Unknown

Dataset Information

0

Bacterial laccase: recent update on production, properties and industrial applications.


ABSTRACT: Laccases (benzenediol: oxygen oxidoreductase, EC 1.10.3.2) are multi-copper enzymes which catalyze the oxidation of a wide range of phenolic and non-phenolic aromatic compounds in the presence or absence of a mediator. Till date, laccases have mostly been isolated from fungi and plants, whereas laccase from bacteria has not been well studied. Bacterial laccases have several unique properties that are not characteristics of fungal laccases such as stability at high temperature and high pH. Bacteria produce these enzymes either extracellularly or intracellularly and their activity is in a wide range of temperature and pH. It has application in pulp biobleaching, bioremediation, textile dye decolorization, pollutant degradation, biosensors, etc. Hence, comprehensive information including sources, production conditions, characterization, cloning and biotechnological applications is needed for the effective understanding and application of these enzymes at the industrial level. The present review provides exhaustive information of bacterial laccases reported till date.

SUBMITTER: Chauhan PS 

PROVIDER: S-EPMC5602783 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Bacterial laccase: recent update on production, properties and industrial applications.

Chauhan Prakram Singh PS   Goradia Bindi B   Saxena Arunika A  

3 Biotech 20170916 5


Laccases (benzenediol: oxygen oxidoreductase, EC 1.10.3.2) are multi-copper enzymes which catalyze the oxidation of a wide range of phenolic and non-phenolic aromatic compounds in the presence or absence of a mediator. Till date, laccases have mostly been isolated from fungi and plants, whereas laccase from bacteria has not been well studied. Bacterial laccases have several unique properties that are not characteristics of fungal laccases such as stability at high temperature and high pH. Bacter  ...[more]

Similar Datasets

| S-EPMC7193024 | biostudies-literature
| S-EPMC5959032 | biostudies-literature
| S-EPMC7663106 | biostudies-literature
| S-EPMC6399708 | biostudies-literature
| S-EPMC2755758 | biostudies-literature