Table 1 Recent advances in elucidating the interactions between laccase and DES

Bacillus HR03

ChCl-based and betaine-based NADESs aqueous buffer

CAA (substrate: ABTS); fluorescence spectrocopy

Enhanced 300%, 20% (v/v) betaine:glycerol

(Khodaverdian et al. 2018)

Trametes versicolor

Sixteen DES aqueous solutions (10, 25 and 50 wt%)

CAA (substrate: ABTS); molecular docking

1. ChCl-based DESs led to a decrease in the enzyme activity, while betaine-based DESs enhanced activity;

2. Laccase activity was dependent on the number of hydroxyl groups present in the polyols and their ability to H-bond with the enzyme amino acids;

3. The establishment of stronger H-bonds between DES components and laccase were responsible for the enhanced laccase activity

(Toledo et al. 2019)

Nine aqueous NADES media

CAA (substrate: ABTS)

The thermostability of laccase improved in aqueous betaine-based NADES media (25 wt%)

(Delorme et al. 2020)

Trametes hirsuta

Three betaine-based DES (1:2) and aqueous media

CAA (substrate: ABTS)

1. Laccase completely lost its activity within 3 h in pure betaine-based DESs

2. In a 10% v/v betaine:glycerol (1:2) solution, laccase activity increased by up to 140%

(Khlupova et al. 2021)

Myceliophthora thermophila

Four DES aqueous media (ChCl:LA, ChCl:glycerol, betaine:glycerol, betaine:LA)

CAA (substrate: ABTS); kinetics; DSC; Crystallographic analysis; Fluorescence and CD spectroscopies

1. Laccase activity was enhanced up to 300% at a 2–8% v/v solution of betaine:LA;

2. ChCl:glycerol was a noncompetitive S-parabolic-I-parabolic mixed inhibitor of laccase;

3. DES tirggered changes in the local environments of the amino acids in the active site of laccase

(Chan et al. 2021)

Pleurotus ostreatus

Five betaine-based NADESs at a concentration of 25 wt% Sorbitol (Sor), xylitol (Xyl), glycerol (Gly), ethylene glycol (EtG), and erythritol (Ery)

CAA (substrate: ABTS); molecule docking

1. NADES is better than its individual components

2. The binding energies between laccases and NADES components correlate with the stabilization of laccases

3. The stabilization of interactions on enzyme surface, especially in flexible loops, was important to improve enzyme thermostability

(Varriale et al. 2022)