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Production of heterologous cutinases by E. coli and improved enzyme formulation...

Gomes, Daniela S.; Matamá, Maria Teresa; Paulo, Artur Cavaco; 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 ...


Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heter...

Gomes, Daniela S.; Matamá, Maria Teresa; Paulo, Artur Cavaco; Jordão, R. C. C.; Takaki, G. M. Campos; Salgueiro, Alexandra A.

Cutinases (EC 3.1.1.74)are versatile enzymes that have hydrolytic activity on various esters [1]. The spacial structure and the catalytic site of the enzymes can be protected by chemical additives to promove the stability of the activity [2, 3]. The goal of this work was to improve the stability of a recombinant cutinase produced by Escherichia coli.


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Fundação para a Ciência e a Tecnologia Universidade do Minho   Governo Português Ministério da Educação e Ciência Programa Operacional da Sociedade do Conhecimento União Europeia