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Doctoral Thesis
DOI
https://doi.org/10.11606/T.11.2019.tde-20191220-130346
Document
Author
Full name
Marcelo Fossa da Paz
E-mail
Institute/School/College
Knowledge Area
Date of Defense
Published
Piracicaba, 2004
Supervisor
Title in Portuguese
Imobilização das exoenzimas de Kluyveromyces marxianus MMIII-41 com atividade inulinolítica e pectinolítica
Keywords in Portuguese
ATIVIDADE ENZIMÁTICA
ENZIMAS EXTRACELULARES
IMOBILIZAÇÃO
LEVEDURAS
Abstract in Portuguese
A levedura Kluyveromyces marxianus MMIII-41 possui atividade hidrolítica identificada com a produção das enzimas inulinase, invertase e pectinase. A atividade da invertase é mais ativa a temperaturas entre 30 e 40°C e pHs entre 4,0 e 6,0. A atividade da inulinase foi maior em temperaturas mais elevadas não apresentando diferenças significativas entre 40 e 60°C e pH em torno de 5,0. O mesmo se observa com a atividade da pectinase não apresentando diferenças significativas 30 a 40°C e pHs entre 4,0 e 7,0. Estas enzimas foram estudadas na condição de imobilização nas matrizes alginato, copolímero alginato-gel-quitosana, nylon 6®, quitina e isopor, com o objetivo de identificar dentre estas qual seria a mais adequada a estudos futuros de ampliação de escala. As respectivas atividades enzimáticas foram determinadas mediante determinação de açúcares redutores totais formados a partir dos substratos inulina, pectina e sacarose (Somogyi e Nelson, 1945). Os experimentos com as enzimas imobilizadas em cada uma das matrizes foram realizados nos sistemas descontínuo e contínuo. No sistema contínuo ficaram evidentes os problemas operacionais de cada matriz, sendo que o Nylon 6 e o isopor não apresentaram atividade já nas primeiras horas de processo. A quitina causou entupimento do sistema por compactação e as esferas de alginato em pouco tempo vieram a se desfazer. Nas condições experimentais avaliadas o copolímero alginato-gel-quitosana revelou-se a matriz com maior atividade, estabilidade e vida média. Nesta matriz a melhor atividade da inulinase aconteceu com a imobilização por ligações covalentes, enquanto que a imobilização por aprisionamento produziu melhores resultados para as atividades de pectinase e invertase.
Title in English
A Kluyveromyces marxianus MMIII-41 exonzyme immobilization with inulinolitic and pectinolitic activities
Abstract in English
The Kluyveromyces marxianus MMIlI-41 yeast presents hydrolitic activity identifyed with inulinase, invertase and pectinase. The invertase activity is better under temperatures of 30 and 40°C and pHs 4,0 and 6,0. The inulinase activity was better in high temperatures without importamt differences between 40 and 60°C and pH around 5,0. The same situation is observed with pectinase activity not presenting important differences from 30 to 40°C and pHs between 4,0 and 7,0. This enzymes were studied in immobilization conditions in alginate, chitosan-alginate-gel copolymer, nylon 6® , chitin and expanded polystirene, in order to find the best matrice to be used in future studies for the scale amplification.The respective enzymatic activities were measured by reducing sugar methods from inulin, pectin and sucrose on Somogyi and Nelson (1945) method. The experiments with any enzymes were made in bath and continuous system. On continuous systems the operation problems of any matrice become clear. Nylon 6 and expanded polystirene lost activity in the beginning ofthe process. The chitin obstructed the system by compactation and the alginate beads become deranged in a short time. On the evaluated experimental conditions the alginate-chitosan-gel showed the highest activity, stableness and higher mean-Iife matrice. On this matrice the best inuIinase activity was took pIace by covalent bonds whereas bonding by entrapment was better to pectinase and invertase.
 
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PazMarceloFossaDa.pdf (6.52 Mbytes)
Publishing Date
2019-12-20
 
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