Work

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

Year: 2013

Type: conference-paper

Abstract: 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.

Source: Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

Authors: Daniela Gomes, Teresa Matamá, Artur Cavaco‐Paulo, R. C. C. Jordão, Galba Maria de Campos‐Takaki, Alexandra A. Salgueiro

Language: English

Topic: Enzyme Catalysis and Immobilization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W2247129703

FWCI:

Cites: 2

Cited by:

Related to: 10