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Corrêa,Ana Paula F.; Daroit,Daniel J.; Velho,Renata V.; Brandelli,Adriano. |
The production of extracellular hydrolases by a psychrotrophic bacterium isolated from refrigerated raw milk, and identified as a Pseudomonas sp. belonging to the Pseudomonas jenssenii group, was studied. This bacterium produced proteolytic and lipolytic enzymes in all media investigated (skim milk, cheese whey, casein broth, and tryptone soy broth). High levels of α-glucosidase were produced in skim milk broth. Hydrolytic enzymes detected in skim milk broth are of particular concern, indicating that these enzymes could be produced by Pseudomonas sp. during the cold storage of raw milk, contributing to the spoilage problem in milk and dairy products. |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Pseudomonas; Hydrolases; Protease; Lipase; Glycosidase. |
Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000400034 |
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Marco,Janice Lisboa De; Valadares-Inglis,Maria Cléria; Felix,Carlos Roberto. |
Two isolates of Trichoderma, which reduce the incidence of witches'broom disease caused in cocoa by Crinipellis perniciosa, were evaluated for their potential to produce hydrolases in liquid medium. Very low or no hydrolytic activity was produced in the absence of any substrate. The activities of chitinase, N-acetylglucosaminidase, beta-1,3-glucanase, total cellulase, endoglucanase, aryl- beta-glucosidase, beta-glucosidase, protease and amylase increased dramatically within 72-120 h of growth in the presence of specific substrates. Except for N-acetylglucosaminidase and beta-glucosidase Trichoderma harzianum isolate 1051 produced the largest amounts of hydrolases. The possible involvement of these enzymes in the antagonistic interaction between Trichoderma... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Trichoderma; Crinipellis perniciosa; Hydrolases; Antagonistic interaction. |
Ano: 2003 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822003000100008 |
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Kumar,Sumit; Karan,Ram; Kapoor,Sanjay; Singh,S.P.; Khare,S.K.. |
Halophiles are excellent sources of enzymes that are not only salt stable but also can withstand and carry out reactions efficiently under extreme conditions. The aim of the study was to isolate and study the diversity among halophilic bacteria producing enzymes of industrial value. Screening of halophiles from various saline habitats of India led to isolation of 108 halophilic bacteria producing industrially important hydrolases (amylases, lipases and proteases). Characterization of 21 potential isolates by morphological, biochemical and 16S rRNA gene analysis found them related to Marinobacter, Virgibacillus, Halobacillus, Geomicrobium, Chromohalobacter, Oceanobacillus, Bacillus, Halomonas and Staphylococcus genera. They belonged to moderately halophilic... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Halophiles; Biodiversity; Halophilic enzymes; Hydrolases; Solvent-stable. |
Ano: 2012 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000400044 |
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Costa,Bruna Zucoloto da; Rodrigues,Viviane Drumond; Oliveira,Valéria Maia de; Ottoboni,Laura Maria Mariscal; Marsaioli,Anita Jocelyne. |
Abstract Copper mine drainages are restricted environments that have been overlooked as sources of new biocatalysts for bioremediation and organic syntheses. Therefore, this study aimed to determine the enzymatic activities (esterase, epoxide hydrolase and monooxygenase) of 56 heterotrophic bacteria isolated from a neutral copper mine drainage (Sossego Mine, Canaã dos Carajás, Brazil). Hydrolase and monooxygenase activities were detected in 75% and 20% of the evaluated bacteria, respectively. Bacterial strains with good oxidative performance were also evaluated for biotransformation of organic sulfides. Fourteen strains with good enzymatic activity were identified by 16S rRNA gene sequencing, revealing the presence of three genera: Bacillus, Pseudomonas... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Copper mine drainage; High-throughput screening; Hydrolases; Monooxygenases. |
Ano: 2016 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000400846 |
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