Banca de DEFESA: MARIANA DE MENEZES OLIVEIRA

Uma banca de DEFESA de MESTRADO foi cadastrada pelo programa.
DISCENTE : MARIANA DE MENEZES OLIVEIRA
DATA : 31/08/2016
HORA: 09:00
LOCAL: SALA DE AULA II DO PPGCF
TÍTULO:

AVALIAÇÃO ENZIMÁTICA DA L-ASPARAGINASE PRODUZIDA POR MICRORGANISMOS UTILIZANDO RESÍDUO AGROINDUSTRIAL

PALAVRAS-CHAVES:

L-asparaginase, resíduo da casca de abacaxi, microrganismos, fermentação submersa.

PÁGINAS: 102
GRANDE ÁREA: Ciências da Saúde
ÁREA: Farmácia
RESUMO:

    L-asparaginase is an enzyme that catalyzes by deamination the L-asparagine aminoacid into L-aspartic acid and ammonia, due this mechanism of action, the enzyme is used as first choice treatment drug to Acute Lymphoblastic Leukemia (AAL). The depletion of aminoacid causes death of the tumor cells. The main producer microorganism is Escherichia coli by submerged fermentation process (SmF). However bacterial L-asparaginase has adverse effects as hypersensivity and imonugenicity, and researches have showed that L-asparaginase from fungi may has less effects, due to this several studies are being carried out using fungi that could to produce L-asparaginase that presents anticancer activity and possesses fewer adverse effects. The aim of this study was the L-asparaginase production by Aspergillus terreus, Penicillium chrysogenum, and Zymomonas mobilis microrganisms by SmF using as carbon source the pineapple in natura peels. Also it performed a Central Compound Design (CCD), in order to optimize the hydrolysis capacity and stability studies in pH and temperature of L-asparaginase. The Penicillium chrysogenum was the microorganism that showed higher enzyme activity (7.00 U.mL-1) during SmF. Followed by Zymomonas mobilis (6.17 U.mL-1), and Aspergillus terreus (4.24 U.mL-1). The experimental design and stability studies were carried out from Penicillium chrysogenum L-asparaginase. The CCD results showed that the only independent variable statistically significant (p<0,05) was reaction time, suggesting that the enzyme has fast reaction mechanism. The results of pH and temperature stability from Penicillium chrysogenum L-asparaginase, using the hydrolysis conditions of L-asparagine obtained by CCD, were 9.0 and 20 °C, respectively. The stability study at different temperatures (-20 °C, 25 °C and 37 °C) in time factor, were carried out for 31 days, and results showed that after this period, the enzyme retained its enzyme activity above 50%. This show that the L-asparaginase obtained from Penicillium chrysogenum is a stable enzyme front of the possible variations over time.

MEMBROS DA BANCA:
Interno - 2323511 - ADRIANA AUGUSTO DE REZENDE
Externo à Instituição - MARIA VALDEREZ PONTE ROCHA - UFC
Presidente - 1544647 - MATHEUS DE FREITAS FERNANDES PEDROSA