Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology

Abstract

The ubiquitous members of the multicopper oxidase family of enzymes oxidize a range of aromatic substrates such as polyphenols, methoxy-substituted phenols, amines and inorganic compounds, concomitantly with the reduction of molecular dioxygen to water. This family of enzymes can be broadly divided into two functional classes: metalloxidases and laccases. Several prokaryotic metalloxidases have been described in the last decade showing a robust activity towards metals, such as Cu(I), Fe(II) or Mn(II) and have been implicated in the metal metabolism of the corresponding microorganisms. Many laccases, with a superior efficiency for oxidation of organic compounds when compared with metals, have also been identified and characterized from prokaryotes, playing roles that more closely conform to those of intermediary metabolism. This review aims to present an update of current knowledge on prokaryotic multicopper oxidases, with a special emphasis on laccases, anticipating their enormous potential for industrial and environmental applications.

Laccase encapsulation in chitosan nanoparticles enhances the protein stability against microbial degradation

“…On the other hand, enzymatic transformation of polyaromatic hydrocarbons Thongkred et al 2011;Niu et al 2013), phenolic compounds (Ullah et al 2000;Gaitan et al 2011), pesticides (Maruyama et al 2006;Torres-Duarte et al 2009), endocrine-disrupting compounds (Cabana et al 2007;Torres-Duarte et al 2012), PCBs (Gayosso-Canales et al 2012, pharmaceuticals (Touahar et al 2014), industrial dyes (Rodriguez et al 1999;Wesenberg et al 2003), and cleaning of certain explosives from the soil such as trinitrotoluene (Shraddha et al 2011) by laccase make it an enzyme with enormous potential for remediation processes of polluted sites and elimination of environmental threats. Laccases are considered potential biocatalysts for large-scale transformation of xenobiotic compounds because they do not require exogenous co-factors (Martins et al 2015) and have comparatively high stability (Loera Corral et al 2006) against temperature and pH.…”

Improving the Indigo Carmine Decolorization Ability of a Bacillus amyloliquefaciens Laccase by Site-Directed Mutagenesis

“…Laccases (EC 1.10.3.2) are enzymes that belong to the broader family of multicopper oxidases. They are able to catalyze the oxidation of various aromatic compounds with the reduction of molecular oxygen to water [9]. The first commercial laccase was launched in 1996 by Novozyme, and was used for denim bleaching with the help of a redox mediator.…”

“…The first commercial laccase was launched in 1996 by Novozyme, and was used for denim bleaching with the help of a redox mediator. The product exhibited good performance in oxidizing the indigo dye on denim garments into uncolored compounds [9]. To date, most commercial laccases are of fungal origin, and they are usually active in moderate temperatures and an acidic pH range [9].…”

“…The product exhibited good performance in oxidizing the indigo dye on denim garments into uncolored compounds [9]. To date, most commercial laccases are of fungal origin, and they are usually active in moderate temperatures and an acidic pH range [9]. Since wastewater from denim processing is characterized by high pH and high temperature [10], the application of fungal laccases for the treatment of textile effluent is limited by their instability under these drastic conditions.…”

“…Compared with fungal laccases, bacterial laccases are highly active and much more stable under alkaline and high temperature conditions [9]. In our previous work, we heterologously expressed and characterized a novel laccase from Bacillus amyloliquefaciens LC02.…”