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1.
Microbiol Resour Announc ; 12(9): e0034823, 2023 Sep 19.
Artigo em Inglês | MEDLINE | ID: mdl-37470493

RESUMO

We report here the draft genome sequence of a marine Pseudomonas sp. novel species with lipase activity isolated from a deep-sea water sample of the Gulf of Mexico. The genome consists of 4.3 Mbp in 48 contigs.

2.
Prep Biochem Biotechnol ; 52(3): 325-330, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-34261412

RESUMO

Lipases (triacylglycerol hydrolases, EC 3.1.1.3) are a class of enzymes with high industrial importance. An option for the production of this enzyme is through fungal growth via solid-state fermentation (SSF). Thus, this research presents a study of lipase production by Penicillium roqueforti ATCC 10110 through SSF using cocoa bran residues (Theobroma cacao) as a substrate. To achieve maximum lipase production, fermentation time (0 to 120 h) and palm oil (PO) percentage (0 to 50%) were optimized through analysis of one factor at a time (OFAT), with lipase activity as the response. The amount of cocoa was fixed (5 g), the incubation temperature was maintained at 27 °C, and the moisture content was established at 70%. For a 72 h incubation, the highest enzyme activity achieved using SSF without adding PO was 14.67 ± 1.47 U g-1, whereas with PO (30%), it was 33.33 ± 3.33 U g-1, thus demonstrating a 44% increase in enzyme activity. Through the OFAT methodology, it was possible to confirm that supplementation with palm residue was efficient and maximized the lipase of P. roqueforti ATCC 10110.


Assuntos
Arecaceae/metabolismo , Cacau/metabolismo , Fermentação , Lipase/biossíntese , Penicillium/metabolismo
3.
Braz. arch. biol. technol ; 63: e20180444, 2020. graf
Artigo em Inglês | LILACS | ID: biblio-1132252

RESUMO

Abstract Fungi have always attracted a lot of attention as they are able to produce a vast repertoire of enzymes that find a broad spectrum of uses in biotechnological and industrial fields. Undoubtedly, one of the most promising biocatalysts is the lipase, which has been widely used for the biotransformation of a number of commercial products due to its high stability, high catalytic efficiency, versatility and selectivity, making it one of the most attractive and best-studied enzymes. In this study we report the isolation and molecular identification of new lipase-producing fungi from different environmental samples from Morocco. The production and activity of extracellular lipases, at different parameters, was evaluated using the Rhodamine B agar, submerged fermentation and biochemical methods. Two fungal strains Arthrographis curvata and Rhodosporidium babjevae, were isolated and found to produce large amounts of lipases. The optimal activity of the extracellular lipase was detected at 40°C and pH 9.0 for A. curvata and at 40 °C and pH 8.0 for R. babjevae. This study add new information at the growing list of fungal species producing lipases with improved physicochemical proprieties which could constitute a new line of research for further studies and to be exploited for industrial or bioremediation purposes.


Assuntos
Biotecnologia , Fungos/enzimologia , Lipase/biossíntese
4.
Electron. j. biotechnol ; 30: 33-38, nov. 2017. tab, graf
Artigo em Inglês | LILACS | ID: biblio-1021336

RESUMO

Background: Lipases are used in detergent industries to minimise the use of phosphate-based chemicals in detergent formulations. The use of lipase in household laundry reduces environmental pollution and enhances the ability of detergent to remove tough oil or grease stains. Results: A lipase-producing indigenous Bacillus subtilis strain [accession no. KT985358] was isolated from the foothills of Trikuta mountain in Jammu and Kashmir, India. The lipase (BSK-L) produced by this strain expressed alkali and thermotolerance. Lipase has an optimal activity at pH 8.0 and temperature 37°C, whereas it is stable at pH 6.0­9.0 and showed active lipolytic activity at temperatures 30 to 60°C. Furthermore, lipase activity was found to be stimulated in the presence of the metal ions Mn2+, K+, Zn2+, Fe2+ and Ca2+. This lipase was resistant to surfactants, oxidising agents and commercial detergents, suggesting it as a potential candidate for detergent formulation. BSK-L displayed noticeable capability to remove oil stains when used in different washing solutions containing buffer, lipase and commercial detergent. The maximum olive oil removal percentage obtained was 68% when the optimum detergent concentration (Fena) was 0.3%. The oil removal percentage from olive oil-soiled cotton fabric increased with 40 U/mL of lipase. Conclusions: This BSK-L enzyme has the potential for removing oil stains by developing a pre-soaked solution for detergent formulation and was compatible with surfactants, oxidising agents and commercial detergents.


Assuntos
Bacillus subtilis/metabolismo , Lipase/metabolismo , Temperatura , Bacillus subtilis/isolamento & purificação , Bacillus subtilis/enzimologia , Detergentes , Alcalinização , Termotolerância , Concentração de Íons de Hidrogênio , Lipase/biossíntese
5.
Vitae (Medellín) ; 19(3): 280-286, sep.-dic. 2012. ilus, tab
Artigo em Inglês | LILACS | ID: lil-669353

RESUMO

Background: Extracellular lipases are found in the culture broth when the fermentation is at the end of the exponential phase. Lipases can be induced easily since they are produced by the presence of oily sources or other materials as surfactants, fatty acids, some esters, glycerol and biliary salts. Objective: The aim of this work is to study the effect of carbon source concentration and the use of inductors on biomass production, and the lipolytic activity of a bacterium isolated from mature palm oil fruits. Methods: The yield biomass/substrate was evaluated with glucose as carbon source at different concentrations (3, 5, 7, 10, 15 y 20 g/L) by dry weight and OD (600 nm). Lipolytic activity was evaluated by spectrophotometric assay using p-nitrofenilpalmitate at 37°C for 15 min. Results: Gram negative microorganisms with lipolytic activity isolated from palm fruit were identified as Pseudomona aeruginosa. The growth of the bacteria was inhibited when glucose was used at concentrations greater than 5%. The production of lipase was induced by using three inducers (Palm oil, Tween 20 and palm oil:Tween 20 mixture), at three different induction times (0, 11 and 18 hours of fermentation). The highest activity (3,81 µmoles/mL*min) was observed when the palm oil:Tween 20 mixture was added at 11 hours of fermentation. The kinetic of p-nitrophenylpalmitate hydrolysis using the supernatant of a culture induced with palm oil:Tween 20 mixture at 11 hours showed the production of p-nitrophenol beyond 300 minutes, with the greatest hydrolysis rate during the first 7 minutes. Conclusions: The growth of P. aeruginosa was not affected by using glucose as carbon source at concentrations of 3% and 5%. There was a basal level of lipase production without inducer, and greater lipolytic activity was achieved with the addition of inducers.


Assuntos
Hidrólise , Ácidos Graxos
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