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1.
Sci Rep ; 10(1): 9446, 2020 Jun 10.
Article in English | MEDLINE | ID: mdl-32523126

ABSTRACT

SnO particles were synthesized by an alkali-assisted hydrothermal and microwave methods. The aqueous-based reactions were carried out at pH ~ 8, under inert atmosphere (Ar). The reactions were taken under different times, and a full XRD structural analysis was made to evaluate the conversion from the Sn6O4(OH)4 intermediate to SnO particles. Williamson-Hall analysis showed that the size and strain of the SnO particles were time and route treatment dependent. Microwave heating yielded a single tetragonal SnO phase after 1 h of thermal treatment, and TEM images revealed spherical-shaped SnO nanoparticles with an average size of 9(1) nm. While by the hydrothermal treatment single SnO phase was obtained only after 4 hours, yielding non-uniform and elongated particles with sub-micrometric size. A dissolution-recrystallization process was taken into account as the mechanism for SnO particles formation, in which hydroxylated complexes, Sn2(OH)6-2, then condense to form the oxide. The time-shorting reaction provided by the microwave-assisted synthesis may be attributed to better heat distribution.

2.
Osteoporos Int ; 31(9): 1807-1815, 2020 Sep.
Article in English | MEDLINE | ID: mdl-32383065

ABSTRACT

This study evaluated the peri-implant bone repair in orchiectomized rats receiving intermittently PTH 1-34. The treatment returned the bone quality and quantity of the animals to normal in the computerized microtomography, laser confocal microscopy, and histological analysis. The PTH 1-34 promoted marked bone formation with increased volume, improved quality, and greater bone turnover. INTRODUCTION: Osteoporosis can be a problem in implant osseointegration. So this study aimed to evaluate the quantity and quality of peri-implant bone repair in orchiectomized Wistar rats receiving intermittently administered PTH 1-34. METHODS: Animals (n = 24) were divided into 3 groups: healthy control (SHAM), orchiectomized (ORQ), and orchiectomized and treated with 0.5 µg/kg/day PTH 1-34 (TERI), and each received an implant in the right and left tibial metaphysis, which was allowed to repair for 60 days. The resultant bone formation was evaluated through computerized microtomography (micro-CT) to compare the percent bone volume (BV/TV), trabecular thickness (Tb.Th), trabecular number and separation (Tb.N, Tb.Sp), and bone implant contact (BIC) through the intersection surface (i.S) between groups. Laser confocal microscopy was used to evaluate fluorochrome areas for mineral apposition rate (MAR) and neoformed bone area (NBA). In addition, histological evaluation of calcified tissues with Stevenel blue and alizarin red staining was performed. RESULTS: Treatment with PTH 1-34 returned the bone quality and quantity of the osteoporotic animal to normal, as the TERI group presented statistically significant higher values for BV/TV, Tb.Th, and BIC parameters compared with ORQ (p < 0.05), but when compared with SHAM (p > 0.05), no statistical difference was noted. In addition, in the bone turnover analysis (MAR, NBA) for TERI, the highest results are presented, followed by SHAM, and then ORQ (TERI × ORQ: p < 0.05). CONCLUSIONS: Intermittent treatment with PTH 1-34 on orchiectomized animals promoted marked bone formation with increased volume, improved quality, and greater bone turnover in the peri-implant space, returning the bone quality and quantity to the present standard in healthy animals.


Subject(s)
Osteoporosis , Teriparatide , Animals , Bone Density , Bone and Bones , Female , Humans , Osseointegration , Osteoporosis/drug therapy , Ovariectomy , Rats , Rats, Wistar , X-Ray Microtomography
3.
Appl Biochem Biotechnol ; 172(7): 3670-85, 2014 Apr.
Article in English | MEDLINE | ID: mdl-24562979

