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de Araújo Amanda Dias,de Barros Pimentel Maria do Carmo,Santos Camila da Silva,da Silva Roberto Afonso,Cadena Pabyton Gonçalves,da Silva Nicácio Henrique,Gusmão Norma Buarque,Sleifer Bruno Alonso,da S 경희대학교 융합한의과학연구소 2021 Oriental Pharmacy and Experimental Medicine Vol.21 No.4
The focus of this study was to evaluate the presence and type of carbohydrates and phenolic molecules inaqueous extract (Aq-E) of Alternanthera brasiliana fresh leaves and its antioxidant and antimicrobial activities and cytotoxicity in vitro. The amount and types of the carbohydrates were measured by colorimetric and TLC methods. Phenolic compounds was detected by colorimetric assay and analysed by HPLC profiles. The antioxidant activity was evaluated by ABTS and Phosphomolybdenum methods. Antimicrobial activity was tested by microdilution method using microorganism models and antibiotic as positive control, the cytotoxicity in vitro was tested using Artemia salina. The results showed the presence of high amount of total sugars and uronic acids. TLC chromatograms showed mainly D-glucose, D-fructose, oligosaccharides and uronic acids in the Aq-E and a sugar alcohol in the methanolic extract. The colorimetric determination showed high concentration of phenolic compounds, which were visualised on the HPLC profiles, such as chemical markers of the Amaranthaceae family and several phenolic acids and flavonoids. The Aq-E demonstrated optimal antioxidant activities. The most important results were the excellent antibacterial and bactericidal activities against Mycobacterium megmatis (MIC = 15.6 µg/mL and MBC = 1000 µg/mL) and antimicrobial activity against Candida albicans (MIC = 31.2 µg/mL) and low cytotoxicity. Further possibilities for this plant extract will be to improve the pharmacological potential for developing new herbal medicines and possibly to study its association to allopathic antibiotics for prevention or treatment of infection diseases.
Production of Saccharogenic and Dextrinogenic Amylases by Rhizomucor pusillus A 13.36
Silva Tony M.,Attili-Angelis Derlene,Carvalho Ana Flavia Azevedo,Silva Roberto Da,Boscolo Mauricio,Gomes Eleni The Microbiological Society of Korea 2005 The journal of microbiology Vol.43 No.6
A newly-isolated thermophilic strain of the zygomycete fungus Rhizomucor pusillus 13.36 produced highly active dextrinogenic and saccharogenic enzymes. Cassava pulp was a good alternative substrate for amylase production. Dextrinogenic and saccharogenic amylases exhibited optimum activities at a pH of 4.0-4.5 and 5.0 respectively and at a temperature of $75^{\circ}C$. The enzymes were highly thermostable, with no detectable loss of saccharogenic or dextrinogenic activity after 1 hand 6 h at $60^{\circ}C$, respectively. The saccharogenic activity was inhibited by $Ca^{2+}$ while the dextrinogenic was indifferent to this ion. Both activities were inhibited by $Fe^{2+}\;and\;Cu^{2+}$ Hydrolysis of soluble starch by the crude enzyme yielded $66\%$ glucose, $19.5\%$ maltose, $7.7\%$ maltotriose and $6.6\%$ oligosaccharides.
Imaging evaluation of patellofemoral joint instability: a review
( Roberto M. Barbosa ),( Manuel Vieira Da Silva ),( Carlos Sampaio Macedo ),( Cristina P. Santos ) 대한슬관절학회 2023 대한슬관절학회지 Vol.35 No.-
The multifactorial origin of anterior knee pain in patellofemoral joint disorders leads to a demanding diagnostic process. Patellofemoral misalignment is pointed out as one of the main causes of anterior knee pain. The main anatomical risk factors of patellofemoral instability addressed in the literature are trochlear dysplasia, abnormal patellar height, and excessive tibial tubercle-trochlear groove distance. Diagnostic imaging of the patellofemoral joint has a fundamental role in assessing these predisposing factors of instability. Extensive work is found in the literature regarding the assessment of patellofemoral instability, encompassing several metrics to quantify its severity. Nevertheless, this process is not well established and standardized, resulting in some variability and inconsistencies. The significant amount of scattered information regarding the patellofemoral indices to assess the instability has led to this issue. This review was conducted to collect all this information and describe the main insights of each patellofemoral index presented in the literature. Five distinct categories were created to organize the patellofemoral instability indices: trochlear dysplasia, patellar height, patellar lateralization, patellar tilt, and tibial tubercle lateralization.
Biocompatibility and bioactive potential of the NeoMTA Plus endodontic bioceramic-based sealer
Hoshino Roberto Alameda,Delfino Mateus Machado,da Silva Guilherme Ferreira,Guerreiro-Tanomaru Juliane Maria,Tanomaru-Filho Mário,Sasso-Cerri Estela,Cerri Paulo Sérgio 대한치과보존학회 2021 Restorative Dentistry & Endodontics Vol.46 No.1
Objectives: This study evaluated the biocompatibility and bioactive potential of NeoMTA Plus mixed as a root canal sealer in comparison with MTA Fillapex. Materials and Methods: Polyethylene tubes filled with NeoMTA Plus (n = 20), MTA Fillapex (n = 20), or nothing (control group, CG; n = 20) were inserted into the connective tissue in the dorsal subcutaneous layer of rats. After 7, 15, 30 and 60 days, the specimens were processed for paraffin embedding. The capsule thickness, collagen content, and number of inflammatory cells (ICs) and interleukin-6 (IL-6) immunolabeled cells were measured. von Kossa-positive structures were evaluated and unstained sections were analyzed under polarized light. Two-way analysis of variance was performed, followed by the post hoc Tukey test (p ≤ 0.05). Results: At 7 days, the capsules around NeoMTA Plus and MTA Fillapex had more ICs and IL-6-immunostained cells than the CG. However, at 60 days, there was no significant difference in the IC number between NeoMTA Plus and the CG (p = 0.1137) or the MTA Fillapex group (p = 0.4062), although a greater number of IL-6-immunostained cells was observed in the MTA Fillapex group (p = 0.0353). From 7 to 60 days, the capsule thickness of the NeoMTA Plus and MTA Fillapex specimens significantly decreased, concomitantly with an increase in the collagen content. The capsules around root canal sealers showed positivity to the von Kossa stain and birefringent structures. Conclusions: The NeoMTA Plus root canal sealer is biocompatible and exhibits bioactive potential.
