Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Mais filtros










Intervalo de ano de publicação
1.
Semina cienc. biol. saude ; 41(2): 165-176, jun./dez. 2020. Ilus
Artigo em Inglês | LILACS | ID: biblio-1224275

RESUMO

This study aimed to evaluate the production of lipases by a new strain of Pseudomonas sp. using fermentation medium containing byproducts of poultry meat or soybean oil industry. The results indicate that chicken fat and soybean gum induced 48.3 U/mL and 93.3 of lipase activity, respectively. However, the higher lipase production was obtained when the crude lecithin gum was used, archiving 272.6 U/ml of activity after 24 hours. The partial biochemical characterization of the enzyme showed that the optimum reaction conditions were pH 9.0 and 35 °C. The enzyme was stable at temperatures between 25 to 75 °C and at pH from 6 to 9. The enzyme also showed good stability in organic solvents, such as acetronitrile, hexane, ethanol and isopropanol. This study indicates that the byproducts tested are promising for the production of lipase and can contribute to the reduction of enzymatic production costs on a large scale, increase the value of these byproducts and reduce potential environmental impacts caused by its accumulation in nature.(AU)


Este estudo teve como objetivo avaliar a produção de lipases por uma nova cepa de Pseudomonas sp. utilizando meio de fermentação contendo subprodutos de industrialização de carne de frango e óleo de soja. Os resultados indicaram que a gordura de frango e a goma de soja induziram 48,3 U/mL e 93,3 U/ml de atividade lipásica, respectivamente. No entanto, a produção de lipase mais elevada foi obtida quando a goma de lecitina bruta foi utilizada, induzindo 272,6 U/ml de atividade após 24 horas. A caracterização bioquímica parcial da enzima mostrou que as condições de reação ótimas foram de pH 9,0 e 35 °C. A enzima foi estável nas temperaturas entre 25 a 75 °C e pH de 6 a 9. A enzima mostrou boa estabilidade em solventes orgânicos, tais como acetonitrila, hexano, etanol e isopropanol. Este estudo indicou que os subprodutos testados são promissores para a produção de lipase e podem contribuir para a redução dos custos de produção enzimática em larga escala, aumentar o valor desses subprodutos e reduzir potenciais impactos ambientais causados por sua acumulação na natureza.(AU)


Assuntos
Pseudomonas , Lipase , Lecitinas , Gorduras , Fermentação
2.
Acta sci., Biol. sci ; 42: e52115, fev. 2020. tab, graf
Artigo em Inglês | LILACS, VETINDEX | ID: biblio-1460955

RESUMO

Esterases are enzymes that present good potential for industrial applications since they catalyze the formation or cleavage of ester bonds in water-soluble substrates, and sorghumseeds can represent an alternative source of this enzyme. The extraction of esterase from sorghumseeds is an economical alternative to obtain an enzyme of great interest. Esterases may improve the quality or accelerate the maturation of cheeses, cured bacon and fermented sausages and may also resolve racemic mixtures. Recently, seed esterases have been the focus of much attention as biocatalysts. In some cases, these enzymes present advantages over animal and microbial lipases due to some quite interesting features such as specificity and low cost, being a great alternative for their commercial exploitation as industrial enzymes The esterase studied here was extracted from sorghumseeds and some of its biochemical properties determined using synthetic substrates (p-nitrophenyl butyrate, caprylate, laurate and palmitate). The enzyme presented optimum activity at pH 8.0 and was stable in all the pH ranges studied. The optimum temperature for its activity was 40ºC but it showed low stability at this temperature (40% relative activity). The values derived for Km and Vmax were 0.67mM and 125 U.mg-1, respectively, obtained using p-nitrophenyl butyrate as the substrate. The enzyme showed an increase in activity when K2HPO4was added to the reaction medium, but the ions Mn2+, CO+, Hg+and Fe2+strongly inhibited the enzyme activity. This enzyme showed a preference for the hydrolysis of short chain fatty acids. The characteristics of sorghumesterase are very similar to those of the microbial esterases used in detergent processing.


Assuntos
Esterases/análise , Esterases/química , Sorghum/química , Álcalis
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...