PH of nutrient media for the cultivation of fungi

A. Mallinkrodt-Haupt (Derm. Ztschr. Bd. 55, H. 5/6, 1929), studying the effect of the reaction of the nutrient medium on the growth of fungi (various types of trichophytosis, favus and others), as well as the change in this reaction under the influence of the growth of various fungi, the surface tension of the nutrient medium and, finally, enzyme formation, comes to the conclusion that the strains of fungi in the process of their growth increase the alkalinity of the medium, in parallel with which there is an increase in the surface tension; enzyme formation occurs in an alkaline environment and further increases with the growth of fungi.

Interactions of Dehydrogenase Enzymes with Nanoparticles Industrial and Medical Applications and Challenges: Mini-review

: The general overview aimed to increase the current knowledge interactions between dehydrogenase enzymes and nanoparticles, and introduce dehydrogenases for industrial and health purposes. Nanoparticles (NPs) are particles constituting from 1 to 100 nm based on their size with a surrounding interfacial layer. Nanoparticle-Protein interactions include covalent and non-covalent attachments. Several dehydrogenase enzymes (e.g., alcohol dehydrogenase, lactate dehydrogenase, alanine dehydrogenase, glutamate dehydrogenase, leucine dehydrogenase, phenylalanine dehydrogenase, and malate dehydrogenase) are used for immobilization by nanoparticles. Such as magnetic nanoparticles and quantum dots, represent attractive model systems for biological enzyme assemblies and design of bioanalytical sensors. Further, bioconjugation of nanoparticles with dehydrogenase enzymes has broad applications in biocatalysis and nanomedicine for drug discovery. However, studies on the characterization of nanoparticle-enzyme complexes accept apparent that the anatomy and action of enzymes are afflicted by the chemistry of nanoparticle ligand, size, actual, and labeling methods. Moreover, the nanoparticle-protein conjugation revealed increased/decreased enzymatic activity due to nanoparticle features. Thus, this work reviewed the findings of nanoparticle-enzyme interactions for nanotechnology applications and conjugation techniques. We also highlight several challenges associated with the nanoparticle-enzyme interactions, including stability and reusability of the enzymes in nanoparticle-enzyme formation.

Synonymous codon substitutions perturb cotranslational protein folding in vivo and impair cell fitness

In the cell, proteins are synthesized from N to C terminus and begin to fold during translation. Cotranslational folding mechanisms are therefore linked to elongation rate, which varies as a function of synonymous codon usage. However, synonymous codon substitutions can affect many distinct cellular processes, which has complicated attempts to deconvolve the extent to which synonymous codon usage can promote or frustrate proper protein folding in vivo. Although previous studies have shown that some synonymous changes can lead to different final structures, other substitutions will likely be more subtle, perturbing predominantly the protein folding pathway without radically altering the final structure. Here we show that synonymous codon substitutions encoding a single essential enzyme lead to dramatically slower cell growth. These mutations do not prevent active enzyme formation; instead, they predominantly alter the protein folding mechanism, leading to enhanced degradation in vivo. These results support a model in which synonymous codon substitutions can impair cell fitness by significantly perturbing cotranslational protein folding mechanisms, despite the chaperoning provided by the cellular protein homeostasis network.

3,3′-Diindolylmethane Promotes BDNF and Antioxidant Enzyme Formation via TrkB/Akt Pathway Activation for Neuroprotection against Oxidative Stress-Induced Apoptosis in Hippocampal Neuronal Cells

