Optimisation of the Production and Bleaching Process for a New Laccase from Madurella mycetomatis, Expressed in Pichia pastoris: from Secretion to Yielding Prominent

Purification and characterization of a fungal laccase expressed in Kluyveromyces lactis suitable for baking

“…It is important to clarify that in these trials no laccase activity was detected in the medium without copper in clones with or without a polyhistidine tag. As laccase activity was not evident in YPGal medium, we tested the effect of copper because, being part of the active site of laccase, it is one of the most reported metals in the study of this enzyme (Callejón et al., 2017; Fonseca et al., 2018; Garg et al., 2012; Tülek et al., 2020). Therefore, it was possible to detect enzymatic activity.…”

“…In this sense, in agreement with our results, Bao et al (2013) reported zinc, potassium, and ammonium (tested on purified enzyme) as inhibitors of recombinant laccase, and Li et al (2013) found that ammonium and zinc had no significant effect on recombinant laccase activity. However, the effects of different compounds on laccase activity were not always the same; Bao et al (2013) also reported iron as an inhibitor and Tween as an inducer of recombinant laccase, Tülek et al (2020) said that high concentrations of iron significantly inhibited laccase activity, while zinc and magnesium caused an increase in laccase activity, and Li et al (2013) stated that a recombinant enzyme was completely inactivated with iron, as opposed to our We elucidated that the differences in laccase activity obtained with each compound could be due to the difference in chemical structures, which affects the folding of laccase and significantly increase or decrease the activity. These observations may also be attributed to varying interactions within the complex protein spatial structure, which may affect the catalytic properties of laccase in unpredictable ways.…”

Lignocellulolytic Biocatalysts: The Main Players Involved in Multiple Biotechnological Processes for Biomass Valorization

“…Moreover, laccases have a significant advantage since they act specifically on indigo dyes [ 273 ]. Laccases applied in the bleaching process have already been produced from different microorganisms, such as the fungi Cerrena unicolor and Madurella mycetomatis , and the bacterium Brevibacillus agri , which presented optimal temperatures ranging from 30 to 60 °C, and pH range from 3 to 6 [ 274 , 275 , 276 ]. Moreover, lignocellulolytic enzymes are also used in the polishing process, the last finishing step to improve fabric quality, in which fibers are hydrolyzed, providing a smoother surface with a clean, soft, and shiny touch.…”

Laccases in food processing: Current status, bottlenecks and perspectives

“…It must be stressed, however, that most of these commercial laccases are not recommended for food purposes, but rather for environmental and bioenergy areas. Numerous strategies have already been devised to reduce the production costs of laccases, including the isolation of new natural hypersecretory strains (Iark et al, 2019;Songulashvili et al, 2015), the heterologous expression of laccase genes (Tulek et al, 2020) and the optimization of enzyme production (Tisma, Znidarsic-Plazi, Vasic-Racki, & Zelic, 2012;Wang, Hu, Guo, & Liu, 2016). In spite of these efforts, the production of laccases still remains quite expensive (Antošová & Sychrová, 2016;Yang et al, 2017).…”