Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 2
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Protein interactions in enzymatic processes in textiles Electron. J. Biotechnol.
Tzanov,Tzanko; Andreaus,Jürgen; Guebitz,Georg; Cavaco-Paulo,Artur.
Enzymes are the catalysts of all reactions in living systems. These reactions are catalysed in the active sites of globular proteins. The proteins are composed by amino acids with a variety of side chains ranging from non-polar aliphatic and aromatic to acidic, basic and neutral polar. This fact allows to a globular 3D protein to create in the active site all ranges of microenvironments for catalysis. Major advances in microbial technology and genetics allow recently the broad range of enzymatic applications in the industry. Enzymatic processes have been increasingly incorporated in textiles over the last years. Cotton, wool, flax or starches are natural materials used in textiles that can be processed with enzymes. Enzymes have been used for desizing,...
Tipo: Journal article
Ano: 2003 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582003000300013
Imagem não selecionada

Imprime registro no formato completo
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation Electron. J. Biotechnol.
Gomes,Daniela S; Matamá,Teresa; Cavaco-Paulo,Artur; Campos-Takaki,Galba M; Salgueiro,Alexandra A.
Background: The hydrolytic action of cutinases has been applied to the degradation of plastics. Polyethylene terephthalate (PET) have long half-life which constitutes a major problem for their treatment as urban solid residues. The aim of this work was to characterize and to improve stable the enzyme to optimize the process of degradation using enzymatic hydrolysis of PET by recombinant cutinases. Results: The wild type form of cutinase from Fusarium solani pisi and its C-terminal fusion to cellulose binding domain N1 from Cellulomonas fimi were produced by genetically modified Escherichia coli. The maximum activity of cutinases produced in Lactose Broth in the presence of ampicillin and isopropyl β-D-1-thiogalactopyranoside (IPTG) was 1.4 IU/mL....
Tipo: Journal article Palavras-chave: Cutinase; Environmental application; Poly(ethylene terephthalate).
Ano: 2013 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000500003
Registros recuperados: 2
Primeira ... 1 ... Última
 

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