Production of Saccharogenic and Dextrinogenic Amylases by Rhizomucor pusillus A 13.36
Tony M. Silva,Derlene Attili-Angelis,Ana Flavia Azevedo Carvalho,Roberto Da Silva,Mauricio Boscolo,Eleni Gomes 한국미생물학회 2005 The journal of microbiology Vol.43 No.6
A newly-isolated thermophilic strain of the zygomycete fungus Rhizomucor pusillus 13.36 produced highly active dextrinogenic and saccharogenic enzymes. Cassava pulp was a good alternative substrate for amylase production. Dextrinogenic and saccharogenic amylases exhibited optimum activities at a pH of 4.0-4.5 and 5.0 respectively and at a temperature of 75oC. The enzymes were highly thermostable, with no detectable loss of saccharogenic or dextrinogenic activity after 1 h and 6 h at 60oC, respectively. The saccharogenic activity was inhibited by Ca2+ while the dextrinogenic was indifferent to this ion. Both activities were inhibited by Fe2+ and Cu2+ Hydrolysis of soluble starch by the crude enzyme yielded 66% glucose, 19.5% maltose, 7.7% maltotriose and 6.6% oligosaccharides.
Conditions to avoid synchronization effects in lateral vibration of footbridges
Andrade, Alexandre R.,Pimentel, Roberto L.,Silva, Simplicio A. da,Souto, Cicero da R. Techno-Press 2022 Structural monitoring and maintenance Vol.9 No.2
Lateral vibrations of footbridges may induce synchronization between pedestrians and structure itself, resulting in amplification of such vibrations, a phenomenon identified by lock-in. However, investigations about accelerations and frequencies of the structural movement that are related to the occurrence of synchronization are still incipient. The aim of this paper is to investigate conditions that could lead to avoidance of synchronization among pedestrians themselves and footbridge, expressed in terms of peak acceleration. The focus is on the low acceleration range, employed in some guidelines as a criterion to avoid synchronization. An experimental campaign was carried out, employing a prototype footbridge that was set into oscillatory motion through a pneumatic exciter controlled by a fuzzy system, with controlled frequency and amplitude. Test subjects were then asked to cross the oscillating structure, and accelerations were simultaneously recorded at the structure and at the subject's waist. Pattern and phase differences between these signals were analysed. The results showed that test subjects tended to keep their walking patterns without synchronization induced by the vibration of the structure, for structural peak acceleration values up to 0.18 m/s<sup>2</sup>, when frequencies of oscillation were around 0.8 to 0.9 Hz. On the other hand, for frequencies of oscillation below 0.7 Hz, structural peak accelerations up to 0.30 m/s<sup>2</sup> did not induce synchronization.
Carvalho Ana Flavia Azevedo,Goncalves Aline Zorzetto,Silva Roberto da,Gomes Eleni The Microbiological Society of Korea 2006 The journal of microbiology Vol.44 No.3
The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (${\alpha}$-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II ${\alpha}$-glucosidase. The optimum temperature of the enzyme was $70^{\circ}C$. In addition, the enzyme was highly thermostable (100% stability for 10 h at $60^{\circ}C$ and a half-life of 15 min at $80^{\circ}C$), and stable within a wide pH range.
Ana Flavia Azevedo Carvalho,Aline Zorzetto Gonclves,Roberto da Silva,Eleni Gomes 한국미생물학회 2006 The journal of microbiology Vol.44 No.3
The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (α-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II α-glucosidase. The optimum temperature of the enzyme was 70°C. In addition, the enzyme was highly thermostable (100% stability for 10 h at 60°C and a half-life of 15 min at 80°C), and stable within a wide pH range.
Ana Flávia Azevedo Carvalho,Maurício Boscolo,Roberto da Silva,Henrique Ferreira,Eleni Gomes 한국미생물학회 2010 The journal of microbiology Vol.48 No.4
Αn α-glucosidase enzyme produced by the fungus Thermoascus aurantiacus CBMAI 756 was purified by ultra filtration, ammonium sulphate precipitation, and chromatography using Q Sepharose, Sephacryl S-200, and Superose 12 columns. The apparent molecular mass of the enzyme was 83 kDa as determined in gel electrophoresis. Maximum activity was observed at pH 4.5 at 70°C. Enzyme showed stability stable in the pH range of 3.0-9.0 and lost 40% of its initial activity at the temperatures of 40, 50, and 60°C. In the presence of ions Na+, Ba2+, Co2+, Ni2+, Mg2+, Mn2+, Al3+, Zn2+, Ca2+ this enzyme maintained 90-105% of its maximum activity and was inhibited by Cr3+, Ag+, and Hg2+. The enzyme showed a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides and α-PNPG. The Km measured for the α-glucosidase was 0.07 μM, with a Vmax of 318.0 μmol/min/mg.