Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in last decades due to their ability to oxidize both phenolic and non-phenolic lignin related compounds as well as highly recalcitrant environmental pollutants. This makes these biocatalysts very useful for their application in several biotechnological processes. Such applications include the detoxification of industrial effluents, mostly from the paper and pulp, textile and petrochemical industries, polymer synthesis, bioremediation of contaminated soils, wine and beverage stabilization. Laccases are also used as catalysts for the manufacture of anti-cancer drugs and even as ingredients in cosmetics. Recently, the utility of laccases has also been applied to nanobiotechnology. This paper reviews recent and important patents related to the properties, heterologous production, molecular cloning, and applications of laccases within different industrial fields as well as their potential extension to the nanobiotechnology area.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.2174/187220808783330965 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Development of an integrated micro-millisystem for continuous laccase extraction.
Bioresour Technol
January 2025
University of Zagreb Faculty of Chemical Engineering and Technology, Marulićev trg 19, HR-10000 Zagreb, Croatia. Electronic address:
Efforts to reduce the impact of chemical processes on the environment are leading to a shift to enzymatic alternatives, with laccases standing out for their versatile substrate oxidation capabilities. This study addresses the improvement of biocatalytic reactions by deep eutectic solvents (DES), in particular DES-based aqueous two-phase systems (ATPS) for the extraction of biomolecules. Continuous laccase extraction from crude samples was achieved using a DES-based ATPS, which was first optimized in a batch extractor and later intensified in a microextractor.
View Article and Find Full Text PDFEco-friendly decolorization of synthetic dyes using radiation-induced whole cell biocatalyst with enhanced copper resistance.
Environ Res
January 2025
Radiation Biotechnology Division, Korea Atomic Energy Research Institute, Jeongeup 56212, Republic of Korea. Electronic address:
Toxic and carcinogenic compounds, such as synthetic dyes and polyphenols, were widely employed and released as pollutants in a variety of industries, including textiles, food, and cosmetics. Biological oxidation process that used oxidizing enzymes to breakdown pollutant compounds were environmentally favorable. However, due to the cell toxicity of metal ions supplements used for the biosynthesis of oxidizing enzymes like laccase, their efficient application for biological degradation is limited.
View Article and Find Full Text PDFStructure-Function Relationship of the β-Hairpin of HB27 Laccase.
Int J Mol Sci
January 2025
Departamento de Micro y Nanotecnologías, Instituto de Ciencias Aplicadas y Tecnología, Universidad Nacional Autónoma de México, Cto. Exterior S/N, C.U., Coyoacán, Ciudad de México C.P. 04510, Mexico.
Thermus thermophilus HB27 laccase (Tth-Lac) is a thermostable enzyme that contains a β-hairpin (Ala292-Gln307) covering the substrate entrance. We analyzed the role of this β-hairpin in the enzymatic activity of Tth-Lac through three β-hairpin mutants: two variants without the β-hairpin (C1Tth-Lac and C2Tth-Lac) and one with a partially modified β-hairpin (P1Tth-Lac). Enzymatic activity was assayed with different substrates with and without copper.
View Article and Find Full Text PDF[Directed evolution improves the catalytic activity of laccase in papermaking].
Sheng Wu Gong Cheng Xue Bao
January 2025
State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei University, Wuhan 430062, Hubei, China.
As a biocatalyst, laccase has been widely studied and applied in the papermaking industry. However, the low catalytic efficiency and poor stability of natural laccase limit its application in the pulping process. To develop the laccase with high activity and strong tolerance, we carried out directed evolution for modification of the laccase derived from and screened out the mutants F282L/F306L and Q275P from the random mutant library by high-throughput screening.
View Article and Find Full Text PDFLACCASE35 Enhances Lignification and Resistance Against Pseudomonas syringae pv. actinidiae Infection in Kiwifruit.
Plant Physiol
January 2025
Anhui Key Laboratory for Horticultural Crop Quality Biology, School of Horticulture, Anhui Agricultural University, Hefei, 230036, P.R. China.
Kiwifruit bacterial canker, a highly destructive disease caused by Pseudomonas syringae pv. actinidiae (Psa), seriously affects kiwifruit (Actinidia spp.) production.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!