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1.
Electron. j. biotechnol ; 43: 1-7, Jan. 2020. tab, graf, ilus
Artigo em Inglês | LILACS | ID: biblio-1087520

RESUMO

Background: Textile industry not only plays a vital role in our daily life but also a prominent factor in improving global economy. One of the environmental concern is it releases huge quantities of toxic dyes in the water leading to severe environmental pollution. Bacterial laccase and azoreductase successfully oxidize complex chemical structure of nitrogen group-containing azo dyes. Additionally, the presence of textile dye infuriates bacterial peroxidase to act as a dye degrading enzyme. Our present study deals with three textile dye degrading enzymes laccase, azoreductase, and peroxidase through analyzing their structural and functional properties using standard computational tools. Result: According to the comparative analysis of physicochemical characteristics, it was clear that laccase was mostly made up of basic amino acids whereas azoreductase and peroxidase both comprised of acidic amino acids. Higher aliphatic index ascertained the thermostability of all these three enzymes. Negative GRAVY value of the enzymes confirmed better water interaction of the enzymes. Instability index depicted that compared to laccase and preoxidase, azoreductase was more stable in nature. It was also observed that the three model proteins had more than 90% of total amino acids in the favored region of Ramachandran plot. Functional analysis revealed laccase as multicopper oxidase type enzyme and azoreductase as FMN dependent enzyme, while peroxidase consisted of α-ß barrel with additional haem group. Conclusion: Present study aims to provide knowledge on industrial dye degrading enzymes, choosing the suitable enzyme for industrial set up and to help in understanding the experimental laboratory requirements as well.


Assuntos
Compostos Azo/metabolismo , Peroxidase/química , Lacase/química , NADH NADPH Oxirredutases/química , Temperatura , Compostos Azo/química , Indústria Têxtil , Biodegradação Ambiental , Simulação por Computador , Estabilidade Enzimática , Peroxidase/metabolismo , Lactase/metabolismo , Corantes/metabolismo , NADH NADPH Oxirredutases/metabolismo
2.
J. bras. nefrol ; 36(4): 482-489, Oct-Dec/2014. tab, graf
Artigo em Português | LILACS | ID: lil-731141

RESUMO

Introdução: A hipertensão arterial tem alta prevalência em renais crônicos, sendo a hipervolemia um de seus fatores causais. Objetivo: Avaliar a influência da redução da volemia no controle pressórico e em parâmetros ecocardiográficos de pacientes renais crônicos em diálise peritoneal contínua. Métodos: Doze renais crônicos sem sinais clínicos de hipervolemia foram submetidos à intensificação da diálise com o objetivo de reduzir o peso corporal em 5%. A volemia foi avaliada pela bioimpedância elétrica e pela ultrassonografia de veia cava inferior (VCI). Os voluntários foram submetidos à monitorização ambulatorial da pressão arterial e a exame ecocardiográfico no período basal e após 5 semanas de intervenção. Resultados: Após a intensificação da ultrafiltração, houve redução significativa do peso corporal, da água extracelular e do diâmetro inspiratório da VCI, enquanto o índice de colapsamento da VCI não alterou de modo significativo. A despeito da redução do número de anti-hipertensivos, a pressão sistólica do período de sono reduziu de 138,4 ± 18,6 para 126,7 ± 18,0 mmHg, o descenso pressórico do sono aumentou e o diâmetro sistólico final do ventrículo esquerdo reduziu significantemente. Conclusão: A redução da volemia de pacientes em diálise peritoneal, clinicamente euvolêmicos, se associou a melhor controle pressórico e à diminuição do diâmetro sistólico final do ventrículo esquerdo. .


Introduction: Hypertension is highly prevalent in patients with chronic kidney disease and hypervolemia is one of the principal causes. Objective: To evaluate the influence of the reduction of volemia on blood pressure as well as on echocardiographic parameters in patients on continuous ambulatory peritoneal dialysis. Methods: Twelve patients with no clinical evidence of hypervolemia were submitted to an increase in the rate of the dialysis with the purpose of reducing body weight by 5%. The volemia was evaluated by electrical bioimpedance and by ultrasound of the inferior cava vena (ICV). Blood pressure was measured by ambulatory blood pressure monitoring and cardiac function was evaluated by echocardiography both at baseline and 5 weeks after the intervention period. Results: After the increase in the ultrafiltration, body weight, extracellular water and the inspiratory diameter of the ICV decreased significantly in parallel with a non-significant increase in the collapsing ICV index. Despite the reduction of anti-hypertensive drugs, systolic blood pressure during the sleep period decreased from 138.4 ± 18.6 to 126.7 ± 18.0 mmHg, the nocturnal blood pressure drop increased and the final systolic left ventricular diameter decreased significantly. Conclusion: Reduction of the volemia of patients on peritoneal dialysis, with no signs of hypervolemia, was associated with a better blood pressure control and with a decrease of the final systolic left ventricular diameter. .


Assuntos
Animais , Bovinos , NADH NADPH Oxirredutases/química , NADH NADPH Oxirredutases/metabolismo , Ubiquinona/metabolismo , Sítios de Ligação , Complexo I de Transporte de Elétrons , Inibidores Enzimáticos/farmacologia , Técnicas In Vitro , Cinética , Miocárdio/enzimologia , NADH NADPH Oxirredutases/antagonistas & inibidores , Ressonância Magnética Nuclear Biomolecular , Rotenona/farmacologia
3.
Indian J Exp Biol ; 1993 Dec; 31(12): 951-4
Artigo em Inglês | IMSEAR | ID: sea-61926

RESUMO

Two azoreductases (I and II) were purified to homogeneity from extracts of E. coli K12. Azoreductase I was a dimer of two identical subunits of molecular weight 28000 whereas azoreductase II was a monomer of 12,000 molecular weight. Both NADH and NADPH functioned as electron donors for the azoreductases. Azoreductase I and II used Ponceau SX, Tartrazine, Amaranth and Orange II as substrates. Ponceau SX was the best substrate for both the enzymes. However, azoreductase II utilized tartrazine, amaranth and orange II less efficiently than azoreductase I.


Assuntos
Compostos Azo , Escherichia coli/enzimologia , Concentração de Íons de Hidrogênio , Cinética , Peso Molecular , NAD/metabolismo , NADH NADPH Oxirredutases/química , NADP/metabolismo , Conformação Proteica , Especificidade por Substrato
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