic, chemical engineering, and statistical methods to increase the production of microbial ligninolytic enzymes
• The isolation, characterization, and application of exceptional microbial ligninolytic enzymes
• Immobilization of ligninolytic enzymes on novel supports, such as nanocomposites, for use in:
- Biosensors
- biofuel cells
• Other cutting-edge potential biotechnological and environmental applications, such as green biodegradation of xenobiotic compounds and polycyclic aromatic hydrocarbons

Please note that all submissions to this Research Topic should have an experimental focus and papers which focus solely on screening will not be accepted. All submissions should be within the scope of the Microbiotechnology section.

Research Topic Research topic image

Keywords: Laccases, microbial ligninolytic enzymes, peroxidases, bio-nanotechnology

Important note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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