» Articles » PMID: 31834437

Beyond Natural Laccases: Extension of Their Potential Applications by Protein Engineering

Overview
Date 2019 Dec 14
PMID 31834437
Citations 6
Authors
Affiliations
Soon will be listed here.
Abstract

Laccases bring exciting promises into the green industries, and the development of enzymes with improved properties is further raising their exploitation potential. Molecular engineering methods to build highly efficient catalysts both through rational and random mutagenesis were extensively applied. Moreover, computational approaches are becoming always more reliable in aiding proper design of efficient and tailored catalyst for specific applications. In this review, the results of the last 10 years about industrial application of engineered laccases in different fields are analyzed. Tailoring laccase towards a target substrate and defining a proper screening strategy for the selection of the "jackpot mutant" represent the keys of a winning mutagenesis pathway. Likewise, laccase chimerae, built by the fusion of laccases with relevant proteins, emerged as an added value in the designing of flexible and well-rounded biocatalysts. Despite being promising in most of the reported examples, evolved laccases are currently tested at a laboratory scale and a feedback from the industry world is continuously required to strengthen the biotechnological exploitation of these improved enzymes.

Citing Articles

Laccase Engineering: Redox Potential Is Not the Only Activity-Determining Feature in the Metalloproteins.

Ali M, Bhardwaj P, Ishqi H, Shahid M, Islam A Molecules. 2023; 28(17).

PMID: 37687038 PMC: 10488915. DOI: 10.3390/molecules28176209.


Detoxification and decolorization of complex textile effluent in an enzyme membrane reactor: batch and continuous studies.

Dahiya M, Islam D, Srivastava P, Sreekrishnan T, Mishra S Front Microbiol. 2023; 14:1193875.

PMID: 37485538 PMC: 10361525. DOI: 10.3389/fmicb.2023.1193875.


Fungal Laccases: The Forefront of Enzymes for Sustainability.

Loi M, Glazunova O, Fedorova T, Logrieco A, Mule G J Fungi (Basel). 2021; 7(12).

PMID: 34947030 PMC: 8708107. DOI: 10.3390/jof7121048.


Recombinant laccase rPOXA 1B real-time, accelerated and molecular dynamics stability study.

Ardila-Leal L, Monterey-Gutierrez P, Poutou-Pinales R, Quevedo-Hidalgo B, Galindo J, Pedroza-Rodriguez A BMC Biotechnol. 2021; 21(1):37.

PMID: 34088291 PMC: 8178886. DOI: 10.1186/s12896-021-00698-3.


Rational engineering of the lccβ laccase for the mediator-less oxidation of large polycyclic aromatic hydrocarbons.

Chiado A, Bosco F, Bardelli M, Simonelli L, Pedotti M, Marmo L Comput Struct Biotechnol J. 2021; 19:2213-2222.

PMID: 33995914 PMC: 8099718. DOI: 10.1016/j.csbj.2021.03.017.