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	Provedor de dados BJM (2) Autor Pinto,Uelinton M. (2) Costa,Esther D. (1) Mantovani,Hilario C. (1) Martins,Maurilio L. (1) Riedel,Katharina (1) Vanetti,M.C.D. (1) Vanetti,Maria C.D. (1) Mais... Palavra-chave Pseudomonas fluorescens (2) Extracellular lipase (1) Extracellular protease (1) Food deterioration (1) Proteolytic activity (1) Quorum sensing (1) Raw milk (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2015 (1) 2010 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última The proteolytic activity of Pseudomonas fluorescens 07A isolated from milk is not regulated by quorum sensing signals BJM Pinto,Uelinton M.; Costa,Esther D.; Mantovani,Hilario C.; Vanetti,M.C.D.. The proteolytic activity of Pseudomonas fluorescens 07A was investigated, and was optimal on tryptone-calcium medium. N-acyl-homoserine lactones (AHLs) were not detected on supernatants of late-exponential and stationary-phase culture broths. Synthetic AHLs or bacterial cell extracts added to the medium did not influence growth or proteolytic activity suggesting that quorum sensing might not regulate protease production in this strain. Tipo: Info:eu-repo/semantics/article Palavras-chave: Pseudomonas fluorescens; Proteolytic activity; Quorum sensing. Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822010000100015 Milk-deteriorating exoenzymes from Pseudomonas fluorescens 041 isolated from refrigerated raw milk BJM Martins,Maurilio L.; Pinto,Uelinton M.; Riedel,Katharina; Vanetti,Maria C.D.. The practice of refrigerating raw milk at the farm has provided a selective advantage for psychrotrophic bacteria that produce heat-stable proteases and lipases causing severe quality problems to the dairy industry. In this work, a protease (AprX) and a lipase (LipM) produced by Pseudomonas fluorescens 041, a highly proteolytic and lipolytic strain isolated from raw milk obtained from a Brazilian farm, have been purified and characterized. Both enzymes were purified as recombinant proteins from Escherichia coli. The AprX metalloprotease exhibited activity in a broad temperature range, including refrigeration, with a maximum activity at 37 °C. It was active in a pH range of 4.0 to 9.0. This protease had maximum activity with the substrates casein and... Tipo: Info:eu-repo/semantics/article Palavras-chave: Raw milk; Food deterioration; Pseudomonas fluorescens; Extracellular protease; Extracellular lipase. Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000100207 Registros recuperados: 2 Primeira ... 1 ... Última

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