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Previous issue date: 2008-10-24 / Coordena??o de Aperfei?oamento de Pessoal de N?vel Superior / A ?-D-N-acetilglucosaminidase extracted and partially isolated from crustacean Artemia franciscana by ammonium sulfate precipitation and filtration
gel chromatography Bio Gel A 1.5m. the enzyme was immobilized on ferromagnetic Dacron yielding a insoluble active derivative with 5.0 units/mg
protein and 10.35% of the soluble enzyme activity. ?-D-N-acetilglucosaminidase-ferromagnetic Dacron was easily removed from the reaction mixture by a magnetic field, it was reused for ten times without loss in its activity. The ferromagnetic Dacron was better activated at pH 5.0. The particles visualized at scanning electron microscope (SEM) had presented different sizes, varying between 721nm and 100?m. Infra red confirmed immobilization on support, as showed by primary amino peaks at 1640 and 1560 cm-1
. The immobilize enzyme presented Km of 2.32 ? 0.48 mM and optimum temperature of 50?C. Bought
presented the same thermal stable of the soluble enzyme and larger enzymatic activity at pH 5.5. ?-D-N-acetilglucosaminidase-Dacron ferromagn?tico showed
sensible for some ?ons as the silver (AgNO3), with loss of activity. The ?-D-N acetilglucosaminidase activity for mercury chloride (HgCl2), whom is one of the
most toxic substance joined in nature, it was presented activity already diminished at 0,01mM and lost total activity at 4mM, indicating sensitivity for this
type of metal. ?-D-N-acetilglucosaminidase-ferromagnetic Dacron showed degradative capacity on heparan sulfate, the enzyme still demonstrated
degradative capacity on heparan sulphate, suggesting a possible application to produce fractions of this glycosaminoglycan / A ?-D-N-acetilglucosaminidase, extra?da e parcialmente isolada do crust?ceo Artemia franciscana atrav?s de precipita??o com sulfato de am?nio e cromatografia em gel filtra??o Bio Gel A 1.5m foi imobilizada em Dacron
ferromagn?tico rendendo um derivado insol?vel ativo contendo 5,0 unid/mg de prote?na e retendo 10,35% da atividade da enzima sol?vel. A ?-D-N-acetilglucosaminidase-Dacron ferromagn?tico foi facilmente removida do meio reacional com o aux?lio de um campo magn?tico e p?de ser reutilizada por dez
vezes seguidas sem perda de atividade. O Dacron ferromagn?tico foi melhor ativado a pH 5,0 As part?culas visualizadas no microsc?pio eletr?nico de
varredura (MEV) apresentaram diferentes tamanhos, variando entre 721nm e 100?m. O infra vermelho confirmou a imobiliza??o ao suporte, quando exibiu os
picos de aminas prim?rias a 1640 e 1560 cm-1
. A enzima imobilizada apresentou Km aparente de 2,32 ? 0,48 mM e atividade ?tima a temperatura de 50?C. Ambos apresentaram praticamente a mesma estabilidade t?rmica da enzima sol?vel e maior atividade enzim?tica no pH 5,5. A ?-D-N-acetilglucosaminidase-Dacron
ferromagn?tico apresentou-se sens?vel a alguns ?ons como a prata (AgNO3), demonstrando perda de atividade. A atividade ?-D-N-acetilglucosaminidasica
para cloreto de merc?rio (HgCl2), que ? uma das subst?ncias mais t?xicas encontradas na natureza, apresentou-se diminu?da j? a 0,01mM e perdeu a
atividade total a 4mM, indicando sensibilidade a esse tipo de metal. A enzima ainda demonstrou capacidade degradativa sobre o heparan sulfato, sugerindo
uma poss?vel aplica??o para produzir fragmentos desse glicosaminoglicano
| Identifer | oai:union.ndltd.org:IBICT/oai:repositorio.ufrn.br:123456789/12538 |
| Date | 24 October 2008 |
| Creators | Santos, Pablo de Castro |
| Contributors | CPF:76111830449, http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4799567J8&dataRevisao=null, Pereira, Wogelsanger Oliveira, CPF:02392207496, http://lattes.cnpq.br/4661963400736302, Moura, Carlos Eduardo Bezerra de, CPF:03597959431, http://lattes.cnpq.br/4717410137206021, Rocha, Hugo Alexandre de Oliveira |
| Publisher | Universidade Federal do Rio Grande do Norte, Programa de P?s-Gradua??o em Bioqu?mica, UFRN, BR, Bioqu?mica; Biologia Molecular |
| Source Sets | IBICT Brazilian ETDs |
| Language | Portuguese |
| Detected Language | English |
| Type | info:eu-repo/semantics/publishedVersion, info:eu-repo/semantics/masterThesis |
| Format | application/pdf |
| Source | reponame:Repositório Institucional da UFRN, instname:Universidade Federal do Rio Grande do Norte, instacron:UFRN |
| Rights | info:eu-repo/semantics/openAccess |
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