Microbial diversity and enzymatic potential for plastic degradation in contaminated dumpsites in Mazamitla, Jalisco.

Plastic pollution has become an important global environmental concern, emphasizing the urgent need for effective plastic degradation strategies. Microorganisms have demonstrated potential in degrading plastics through enzymatic activities. This study investigated the microbial diversity and enzymatic potential of microorganisms isolated from plastic-contaminated dumpsites located in Mazamitla, Jalisco a west-central region of Mexico.

[Free radical scavenging capacity of traditional Mexican food].

Objective and methodology: the aim of this research was to determine the TAC of foods traditionally prepared in Mexico. TAC was assessed using the oxygen radical absorbance capacity (ORAC) assay, the 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) radical (ABTS), and 1,1-diphenyl-2-picrylhydrazyl (DPPH) assays. Additionally, the capacity of the samples to reduce ferric ions to ferrous ions (FRAP) was measured.

Further Characterization of Lipase B from Ustilago maydis Expressed in Pichia pastoris: a Member of the Candida antarctica Lipase B-like Superfamily.

Lipases from the basidiomycete fungus Ustilago maydis are promising but underexplored biocatalysts due to their high homology with Candida antarctica lipases. This study provides a comprehensive characterization of a recombinant CALB-like lipase from U. maydis, expressed in Pichia pastoris (rUMLB), and compares its properties with those of the well-studied recombinant lipase B from C.

Synthesis and toxicity of monothiooxalamides against human red blood cells, brine shrimp (), and fruit fly ( ).

A new family of monothiooxalamides derived from 2-aminobenzimidazole was synthesized, and their structures were confirmed by H and C one-dimensional and 2D NMR experiments (COSY, HSQC, and HMBC). The antioxidant capacity was evaluated by free radical scavenging assays: 1,1-diphenyl-2-picrylhydrazyl (DPPH•), 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) radical cation (ABTS•), ferric reducing antioxidant power (FRAP), oxygen radical absorbance capacity (ORAC), and the Fe(II) chelating ability. Our work group has previously reported the synthesis and antioxidant activity of monothiooxalamides derived from 2-aminopyridine ().

Unveiling potential PET degrading eukaryotes through in silico bioprospecting of PETases.

This study addresses the environmental problem of PET plastic through in silico bioprospecting for the identification and experimental validation of novel PET degrading eukaryotes through the in silico bioprospectingI of PETases, employing a methodology that combines Hidden Markov Models (HMMs), clustering techniques, molecular docking, and dynamic simulations. A total of 424 putative PETase sequences were identified from 219 eukaryotic organisms, highlighting six sequences with low affinity energies. The Aspergillus luchuensis sequence showed the lowest Gibbs free energy and exhibited stability at different temperatures in molecular dynamics assays.

Cloning, expression, and biochemical characterization of β-etherase LigF from sp. B11.

Lignin, a complex heteropolymer present in plant cell walls, is now recognized as a valuable renewable resource with potential applications in various industries. The lignin biorefinery concept, which aims to convert lignin into value-added products, has gained significant attention in recent years. β-etherases, enzymes that selectively cleave β--4 aryl ether bonds in lignin, have shown promise in lignin depolymerization.

Comparative features between recombinant lipases CALA-like from U. maydis and CALA from C. antarctica in thermal stability and selectivity.

Objectives: Ustilago maydis lipase A (UMLA) expressed in Pichia pastoris was compared with Candida antarctica lipase A (CALA) to study its biochemical properties such as thermostability and selectivity.

Results: UMLA had similar behavior to its homologue CALA regarding the effect of pH and temperature on enzymatic activity, substrate preference and selectivity. Both lipases were active on insoluble triglycerides as well as natural oils and hydrolyzed preferably esters with short and medium acyl and alkyl chains.