ABSTRACT

Nowadays, hydrogen produced globally has been synthesized from fossil fuel with limited source. Therefore, research has been developed in order to explore biological H2 production by dark fermentation. The purpose of this work was to evaluate the effect of initial pH and ferrous sulfate and ammonium sulfate concentrations on the production of biohydrogen by dark fermentation. The process was carried out in batch mode under anaerobic conditions, in the absence of light, and at standard room temperature and pressure. A microbial consortium provided by the effluent treatment plant of a local dairy company was inoculated into a synthetic medium supplemented with cheese whey permeate (20 g/L of lactose) as a carbon source. The influence of three variables was analyzed by a central composite design 2((3)), and the optimum results of hydrogen yield (4.13 mol H2/mol lactose) and productivity (86.31 mmol H2/L/day) were achieved at initial pH 7.0 and FeSO4 and (NH4)2SO4 concentrations of 0.6 and 1.5 g/L, respectively. Under these conditions, the kinetic parameters of fermentation were investigated by analyzing the profile of H2 yield and productivity, metabolite concentrations, pH, and concentration of dissolved iron. In the kinetic analysis, the modified Gompertz equation described adequately the fermentative hydrogen production from cheese whey permeate (R (2) = 0.98). The profile of ethanol and volatile organic acids showed that lactic acid and butyric acid were the main metabolites produced, and the sum of both by-products corresponded to about 58 % of the total metabolites.


Subject(s)
Bacteria/metabolism , Hydrogen/metabolism , Industrial Microbiology/methods , Lactose/metabolism , Microbial Consortia , Bioreactors/microbiology , Cheese/analysis , Fermentation , Industrial Microbiology/instrumentation , Waste Products/analysis
4.
Protein Sci ; 9(11): 2285-91, 2000 Nov.
Article in English | MEDLINE | ID: mdl-11305239

ABSTRACT

The three-dimensional (3D) structure of fructan biosynthetic enzymes is still unknown. Here, we have explored folding similarities between reported microbial and plant enzymes that catalyze transfructosylation reactions. A sequence-structure compatibility search using TOPITS, SDP, 3D-PSSM, and SAM-T98 programs identified a beta-propeller fold with scores above the confidence threshold that indicate a structurally conserved catalytic domain in fructosyltransferases (FTFs) of diverse origin and substrate specificity. The predicted fold appeared related to that of neuraminidase and sialidase, of glycoside hydrolase families 33 and 34, respectively. The most reliable structural model was obtained using the crystal structure of neuraminidase (Protein Data Bank file: 5nn9) as template, and it is consistent with the location of previously identified functional residues of bacterial levansucrases (Batista et al., 1999; Song & Jacques, 1999). The sequence-sequence analysis presented here reinforces the recent inclusion of fungal and plant FTFs into glycoside hydrolase family 32, and suggests a modified sequence pattern H-x (2)-[PTV]-x (4)-[LIVMA]-[NSCAYG]-[DE]-P-[NDSC][GA]3 for this family.


Subject(s)
Catalytic Domain , Hexosyltransferases/chemistry , Amino Acid Sequence , Databases, Factual , Models, Molecular , Molecular Sequence Data , Phylogeny , Plant Proteins/chemistry , Protein Folding , Sequence Homology, Amino Acid , Software , Substrate Specificity
5.
Biochem J ; 337 ( Pt 3): 503-6, 1999 Feb 01.
Article in English | MEDLINE | ID: mdl-9895294

ABSTRACT

beta-Fructofuranosidases share a conserved aspartic acid-containing motif (Arg-Asp-Pro; RDP) which is absent from alpha-glucopyranosidases. The role of Asp-309 located in the RDP motif of levansucrase (EC 2.4.1.10) from Acetobacter diazotrophicus SRT4 was studied by site-directed mutagenesis. Substitution of Asp-309 by Asn did not affect enzyme secretion. The kcat of the mutant levansucrase was reduced 75-fold, but its Km was similar to that of the wild-type enzyme, indicating that Asp-309 plays a major role in catalysis. The two levansucrases showed optimal activity at pH 5.0 and yielded similar product profiles. Thus the mutation D309N affected the efficiency of sucrose hydrolysis, but not the enzyme specificity. Since the RDP motif is present in a conserved position in fructosyltransferases, invertases, levanases, inulinases and sucrose-6-phosphate hydrolases, it is likely to have a common functional role in beta-fructofuranosidases.


Subject(s)
Acetobacter/enzymology , Asparagine/genetics , Aspartic Acid/genetics , Conserved Sequence , Hexosyltransferases/metabolism , Sucrose/metabolism , Acetobacter/genetics , Amino Acid Sequence , Amino Acid Substitution , Chromatography, High Pressure Liquid , Hexosyltransferases/genetics , Hydrolysis , Mutagenesis, Site-Directed
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