Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Registro completo
Provedor de dados:  BABT
País:  Brazil
Título:  Immobilization of alpha-amylase produced by Bacillus circulans GRS 313
Autores:  Dey,Gargi
Bhupinder,Singh
Banerjee,Rintu
Data:  2003-03-01
Ano:  2003
Palavras-chave:  Bacillus circulans GRS313
Entrapment
Maltooligosaccharide-forming amylase
Response surface methodology
Starchy residues
Resumo:  A maltooligosaccharide-forming amylase from B circulans GRS 313 was immobilized by entrapment in calcium alginate beads. The immobilized activity was affected by the size of the bead and bead size of 2mm was found to be most effective for hydrolysis. Kinetics constants, Km and Vmax were estimated and were found to be affected by the bead size. The catalytic activity of the enzyme was studied in presence of various starchy residues and metal ions. HgCl2, CuSO4 and FeCl3 caused inhibition of the enzyme. The reaction conditions, pH and temperature, was optimized using response surface methodology. At the optimum pH and temperature of 4.9 and 57ºC, the apparent activity was 25.6U/g of beads, resulting in almost 2-fold increase in activity. The immobilized enzyme showed a high operational stability by retaining almost 85% of the initial activity after seventh use.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132003000200005
Editor:  Instituto de Tecnologia do Paraná - Tecpar
Relação:  10.1590/S1516-89132003000200005
Formato:  text/html
Fonte:  Brazilian Archives of Biology and Technology v.46 n.2 2003
Direitos:  info:eu-repo/semantics/openAccess
Fechar
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional