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Trametes hirsuta GMA-01 was cultivated in a culture medium supplemented with orange waste, starch, wheat bran, yeast extract, and salts. The fungus produced several holoenzymes, but the laccase levels were surprisingly high. Given the highlighted applicability of laccases in various biotechnological areas with minimal environmental impact, we provided a strategy to increase its production using response surface methodology. The immobilization of laccase into ionic supports (CM-cellulose, DEAE-agarose, DEAE-cellulose, DEAE-Sephacel, MANAE-agarose, MANAE-cellulose, and PEI-agarose) was found to be efficient and recuperative, showcasing the technical prowess of research. The crude extract laccase (CE) and CM-cellulose-immobilized crude extract (ICE) showed optimum activity in acidic conditions (pH 3.0) and at 70 °C for the CE and 60 °C for the ICE. The ICE significantly increased thermostability at 60 °C for the crude extract, which retained 21.6% residual activity after 240 min. The CE and ICE were successfully applied to sugarcane bagasse hydrolysis, showing 13.83 ± 0.02 µmol mL−1 reducing sugars after 48 h. Furthermore, the CE was tested for dye decolorization, achieving 96.6%, 71.9%, and 70.8% decolorization for bromocresol green, bromophenol blue, and orcein, respectively (0.05% (w/v) concentration). The properties and versatility of T. hirsuta GMA-01 laccase in different biotechnological purposes are interesting and notable, opening several potential applications and providing valuable insights into the future of biotechnological development.

The examination of fungal secretomes has garnered attention for its potential to unveil the repertoire of secreted proteins, notably CAZymes (Carbohydrate-Active enzymes), across various microorganisms. This study presents findings on categorizing the secretome profile of CAZymes by their function and family, derived from the filamentous fungus Trichoderma longibrachiatum LMBC 172. The cultivation was performed through submerged fermentation with three distinct carbon sources: sugarcane bagasse, tamarind seeds, and a control simulating hemicellulose containing 0.5% beechwood xylan plus 0.5% oat spelt xylan. The secretome analysis revealed 206 distinct CAZymes. Each carbon source showed particularities and differences. Of these, 89 proteins were produced simultaneously with all the carbon sources; specifically, 41 proteins using only the hemicellulose simulation, 29 proteins when sugarcane bagasse was used as a carbon source, and only 3 when tamarind seeds were used. However, in this last condition, there was a high intensity of xyloglucanase GH74 production, thus reaffirming the richness of xyloglucan in the constitution of these seeds. When evaluating the proteins found in two conditions, 18 proteins were shown between the simulation of hemicellulose and sugarcane bagasse, 11 proteins between the simulation of hemicellulose and tamarind seeds, and 15 proteins between sugarcane bagasse and tamarind seeds. Among the proteins found, there are representatives of different families such as glycosyl hydrolases (GHs) that cleave cellulose, hemicellulose, pectin, or other components; carbohydrate esterases (CEs); polysaccharide lyases (PLs); carbohydrate-binding modules (CBMs); and auxiliary activity enzymes (AAs). These results demonstrate the importance of analyzing CAZymes secreted by microorganisms under different culture conditions.

Substantial amounts of organo-pollutants, often persistent and toxic, are generated globally each year, posing a threat to soil, water, groundwater, and air. The pollutants encompass a wide range of substances from various sources, which include solid as well as liquid ones, such as landfill leachates and wastewaters. The compounds include paper and pulp mill byproducts, pharmaceuticals, diverse types of plastics, hydrocarbons, pigments, and dyes, as well as pesticides and insecticides. Fungal bioremediation stands out as a promising technology that uses the metabolic potential of fungi to eliminate or mitigate the impact of pollutants. Notably, species of the genus Pycnoporus exhibit significant capabilities for degrading a broad spectrum of toxic molecules. This degradation is facilitated by released ligninolytic enzymes, especially laccase, and cellular enzymes pertaining to the cytochrome P450 monooxygenase system. The laccase, which is overproduced by the genus Pycnoporus, is quite remarkable for its high redox potential. The objective of this review is to highlight the proficiency of the Pycnoporus genus in the degradation of pollutants in submerged and solid-state fermentation. Recent studies conducted over the past decade consistently highlight the Pycnoporus genus as a robust contender in the realm of white biotechnology.

The analysis of the secretome allows us to identify the proteins, especially carbohydrate-active enzymes (CAZymes), secreted by different microorganisms cultivated under different conditions. The CAZymes are divided into five classes containing different protein families. Thermothelomyces thermophilus is a thermophilic ascomycete, a source of many glycoside hydrolases and oxidative enzymes that aid in the breakdown of lignocellulosic materials. The secretome analysis of T. thermophilus LMBC 162 cultivated with submerged fermentation using tamarind seeds as a carbon source revealed 79 proteins distributed between the five diverse classes of CAZymes: 5.55% auxiliary activity (AAs); 2.58% carbohydrate esterases (CEs); 20.58% polysaccharide lyases (PLs); and 71.29% glycoside hydrolases (GHs). In the identified GH families, 54.97% are cellulolytic, 16.27% are hemicellulolytic, and 0.05 are classified as other. Furthermore, 48.74% of CAZymes have carbohydrate-binding modules (CBMs). Observing the relative abundance, it is possible to state that only thirteen proteins comprise 92.19% of the identified proteins secreted and are probably the main proteins responsible for the efficient degradation of the bulk of the biomass: cellulose, hemicellulose, and pectin.