3,3′-Diindolylmethane (DIM), a metabolite of indole-3-carbinol present in Brassicaceae vegetables, possesses various health-promoting effects. Nonetheless, the effect of DIM on neurodegenerative diseases has not been elucidated clearly. In this study, we hypothesized DIM may protect neuronal cells against oxidative stress-induced apoptosis by promoting the formation of brain-derived neurotrophic factor (BDNF) and antioxidant enzymes through stabilizing the activation of the tropomyosin-related kinase receptor B (TrkB) cascade and we investigated the effect of DIM on oxidative stress-mediated neurodegenerative models. DIM protected neuronal cells against oxidative stress-induced apoptosis by regulating the expression of apoptosis-related proteins in glutamate-treated HT-22 cells. Additionally, DIM improved the expression of BDNF and antioxidant enzymes, such as heme oxygenase-1, glutamate-cysteine ligase catalytic subunit, and NAD(P)H quinine oxidoreductase-1, by promoting the activation of the TrkB/protein kinase B (Akt) pathway in the cells. Consistent with in vitro studies, DIM attenuated memory impairment by protecting hippocampal neuronal cells against oxidative damage in scopolamine-treated mice. Conclusionally, DIM exerted neuroprotective and antioxidant actions through the activation of both BDNF production and antioxidant enzyme formation in accordance with the TrkB/Akt pathway in neuronal cells. Such an effect of DIM may provide information for the application of DIM in the prevention of and therapy for neurodegenerative diseases.

Structure and function of urea amidolyase

Urea is the degradation product of a wide range of nitrogen containing bio-molecules. Urea amidolyase (UA) catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source. It is widely distributed in fungi, bacteria and other microorganisms, and plays an important role in nitrogen recycling in the biosphere. UA is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains, which catalyze sequential reactions. In some organisms UC and AH are encoded by separated genes. We present here structure of the Kluyveromyces lactis UA (KlUA). The structure revealed that KlUA forms a compact homo-dimer with a molecular weight of 400 kDa. Structure inspired biochemical experiments revealed the mechanism of its reaction intermediate translocation, and that the KlUA holo-enzyme formation is essential for its optimal activity. Interestingly, previous studies and ours suggest that UC and AH encoded by separated genes probably do not form a KlUA-like complex, consequently they might not catalyze the urea to ammonium conversion as efficiently.

In VitroCross-Linking of Mycobacterium tuberculosis Peptidoglycan by l,d-Transpeptidases and Inactivation of These Enzymes by Carbapenems

ABSTRACTTheMycobacterium tuberculosispeptidoglycan is cross-linked mainly byl,d-transpeptidases (LDTs), which are efficiently inactivated by a single β-lactam class, the carbapenems. Development of carbapenems for tuberculosis treatment has recently raised considerable interest since these drugs, in association with the β-lactamase inhibitor clavulanic acid, are uniformly active against extensively drug-resistantM. tuberculosisand kill both exponentially growing and dormant forms of the bacilli. We have purified the fivel,d-transpeptidase paralogues ofM. tuberculosis(Mt1 to -5) and compared their activities with those of peptidoglycan fragments and carbapenems. The five LDTs were functionalin vitrosince they were active in assays of peptidoglycan cross-linking (Mt5), β-lactam acylation (Mt3), or both (Mt1, Mt2, and Mt4). Mt3 was the only LDT that was inactive in the cross-linking assay, suggesting that this enzyme might be involved in other cellular functions such as the anchoring of proteins to peptidoglycan, as shown inEscherichia coli. Inactivation of LDTs by carbapenems is a two-step reaction comprising reversible formation of a tetrahedral intermediate, the oxyanion, followed by irreversible rupture of the β-lactam ring that leads to formation of a stable acyl enzyme. Determination of the rate constants for these two steps revealed important differences (up to 460-fold) between carbapenems, which affected the velocity of oxyanion and acyl enzyme formation. Imipenem inactivated LDTs more rapidly than ertapenem, and both drugs were more efficient than meropenem and doripenem, indicating that modification of the carbapenem side chain could be used to optimize their antimycobacterial activity.

A simplified model for A. Niger FS3 growth during phytase formation in solid State fermentation

A simplified model to describe fungal growth during citric pulp fermentation for phytase production was described for the first time. Experimental data for biomass growth were adjusted to classical mathematical growth models (Monod and Logistic). The Monod model predictions showed good agreement with the experimental results for biomass concentration during 96 hours of fermentation. Parameters such as yield of biomass from oxygen (Y X/O), maintenance coefficient (m) and specific growth rate (µ) were compared showing a good correlation between the data and the model. An alternative method for biomass determination in this process was developed since a great correlation was found between biomass growth and enzyme formation.