Laccase

Thomas, Deepa; Gangawane, Ajit K.

doi:10.1002/9781119547976.ch3

Cited by 1 publication

(1 citation statement)

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“…Laccases (benzenediol oxygen reductases, EC 1.10.3.2) are a family of copper-containing polyphenol oxidases that belongs to the multicopper oxidases [ 1 ]. Due to their low substrate specificity, laccases are able to catalyze the one-electron oxidation of a wide range of organic compounds, including phenols and aromatic amines, with the simultaneous reduction of molecular oxygen (O 2 ) to water (H 2 O) [ 2 , 3 ]. The catalytic reaction of laccase involves the removal of one electron from the substrates for the production of free radicals.…”

Section: Introductionmentioning

confidence: 99%

Thermostabilization of a fungal laccase by entrapment in enzymatically synthesized levan nanoparticles

Alishah Aratboni,

Martinez,

Olvera

et al. 2024

PLoS ONE

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In this work, we present a comprehensive investigation of the entrapment of laccase, a biotechnologically relevant enzyme, into levan-based nanoparticles (LNPs). The entrapment of laccase was achieved concomitantly with the synthesis of LNP, catalyzed by a truncated version of a levansucrase from Leuconostoc mesenteroides. The study aimed to obtain a biocompatible nanomaterial, able to entrap functional laccase, and characterize its physicochemical, kinetic and thermal stability properties. The experimental findings demonstrated that a colloidal stable solution of spherically shaped LNP, with an average diameter of 68 nm, was obtained. An uniform particle size distribution was observed, according to the polydispersity index determined by DLS. When the LNPs synthesis was performed in the presence of laccase, biocatalytically active nanoparticles with a 1.25-fold larger diameter (85 nm) were obtained, and a maximum load of 243 μg laccase per g of nanoparticle was achieved. The catalytic efficiency was 972 and 103 (μM·min)-1, respectively, for free and entrapped laccase. A decrease in kcat values (from 7050 min-1 to 1823 min-1) and an increase in apparent Km (from 7.25 μM to 17.73 μM) was observed for entrapped laccase, compared to the free enzyme. The entrapped laccase exhibited improved thermal stability, retaining 40% activity after 1 h-incubation at 70°C, compared to complete inactivation of free laccase under the same conditions, thereby highlighting the potential of LNPs in preserving enzyme activity under elevated temperatures. The outcomes of this investigation significantly contribute to the field of nanobiotechnology by expanding the applications of laccase and presenting an innovative strategy for enhancing enzyme stability through the utilization of fructan-based nanoparticle entrapments.

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Section: Introductionmentioning

confidence: 99%