Exploring soybean cultivar susceptibility to sudden death syndrome: Insights into isoflavone responses and biocontrol potential.

Sudden Death Syndrome (SDS) caused by Fusarium tucumaniae is a significant threat to soybean production in Argentina. This study assessed the susceptibility of SY 3 × 7 and SPS 4 × 4 soybeans cultivars to F. tucumaniae and studied changes in root isoflavone levels after infection.

High-efficiency novel extraction process of target polyphenols using enzymes in hydroalcoholic media.

Agro-industrial by-products are a sustainable source of natural additives that can replace the synthetic ones in the food industry. Grape pomace is an abundant by-product that contains about 70% of the grape's polyphenols. Polyphenols are natural antioxidants with multiple health-promoting properties.

Soybean (Glycine max) hull valorization through the extraction of polyphenols by green alternative methods.

Soybean is one of the greatest crops in the world, with about 348.7 million tons being produced in 2018. Soybean hull is a by-product produced during the processing of soybean to obtain flour and oil.

Valorization of two agroindustrial wastes to produce alpha-amylase enzyme from Aspergillus oryzae by solid-state fermentation.

The global amount of soybean and wheat produced is about 350 and 750 million metric tons every year, respectively. In consequence, huge amounts of waste are produced from them. The aim of this work was to employ two wastes -soybean husk and flour mill waste- to produce high quantities of alpha-amylase enzyme.

Recovery of phenolic antioxidants from Syrah grape pomace through the optimization of an enzymatic extraction process.

Phenolic compounds are highly valuable products that remain trapped in grape pomace, an abundant winery by-product. Therefore, efficient extraction procedures of these compounds represent a route for grape pomace valorisation. Here we performed a screening of the factors affecting the aqueous enzymatic extraction of phenolic compounds from Syrah grape pomace, including the following independent variables: temperature, pH, pectinase, cellulase and tannase; and a subsequent optimization through response surface methodology.

Overcoming differences: The catalytic mechanism of metallo-β-lactamases.

Metallo-β-lactamases are the latest resistance mechanism of pathogenic and opportunistic bacteria against carbapenems, considered as last resort drugs. The worldwide spread of genes coding for these enzymes, together with the lack of a clinically useful inhibitor, have raised a sign of alarm. Inhibitor design has been mostly impeded by the structural diversity of these enzymes.

Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

Understanding the driving forces behind protein evolution requires the ability to correlate the molecular impact of mutations with organismal fitness. To address this issue, we employ here metallo-β-lactamases as a model system, which are Zn(II) dependent enzymes that mediate antibiotic resistance. We present a study of all the possible evolutionary pathways leading to a metallo-β-lactamase variant optimized by directed evolution.

Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.

The production of β-lactamase enzymes is one of the most distributed resistance mechanisms towards β-lactam antibiotics. Metallo-β-lactamases constitute a worrisome group of these kinds of enzymes, since they present a broad spectrum profile, being able to hydrolyze not only penicillins, but also the latest generation of cephalosporins and carbapenems, which constitute at present the last resource antibiotics. The VIM, IMP, and NDM enzymes comprise the main groups of clinically relevant metallo-β-lactamases.

Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.

A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent β-lactamases. We show that metal uptake leading to an active dinuclear enzyme in the periplasmic space of Gram-negative bacteria is ensured by a cysteine residue, an unusual metal ligand in oxidizing environments. Kinetic, structural and affinity data show that such Zn(II)-cysteine interaction is an adaptive trait that tunes the metal binding affinity, thus enabling antibiotic resistance at restrictive Zn(II) concentrations.