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Β-glucosidase (BGLs) act synergistically with endoglucanases and exoglucanases and then are of great interest for biomass conversion into bioethanol. Thus, the aim of the current study is to produce a recombinant β-glycosidase from Moniliophtora perniciosa expressed in Escherichia coli cells. Enzyme coding sequence expression was confirmed through Sanger sequencing after using wheat bran (WB) and carboxymethylcellulose (CMC) as fungal growth media. Synthetic gene betaglyc-GH1 with optimized codons for E. coli expression was cloned in pET-28a. β-glucosidase recombinant (GH1chimera) was purified using a nickel column and its identity was confirmed through mass spectrometry. The recombinant enzyme presented an apparent molecular mass of 53.23 kDa on SDS-PAGE. Recombinant β-glucosidase has shown hydrolytic activity using p-nitrophenyl-β-D-glycopyranoside (pNPG) as substrate and maximum activity at pH 4.6 and 65 °C. Thus, the results indicate that the application of the GH1chimera in the hydrolysis of lignocellulosic materials to obtain glucose monomers can be efficient., Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-024-04128-x., Competing Interests: Conflict of interestThe authors declare no competing interests., (© King Abdulaziz City for Science and Technology 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.)

β-Glucosidases (BGLs) belong to the group of enzymes of cellulases and act in the last stage of cellulose degradation, releasing glucose molecules, eliminating the inhibitory effect of cellobiose. This study focused on the production, characterization, and application of BGL from Moniliophthora perniciosa in the hydrolysis of pretreated sugarcane bagasse (3% NaOH + 6% Na 2 SO 3 ), with varying enzymatic loads and reaction times. The enzyme showed an optimum pH of 4.5 and 60°C. It was stable at all temperatures analyzed (50-90°C) and retained about 100% of its activity at 50°C after 60 min of incubation. Among the ions analyzed, BaCl 2 increased BGL activity 9.04 ± 1.41 times. The maximum production of reducing sugars (89.15%) was achieved after 48 h with 10 mg of protein., (© 2021 International Union of Biochemistry and Molecular Biology, Inc.)

Background: Elderly men have been characterized as a group vulnerable to suicide, motivated by loneliness, loss of loved ones and feelings of uselessness to family members., Objectives: To ascertain the prevalence of different mental disorders among elderly men who attempted suicide., Design and Setting: Systematic review of observational studies developed as a result of a partnership between two postgraduate schools (Lagarto and Uberlândia)., Methods: An electronic search was performed in eight electronic databases, including "grey literature", in January 2019. Observational studies that assessed mental disorders among men older than 60 years who attempted suicide were eligible for inclusion., Results: Among the disorders evaluated, mood disorders had the highest prevalence (42.0%; 95% confidence interval, CI: 31.0-74.0%; I2: 0.0%; P = 0.763), followed by substance use-related disorders (41.0%; 95% CI: 8.0-74.0%; I2: 96.4; P < 0.001) and, lastly, schizophrenic disorders (5.0%; 95% CI: 0.0%-14.0%; I2: 80.3%; P = 0.024)., Conclusions: It seems that mood disorders and substance use-related disorders are quite prevalent among elderly men with mental disorders who attempted suicide. It is important to consider the role of healthcare services in making early diagnoses of mental disorders among elderly men, in order to diminish the chances of suicide attempts among them., Systematic Review Registration: CRD42018105981.

Background: A pathophysiological link exists between dysregulation of MEF2C transcription factors and heart failure (HF), but the underlying mechanisms remain elusive. Alternative splicing of MEF2C exons α, β and γ provides transcript diversity with gene activation or repression functionalities., Methods: Neonatal and adult rat ventricular myocytes were used to overexpress MEF2C splicing variants γ+ (repressor) or γ-, or the inactive MEF2Cγ+23/24 (K23T/R24L). Phenotypic alterations in cardiomyocytes were determined by confocal and electron microscopy, flow cytometry and DNA microarray. We used transgenic mice with cardiac-specific overexpression of MEF2Cγ+ or MEF2Cγ- to explore the impact of MEF2C variants in cardiac phenotype. Samples of non-infarcted areas of the left ventricle from patients and mouse model of myocardial infarction were used to detect the expression of MEF2Cγ+ in failing hearts., Findings: We demonstrate a previously unrealized upregulation of the transrepressor MEF2Cγ+ isoform in human and mouse failing hearts. We show that adenovirus-mediated overexpression of MEF2Cγ+ downregulates multiple MEF2-target genes, and drives incomplete cell-cycle reentry, partial dedifferentiation and apoptosis in the neonatal and adult rat. None of these changes was observed in cardiomyocytes overexpressing MEF2Cγ-. Transgenic mice overexpressing MEF2Cγ+, but not the MEF2Cγ-, developed dilated cardiomyopathy, correlated to cell-cycle reentry and apoptosis of cardiomyocytes., Interpretation: Our results provide a mechanistic link between MEF2Cγ+ and deleterious abnormalities in cardiomyocytes, supporting the notion that splicing dysregulation in MEF2C towards the selection of the MEF2Cγ+ variant contributes to the pathogenesis of HF by promoting cardiomyocyte dropout., Funding: São Paulo Research Foundation (FAPESP); Brazilian National Research Council (CNPq)., Competing Interests: Declaration of competing interest The authors declare that they have no conflict of interest., (Copyright © 2019 The Authors. Published by Elsevier B.V. All rights reserved.)