Banca de QUALIFICAÇÃO: JULIENE DA CÂMARA ROCHA
Uma banca de QUALIFICAÇÃO de MESTRADO foi cadastrada pelo programa.DISCENTE : JULIENE DA CÂMARA ROCHA
DATA : 21/06/2018
HORA: 14:00
LOCAL: Auditório PPGEQ
TÍTULO:
Production, characterization and application of pectinolytic enzymes from Aspergillus niger IOC 4003 using tropical residues of fruits as substrate
PALAVRAS-CHAVES:
Aspergillus niger, solid-state fermentation, pectinases, pectin lyase, polygalacturonase, agro-industrial residue.
PÁGINAS: 80
GRANDE ÁREA: Engenharias
ÁREA: Engenharia Química
SUBÁREA: Processos Industriais de Engenharia Química
ESPECIALIDADE: Processos Bioquímicos
RESUMO:
At the last decades, the demand for microbial enzymes for biotechnological applications has grown significantly. The pectinolytic enzymes are responsible for cleaving both pectin and other pectic polysaccharides in galacturonic acid monomers and they are applied in several industrial sectors such as fruit and wine juice processing, essential oil recovery, vegetable oil extraction, textile and, paper and pulp industry. In this context, the aim of this work was to evaluate the production of pectinolytic enzymes by the Aspergillus niger IOC 4003 strain using acerola and cajá residues as a substrate of solid-state fermentation (SSF). With that purpose the residues of washed and unwashed acerola and cajá were initially dried and it had their chemical and physicochemical composition determined. The percentage of calcium pectate - pectin indicator - found in the residues was 3.46 ± 0.11%, 2,944 ± 0,18%, 5,847 ± 0,01%, 5,34 ± 0,23% for acerola not washed, acerola washed, cajá not washed and cajá washed, respectively. Hereby, the potential of these substrates as inducers was evaluated for the production of pectinolytic and cellulolytic enzymes by SSF for 240 hours at initial pH 4.5, moisture at 40% and concentration of spores of 1 x 107 spores/g. After all fermentations with different substrate it has been highlighted the polygalacturonase production using the washed cajá residue that reached the enzymatic concentration of 38.22 ± 0.63 U / g in 72 hours of cultivation. Furthermore, the optimization of enzyme extraction was assessed and the best found condition was the contact time of 30 minutes and using acetate buffer at 50 mM and pH 5.4. In the posterior step, the stability of the enzyme complex was evaluated at different temperatures and distinguished pHs. The finest enzymatic stabilities were obtained at temperatures of 30 and 40 ° C and pH of 4, 5 and 6 for up to two hours of incubation. In regard of the above, the obtained outcomes in this work showed the feasibility of applying industrial residues of fruit pulp as substrates for the production of enzymes of biotechnological interest and their application in food industry.
MEMBROS DA BANCA:
Externo ao Programa - 2378605 - CRISTIANE FERNANDES DE ASSIS
Interno - 1346198 - EVERALDO SILVINO DOS SANTOS
Externo ao Programa - 3652554 - FRANCISCO CANINDE DE SOUSA JUNIOR
Presidente - 347401 - GORETE RIBEIRO DE MACEDO