Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 5
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Isolation and characterization of novel thermophilic lipase-secreting bacteria BJM
Rabbani,Mohammed; Bagherinejad,Mohammad Reza; Sadeghi,Hamid MirMohammad; Shariat,Ziaedin Samsam; Etemadifar,Zahra; Moazen,Fatemeh; Rahbari,Manizheh; Mafakher,Ladan; Zaghian,Saeideh.
The purpose of the present study was to screen and identify the lipase-producing microorganisms from various regions of Iran. Samples collected from hot spring, Persian Gulf, desert area and oil-contaminated soil, were analyzed for thermophilic extracellular-lipase producing organisms. Six strains with high activity on rhodamine B plates were selected for chemical identification and further study. Among these isolated bacteria, four strains show higher activity in pH-Stat method at 55 °C. These strains were identified by PCR amplification of 16s rRNA genes using universal primers. Fermentation increased the activity up to 50%. The growth medium, designed for lipase production, increased the activity up to 4.55 folds. The crude supernatant of ZR-5 after...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Extracellular lipase; PH-stat method; Thermophilic lipase; Fermentation.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822013000400013
Imagem não selecionada

Imprime registro no formato completo
Isolation of a lipase-producing Trichosporon spp and enzyme extraction by two-phase aqueous system BJM
Santos,Juliana A.; Amaral,Marcel C.O.; Araújo,Thiago A.S.; Fernandes,Késsia G.C.; Chaves,Adilson C.; Morais,Márcia M.C..
A lipase-producing yeast strain isolated from crude cheese and identified as Trichosporon spp produced 7.3 U/mL (59.3 U/µg) after 72h of cultivation. Lipase showed optimum activity at pH 7.0-8.0 and 45-50ºC. Extraction by the two-phase aqueous system (PEG-phosphate salts) showed an elevated recuperation (99.8%) of enzymatic activity in the PEG phase.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Extracellular lipase; Trichosporon; Aqueous two phase system; PEG.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822007000100013
Imagem não selecionada

Imprime registro no formato completo
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
Imagem não selecionada

Imprime registro no formato completo
Production and characterization of an extracellular lipase from Candida guilliermondii BJM
Oliveira,Anne Caroline Defranceschi; Fernandes,Maria Luiza; Mariano,André Bellin.
Extracellular lipases from the endophytic yeast Candida guilliermondii isolated from castor leaves (Ricinus communis L.) were produced using low-cost raw materials such as agro-industrial residues and applying them in the esterification of oleic acid for evaluating their potential use in biodiesel production. After partial purification using ammonium sulfate, the enzyme was characterized and presented higher activity (26.8 ± 1.5 U mL-1) in the presence of 5 mmol L-1 NaCl at 30 ºC and pH 6.5. The production through submerged fermentation was formerly performed in 150 mL erlenmeyer flasks and, once the enzyme production was verified, assays in a 14 L bioreactor were conducted, obtaining 18 ± 1.4 U mL-1. The produced enzyme was applied in the oleic acid...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Extracellular lipase; Endophytic yeast; Esterification; Submerged fermentation; Bioreactor.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822014000400047
Imagem não selecionada

Imprime registro no formato completo
Production of extracellular lipase by the phytopathogenic fungus Fusarium solani FS1 Rev. Microbiol.
Maia,Maria de Mascena Diniz; Morais,Marcia Maria Camargo de; Morais Jr.,Marcos Antonio de; Melo,Eduardo Henrique Magalhães; Lima Filho,José Luiz de.
A Brazilian strain of Fusarium solani was tested for extracellular lipase production in peptone-olive oil medium. The fungus produced 10,500 U.l-1 of lipase after 72 hours of cultivation at 25oC in shake-flask at 120 rpm in a medium containing 3% (w/v) peptone plus 0.5% (v/v) olive oil. Glucose (1% w/v) was found to inhibit the inductive effect of olive oil. Peptone concentrations below 3% (w/v) resulted in a reduced lipase production while increased olive oil concentration (above 0.5%) did not further stimulate lipase production. The optimum lipase activity was achieved at pH 8.6 and 30oC and a good enzyme stability (80% activity retention) was observed at pH ranging from 7.6 to 8.6, and the activity rapidly dropped at temperatures above 50oC. Lipase...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Enzyme kinetics; Ester hydrolysis; Extracellular lipase; Fusarium solani.
Ano: 1999 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141999000400003
Registros recuperados: 5
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