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	Provedor de dados BJM (2) Ciênc. Tecnol. Aliment. (1) Electron. J. Biotechnol. (1) Autor Macedo,Gabriela Alves (3) Fraga,Laira Priscila (2) Pio,Tatiana Fontes (2) Campos-Takaki,Galba M (1) Cavaco-Paulo,Artur (1) Fleuri,Luciana Francisco (1) Gomes,Daniela S (1) Lopes,Danielle Branta (1) Matamá,Teresa (1) Salgueiro,Alexandra A (1) Mais... Palavra-chave Cutinase (4) Esterase (2) Environmental application (1) Esterase specific activity (1) Fermentation process (1) Fusarium oxysporum (1) Inoculum (1) Lipase (1) Lipase specific activity (1) Macroscopic characteristics (1) Microbial enzymes (1) Poly(ethylene terephthalate) (1) Screening (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Journal article (1) Ano 2013 (1) 2011 (1) 2008 (1) 2005 (1) País Brazil (3) Chile (1) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Inoculum padronization for the production of cutinase by Fusarium oxysporum BJM Pio,Tatiana Fontes; Fraga,Laira Priscila; Macedo,Gabriela Alves. Cutinase is a versatile enzyme showing several interesting properties for application in industrial processes. The widespread use of this enzyme depends on the development of an efficient and low-cost production system. One of the most important steps in a fermentation process is the standardization of the inoculum characteristics. In this study, the production of cutinase by Fusarium oxysporum showed a statistically significant relationship with both the inoculum size and the inoculum PDA pH. The greatest activities were 19.1 U/mL at PDA pH 7.0 and 22.72 U/mL using an aliquot of 12.72 x 10(7) spores/mL. The macroscopic characteristics of the colonies of Fusarium oxysporum changed according to the variation of the medium pH, with the best results recorded... Tipo: Info:eu-repo/semantics/article Palavras-chave: Fusarium oxysporum; Inoculum; Cutinase; Macroscopic characteristics; Fermentation process. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000100018 A rapid screening method for cutinase producing microorganisms BJM Macedo,Gabriela Alves; Pio,Tatiana Fontes. Both cutinase and lipase belong to the esterase group of enzymes (EC 3.1.1.X), which are capable of catalyzing the hydrolysis of ester bonds. Cutinase catalyzes the hydrolysis of cutin, an insoluble biopolyester which is the structural component of plant cuticles. As cutinase is an efficient catalyst in watery or organic media, it is potentially appropriate for the detergent, food and cosmetic industries. The objective of this work was to isolate microorganisms from plants and perform a pre-selection of molds showing esterase producing ability. The selected strains were then submitted to fermentation in media containing cutin. The lipolytic and cutinolytic activities of the supernatant were determined in order to differentiate lipase producers from... Tipo: Info:eu-repo/semantics/article Palavras-chave: Cutinase; Esterase; Microbial enzymes; Screening. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822005000400016 Lipase and esterase: to what extent can this classification be applied accurately? Ciênc. Tecnol. Aliment. Lopes,Danielle Branta; Fraga,Laira Priscila; Fleuri,Luciana Francisco; Macedo,Gabriela Alves. Enzyme technology is an ever-growing field of knowledge and, in recent years, this technology has raised renewed interest, due to the search for new paradigms in several productive processes. Lipases, esterases and cutinases are enzymes used in a wide range of processes involving synthesis and hydrolysis reactions. The objective of this work was to investigate and compare the specific lipase and esterase activities of five enzymes - four already classified as lipases and one classified as cutinase - in the presence of natural and synthetic substrates. All tested enzymes presented both esterase and lipase specific activities. The highest specific esterase activity was observed for Aspergillus 1068 lipase in natural substrate and for F. oxysporum cutinase in... Tipo: Info:eu-repo/semantics/article Palavras-chave: Lipase; Esterase; Cutinase; Lipase specific activity; Esterase specific activity. Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612011000300009 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: 4 Primeira ... 1 ... Última

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