Banca de QUALIFICAÇÃO: LARISSA COSTA SANTOS

Uma banca de QUALIFICAÇÃO de MESTRADO foi cadastrada pelo programa.
STUDENT : LARISSA COSTA SANTOS
DATE: 01/03/2024
TIME: 13:30
LOCAL: Instituto de Ciências Farmacêuticas
TITLE:

CARACTERIZAÇÃO BIOQUÍMICA DE UM INIBIDOR DE PROTEASE DA LARVA DO INSETO Tribolium castaneum



KEY WORDS:

Tribolium castaneum,enzyme inhibitor, biochemical characterization, flour beetle.



PAGES: 52
BIG AREA: Ciências Biológicas
AREA: Bioquímica
SUBÁREA: Enzimologia
SUMMARY:

Protease inhibitors are substances that have the ability to regulate the action of proteases, blocking their catalytic activity. Many of these inhibitors are produced naturally by the body with the aim of maintaining homeostasis. Protease inhibitors have been the subject of study due to their biotechnological potential in pest control, the food industry, research into new medicines and also to increase understanding of inhibition mechanisms. The present work aimed to investigate the inhibitory activity and biochemical characteristics of a protease inhibitor present in the insect Tribolium castaneum. The first step was to identify in which phase of the insect's life cycle there is a greater production of the inhibitor, then to improve the purity of the sample, the extract was subjected to purification techniques, such as saline precipitation and two-phase and three-phase aqueous systems. After choosing the best technique, the sample was subjected to resistance tests to pH and temperature, the influence of metallic salts and stabilizers, and the action against the phytopathogenic fungus Amphobotrys ricini was also tested. The study revealed the presence of the inhibitor in the larval, pupa and adult stages, with emphasis on the larval stage, which demonstrated more than 40% inhibitory activity. The method that was most efficient for reducing contaminants in the sample was the three-phase aqueous system with isopropanol. The inhibitor activity remained stable at temperatures from 40 to 70ºC, but maintained its activity even at high temperatures, and also remained stable over a wide range of pHs (5-10). Furthermore, the inhibitor activity was influenced by different metal salts and different stabilizers, with BSA and Gelatin notably enhancing the inhibitory activity. Finally, a decrease in the growth rate of the phytopathogenic fungus Amphobotrys ricini was observed. These results highlight the potential use of the endogenous protease inhibitor from the insect T. castaneum, and may also contribute to the understanding of the properties of insect inhibitors and mechanisms of enzyme regulation.



COMMITTEE MEMBERS:
Presidente - 1653558 - LUCIANO APARECIDO MEIRELES GRILLO
Interno(a) - 3509820 - MARIA ALINE BARROS FIDELIS DE MOURA
Externo(a) ao Programa - 2089586 - FRANCIS SOARES GOMES - UFAL
Notícia cadastrada em: 15/02/2024 10:36
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