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1.
Hist. ciênc. saúde-Manguinhos ; 21(4): 1323-1340, Oct-Dec/2014. tab
Article in Portuguese | LILACS | ID: lil-732512

ABSTRACT

Discutem-se aqui as formas de encaminhamento de pacientes ao Hospital Adauto Botelho, localizado em Cariacica, Espírito Santo. A pesquisa se deu por meio de prontuários médicos datados desde a inauguração em 1954 e de depoimentos de pessoas que trabalharam lá durante a segunda metade do século XX. Foram analisados 102 prontuários e entrevistadas quatro pessoas. A pesquisa dos prontuários mostra forte inserção da Chefatura de Polícia no processo de internação. As falas dos entrevistados reiteram esse ponto, mostrando também a longa duração das internações. São as histórias de vida dos internos que dão o tom deste trabalho. Conclui-se, a partir delas, que o Hospital Adauto Botelho, mais que uma instituição de tratamento, era um espaço de confinamento.


This paper discusses the procedures for referring patients to Adauto Botelho Hospital, in Cariacica, Espírito Santo state, Brazil. The research is based on the medical records since its inauguration in 1954 and statements by people who worked there in the second half of the twentieth century. One hundred and two records were analyzed and four people were interviewed. The records revealed the active involvement of the Chief of Police in hospitalizations. The interviews corroborate this, while also showing the long duration of the hospitalizations. The tone of the paper is set by the life stories of the people hospitalized there. The conclusion is that this hospital served not so much for treatment as for confinement.


Subject(s)
Animals , Neoplasm Proteins/metabolism , Peptide Chain Elongation, Translational , RNA Polymerase I/metabolism , Transcription Factors, General , Transcription, Genetic , Transcriptional Elongation Factors , Transcription Factors/metabolism , Amino Acid Sequence , DNA Polymerase II/metabolism , Detergents/metabolism , Electrophoresis, Polyacrylamide Gel , Molecular Sequence Data , Sarcosine/analogs & derivatives , Sarcosine/metabolism , Xenopus
2.
Braz. j. microbiol ; 45(3): 903-910, July-Sept. 2014. ilus, graf
Article in English | LILACS | ID: lil-727019

ABSTRACT

A soil screened Bacillus flexus XJU-1 was induced to simultaneously produce alkaline amylase, alkaline lipase and alkaline protease at their optimum levels on a common medium under submerged fermentation. The basal cultivation medium consisted of 0.5% casein, 0.5% starch and 0.5% cottonseedoil as an inducer forprotease, amylase, and lipase, respectively. The casein also served as nitrogen source for all 3 enzymes. The starch was also found to act as carbon source additive for both lipase and protease. Maximum enzyme production occurred on fermentation medium with 1.5% casein, 1.5% soluble starch, 2% cottonseed oil, 2% inoculum size, initial pH of 11.0, incubation temperature of 37 °C and 1% soybean meal as a nitrogen source supplement. The analysis of time course study showed that 24 h was optimum incubation time for amylase whereas 48 h was the best time for both lipase and protease. After optimization, a 3.36-, 18.64-, and 27.33-fold increase in protease, amylase and lipase, respectively was recorded. The lipase was produced in higher amounts (37.72 U/mL) than amylase and protease about 1.27 and 5.85 times, respectively. As the 3 enzymes are used in detergent formulations, the bacterium can be commercially exploited to secrete the alkaline enzymes for use in detergent industry. This is the first report for concomitant production of 3 alkaline enzymes by a bacterium.


Subject(s)
Amylases/metabolism , Bacillus/enzymology , Bacillus/metabolism , Bacterial Proteins/metabolism , Detergents/metabolism , Endopeptidases/metabolism , Enzyme Inhibitors/metabolism , Lipase/metabolism , Bacillus/growth & development , Bacillus/isolation & purification , Carbon/metabolism , Culture Media/chemistry , Fermentation , Hydrogen-Ion Concentration , Nitrogen/metabolism , Soil Microbiology , Temperature , Time Factors
3.
Electron. j. biotechnol ; 16(3): 3-3, May 2013. ilus, tab
Article in English | LILACS | ID: lil-684001

ABSTRACT

Background: Proteases constitute the largest product segment in the global industrial enzymes market; they are used in food, pharmaceutical, leather, textile, wood and detergent industries. Alkaline proteases improve the cleaning efficiency of detergents and represent one of the most successful applications of modern industrial biotechnology. The aim of this work was to study the performance of two alkaline phytoproteases, araujiain (Araujia hortorum Fourn.) and asclepain (Asclepias curassavica L.), for their potential application as additive in laundry detergent formulations. Results: The effect of pure non-ionic and ionic surfactants on proteolytic activity of araujiain and asclepain was analyzed measuring the remaining activity after 1 hr of incubation of those enzymes in aqueous solutions of surfactants at different concentrations (0.1, 0.4 and 1% v/v) and temperatures (25, 40 and 60ºC). Besides, the compatibility of the enzymes with six commercial laundry detergents was also studied measuring the remaining proteolytic activity at 37ºC after 1 hr. Commercial detergent components influenced in different ways on araujiain and asclepain, in spite of the similar behaviour of the two enzymes in buffer. In commercial detergent solutions, araujiain expressed between 60% and 140% of its remaining proteolytic activity in buffer (pH 8.5) at 37ºC after 1 hr, while asclepain, was practically inactivate in most of them at the same conditions. Conclusions: Proteolytic extract of Araujia hortorum fulfilled all the requirements for its application as additive for laundry detergents: high stability in a broad temperature range (25-70ºC), high activity in alkaline pH (7.5-9.5) and very good compatibility with the commercial detergent additives. Nevertheless, in spite of its high stability and activity in buffer, the proteolytic extract of Asclepias curassavica did not show the same performance than araujiain.


Subject(s)
Endopeptidases/metabolism , Detergents/metabolism , Endopeptidases/isolation & purification , Surface-Active Agents/metabolism , Biotechnology
4.
Indian J Biochem Biophys ; 1990 Apr; 27(2): 112-7
Article in English | IMSEAR | ID: sea-28379

ABSTRACT

The interaction of hexadecyltrimethylammonium bromide (CTAB) with two yeast cells, Kluyveromyces fragilis and Saccharomyces cerevisiae, has been studied. Strong binding of CTAB to the cell was inferred from 1H and 13C NMR studies, the probable site of binding being the cell-surface. 13C and 31P NMR studies have indicated facilitation of free passage of molecules from outside to inside the cell and vice versa on treatment with CTAB. 31P NMR studies showed that intracellular pH (pHi) was affected in presence of CTAB and the rate of exchange of H+ and PO4(-3) between outside and inside of the cell was 508 s-1. CTAB treatment of yeast cells also affected pH and conductance measurements of the cell-suspension. There was a marked difference in the pH changes around the critical micellar concentration (CMC) of CTAB. The observed pH changes were dependent on (i) CTAB concentration, (ii) pH of the cell-suspension and (iii) pK values of groups from molecules released from the cell. Also, it was shown that ionisation of phosphate diester from polar head groups of membranes constituting cell surface enhanced CTAB binding. Conductance measurements have shown that observed changes were independent of the concentration of yeast cells, but probably dependent on CMC of CTAB.


Subject(s)
Cetrimonium Compounds/metabolism , Detergents/metabolism , Quaternary Ammonium Compounds/metabolism , Saccharomycetales/metabolism , Surface-Active Agents/metabolism
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