Caracterización de la actividad Enzimática de la B-Galactosidasa aislada de un cultivo líquido de Pleurotus ostreatus a base de suero de leche

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ABSTRACT The aim of the present research was characterize the enzymatic activity of ß-galactosidase isolated from a liquid culture of Pleurotus ostreatus based on whey. For this, samples of mycelium of P. ostreatus were cultivated in agar whey and incubated for 20-24 days. Fragments of 1 cm2 of the...

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Detalles Bibliográficos
Autor: Plasencia Cerna, Olga Danitza
Formato: tesis de maestría
Fecha de Publicación:2019
Institución:Universidad Nacional de Trujillo
Repositorio:UNITRU-Tesis
Lenguaje:español
OAI Identifier:oai:dspace.unitru.edu.pe:20.500.14414/11833
Enlace del recurso:https://hdl.handle.net/20.500.14414/11833
Nivel de acceso:acceso abierto
Materia:B-galactosidasa
Pleurotus ostreatus
Actividad enzimática
ONPG
Descripción
Sumario:ABSTRACT The aim of the present research was characterize the enzymatic activity of ß-galactosidase isolated from a liquid culture of Pleurotus ostreatus based on whey. For this, samples of mycelium of P. ostreatus were cultivated in agar whey and incubated for 20-24 days. Fragments of 1 cm2 of the mycelial growth were transferred to culture media containing whey broth, leaving in growth for 21 days. The liquid cultures were filtered to obtain the crude extract, from which the enzymatic activity, the concentration of enzyme, the effect of pH, temperature, enzyme, substrate ortho-nitrophenyl-β-galactopyranoside (ONPG) and the incubation time were determined; being found that, the crude extract of ß-galactosidase presents an enzymatic activity of 0.394 U/mL, a protein concentration of 0.8545 mg/mL and a specific activity of 0.461 U/mg. The optimal pH and temperature values of the enzyme in the soluble state were at pH 3 and at 35 °C. To calculate the Vmax and Km values of the β-galactosidase, the Lineweaver-Burk kinetic model was graphed where the values were 0,0262 μmol/min and 16,11 mM, respectively. The results revealed that when the enzymatic reaction (enzyme-substrate) is carried out, the increase in the concentration of the product is observed until the reaction ends or reaches its equilibrium point at 30 minutes.
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