Characterization of Gels and Films Produced from Pinhão Seed Coat Nanocellulose as a Potential Use for Wound Healing Dressings and Screening of Its Compounds towards Antitumour Effects.

The reuse of agro-industrial waste assumes great importance today. Pinhão is the seed of Araucaria angustifolia, which is native to the mountains of southern Brazil, Paraguay, and Argentina. The coat is a by-product of this seed and is rich in phenolic compounds. The present study aimed to use the residue as a precursor material for the production of nanocellulose through the mechanical defibrillation process and perform the characterization of the films and the gel to investigate the effect on the physical and regenerative properties when incorporated with polyvinyl alcohol (PVA). The modulus of elasticity was higher when the MFC of pinhão was added to the PVA. Film and gel had their cytotoxicity tested by MTT assay using 3T3 fibroblast and Schwann cancer cells, and a migration assay was also performed using the scratch test on HaCat keratinocyte cells. For the scratch test, film and gel samples with low concentration presented a complete scratch closure in 72 h. Molecular docking was performed and quercetin had the ideal interaction score values, so it was used with the PACAP protein which presented a slightly moderate interaction with the protein synthesis of Schwann cells, presenting compactness of the compound after 14 ns.

Evaluation of laccase production by Ganoderma lucidum in submerged and solid-state fermentation using different inducers.

Laccases are multicopper oxidases with high potential for industrial applications. Several basidiomycete fungi are natural producers of this enzyme; however, the optimization of production and selection of inducers for increased productivity coupled with low costs is necessary. Lignocellulosic residues are important lignin sources and potential inducers for laccase production. Pinus taeda, a dominant source of wood-based products, has not been investigated for this purpose yet. The aim of this study was to evaluate the production of laccase by the basidiomycete fungus Ganoderma lucidum in the presence of different inducers in submerged and solid-state fermentation. The results of submerged fermentation in presence of 5 µM CuSO 4 , 2 mM ferulic acid, 0.1 g/L P. taeda sawdust, or 0.05 g/L Kraft lignin indicated that although all the tested inducers promoted increase in laccase activity in specific periods of time, the presence of 2 mM ferulic acid resulted in the highest value of laccase activity (49 U/L). Considering the submerged fermentation, experimental design following the Plackett-Burman method showed that the concentrations of ferulic acid and P. taeda sawdust had a significant influence on the laccase activity. The highest value of 785 U/L of laccase activity on submerged fermentation was obtained on the seventh day of cultivation. Finally, solid-state fermentation cultures in P. taeda using ferulic acid or CuSO 4 as inducers resulted in enzymatic activities of 144.62 and 149.89 U/g, respectively, confirming the potential of this approach for laccase production by G. lucidum.

Expression of manganese peroxidase by Lentinula edodes and Lentinula boryana in solid state and submerged system fermentation.

The production of ethanol from lignocellulosic biomass is referred as a second generation biofuel, whose processing is one of the most promising technologies under development. There are few available studies on the use of enzymes produced by fungi as active for the biodegradation of lignocellulosic biomass. However, the manganese peroxidase (MnP) enzyme presents high potential to degrade lignin and the basidiomycetes are the major producers of this oxidase. Thus, this study aimed at evaluating the ability of fungi Lentinula edodes and Lentinula boryana to produce this enzyme when cultivated in submerged fermentation system (SS) and also in solid-state fermentation system (SSF) containing Eucalyptus benthamii sawdust with or without corn cob meal. In the SS the greatest MnP expression occurred on the 25th day, being of 70 UI.L-1 for L. boryana and of 20 UI.L-1 for L. edodes. In the SSF, the best results were obtained on the 10th day for L. edodes, while for L. boryana it happened between the 20th and the 25th days, despite both species presented values close to 110 UI.L-1. Therefore, the results indicated that the studied fungi express the enzyme of interest and that its production is enhanced when cultivated in solid system.

Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds.

Lysine is an essential amino acid synthesized in plants via the aspartic acid pathway. The catabolism of lysine is performed by the action of two consecutive enzymes, lysine 2-oxoglutarate reductase (LOR, EC 1.5.1.8) and saccharopine dehydrogenase (SDH, EC 1.5.1.9). The final soluble lysine concentration in cereal seeds is controlled by both synthesis and catabolism rates. The production and characterization of high-lysine plants species depends on knowledge of the regulatory aspects of lysine metabolism and manipulation of the key enzymes. We have for the first time isolated, partially purified, and characterized LOR and SDH from developing sorghum seeds, which exhibited low levels of activity. LOR and SDH were only located in the endosperm and were very unstable during the isolation and purification procedures. LOR and SDH exhibited some distinct properties when compared to the enzymes isolated from other plant species, including a low salt concentration required to elute the enzymes during anion-exchange chromatography and the presence of multimeric forms with distinct molecular masses.