Prospection of Fungal Lignocellulolytic Enzymes Produced from Jatoba (Hymenaea courbaril) and Tamarind (Tamarindus indica) Seeds: Scaling for Bioreactor and Saccharification Profile of Sugarcane Bagasse.

The lignocellulosic biomass comprises three main components: cellulose, hemicellulose, and lignin. Degradation and conversion of these three components are attractive to biotechnology. This study aimed to prospect fungal lignocellulolytic enzymes with potential industrial applications, produced through a temporal analysis using Hymenaea courbaril and Tamarindus indica seeds as carbon sources. α-L-arabinofuranosidase, acetyl xylan esterase, endo-1,5-α-L-arabinanase, ß-D-galactosidase, ß-D-glucosidase, ß-glucanase, ß-D-xylosidase, cellobiohydrolase, endoglucanase, lichenase, mannanase, polygalacturonase, endo-1,4-ß-xylanase, and xyloglucanase activities were determined. The enzymes were produced for eight filamentous fungi: Aspergillus fumigatus, Trametes hirsuta, Lasiodiplodia sp., two strains of Trichoderma longibrachiatum, Neocosmospora perseae, Fusarium sp. and Thermothelomyces thermophilus. The best producers concerning enzymatic activity were T. thermophilus and T. longibrachiatum. The optimal conditions for enzyme production were the media supplemented with tamarind seeds, under agitation, for 72 h. This analysis was essential to demonstrate that cultivation conditions, static and under agitation, exert strong influences on the production of several enzymes produced by different fungi. The kind of sugarcane, pretreatment used, microorganisms, and carbon sources proved limiting sugar profile factors.

A highly reusable MANAE-agarose-immobilized Pleurotus ostreatus laccase for degradation of bisphenol A.

Bisphenol A (BPA) is an endocrine disruptor compound that is continuously released into the environment and is barely degraded in wastewater treatment plants. A previous study showed that free Pleurotus ostreatus laccase is efficient in degrading BPA producing less toxic metabolites. In the present study, this laccase was successfully immobilized onto MANAE-agarose, improving its efficiency in degrading BPA and its thermal and storage stabilities. In addition to this, the immobilized enzyme retained >90% of its initial capability to degrade BPA after 15cycles of reuse. P. ostreatus laccase immobilized onto MANAE-agarose could be an economical alternative for large scale degradation of BPA in aqueous systems.