Periplasmic trehalase from Escherichia coli: characterization and immobilization on spherisorb
Braz. j. med. biol. res
; 27(3): 627-36, Mar. 1994. tab, graf
Artigo
em Inglês
| LILACS
| ID: lil-148935
Biblioteca responsável:
BR1.1
RESUMO
1. Trehalase was partially purified from Escherichia coli and characterized. The Km for trehalose was 0.78 mM, the pH optimum 5.5 and the temperature optimum 30 degrees C. 2. Trehalase represented approximately 50 per cent of the total protein released by osmotic shock. The preparation was free of nonspecific carbohydrate hydrolases, which act on sucrose, galactose and maltose, permitting trehalose determination in biological samples, such as insect hemolymph and free cell extracts among others. 3. The enzyme was stable in 50 mM maleate buffer, pH 6.2, at -8 degrees C for at least 6 months and could be used to determine trehalose in the range of 6 to 30 nmol. 4. Immobilization of the enzyme was achieved by covalent linkage to spherisorb-5NH2 (spherical silica gel). Retention of total catalytic activity averaged 32 per cent . 5. The reactor, stored for one month at -5 degrees C, retained 98 per cent of its initial immobilized activity. 6. This immobilized form of the enzyme could be used routinely for specific determinations of trehalose
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Coleções:
Bases de dados internacionais
Contexto em Saúde:
Doenças Negligenciadas
Problema de saúde:
Doenças Negligenciadas
/
Zoonoses
Base de dados:
LILACS
Assunto principal:
Trealase
/
Enzimas Imobilizadas
/
Escherichia coli
Idioma:
Inglês
Revista:
Braz. j. med. biol. res
Assunto da revista:
Biologia
/
Medicina
Ano de publicação:
1994
Tipo de documento:
Artigo