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Pesquisa : D08.811.277.352.100.400 [Categoria DeCS]
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Id: biblio-1041762
Autor: Kuhar, Francisco; Castiglia, Valeria C; Zamora, Juan C.
Título: Detección de manganeso peroxidasa y otras exoenzimas en 4 aislamientos de Geastrum (Geastrales) en cultivo puro / Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
Fonte: Rev. argent. microbiol;48(4):274-278, dic. 2016. ilus, graf, tab.
Idioma: en.
Resumo: Knowledge regarding the enzymatic machinery of fungi is decisive to understand their ecological role. The species of the genus Geastrum are known to grow extremely slowly in pure culture, which makes it difficult to evaluate physiological parameters such as enzyme activity. Qualitative assays were performed on isolates of four species of this genus, showing evidence of laccase, cellulase, pectinase, amylase and lipase activity and suggesting that a wide range of carbon sources can be exploited by these species. For the first time in this genus, quantitative assays verified manganese peroxidase activity (up to 0.6 mU/g) in 30-day old cultures, as well as laccase, β-glycosidase and β-xylosidase activities.

El conocimiento de la maquinaria enzimática de un hongo es decisivo para entender su rol ecológico. Las especies del género Geastrum son conocidas por su crecimiento extremadamente lento en cultivos puros, lo que hace difícil la evaluación de parámetros fisiológicos como las actividades enzimáticas. Se realizaron ensayos cualitativos sobre aislamientos de 4 especies de este género, mostrando evidencias de actividades lacasa, celulasa, pectinasa, amilasa y lipasa, mostrando el amplio rango de fuentes de carbono que pueden ser explotadas por estas especies. Ensayos cuantitativos verificaron por primera vez en este género la actividad manganeso peroxidasa (hasta 0,6 mU/g) en cultivos de 30 días, así como también β-glucosidasa y β-xilosidasa.
Descritores: Fungos/enzimologia
-Xilosidases/isolamento & purificação
Biotransformação/fisiologia
Celulase/isolamento & purificação
Lacase/isolamento & purificação
Fungos/fisiologia
Lipase/isolamento & purificação
Tipo de Publ: Ensaio Clínico
Estudo de Avaliação
Responsável: AR635.1 - FCVyS - Servicio de Información y Documentación


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Id: biblio-1224608
Autor: Ungcharoenwiwat, Pakpimol; H-Kittikun, Aran.
Título: Enzymatic synthesis of coconut oil based wax esters by immobilized lipase EQ3 and commercial lipozyme RMIM
Fonte: Electron. j. biotechnol;47:10-16, sept. 2020. graf, tab.
Idioma: en.
Projeto: Institute of Research and Innovation, Walailak University.
Resumo: BACKGROUND: Liquid wax esters are widely used in cosmetic as well as pharmaceutical and other industries. The demand of organic and natural products is increasing nowadays. Coconut oil contains benefit fatty acids and has been mainly used for oil-based and moisturizer products. Liquid wax esters from coconut oil and unsaturated fatty alcohol can be synthesized by enzymatic reaction; and it is interesting for using as an alternative natural ingredient in these industries. RESULTS: Optimal condition for coconut oil based wax ester synthesis by immobilized lipase EQ3 was 10 U of enzyme, temperature at 30°C and molar ratio of coconut oil to oleyl alcohol at 1:3 (mol/mol) (0.33X) dissolved in isooctane for 12 h, while for Lipozyme RM IM optimal condition was 10 U of enzyme, temperature at 45°C and oil/alcohol molar ratio at 1:3 (0.33X) dissolved in isooctane for 3 h. Percentage of wax esters synthesized by both lipases reached more than 88%. Both immobilized lipases catalyzed high yield of wax esters within the 2nd batch; after that, the immobilized lipases showed reduced activity and synthesized b60% of wax esters from the 3rd to 5th batch. The main composition of wax esters was ~48% oleyl laurate with 10% degradation at ~250°C. CONCLUSIONS: The liquid wax ester synthesis by commercial Lipozyme RM IM had higher effect than immobilized lipase EQ3, but both catalysts were stable within 2 batches in the optimum condition. The characteristic properties of wax esters showed potential for use as components in cosmetics and skin care products.
Descritores: Ceras
Ésteres/metabolismo
Óleo de Palmeira/síntese química
Lipase/metabolismo
-Temperatura
Enzimas Imobilizadas
Indústria Cosmética
Responsável: CL1.1 - Biblioteca Central


  3 / 149 LILACS  
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Id: biblio-1128481
Autor: Decarlini, María Florencia.
Título: La hipertrigliceridemia leve a moderada parece incrementar también el riesgo de pancreatitis aguda / Mild-to-moderate hypertrigliceridemia may increase the risk of acute pancreatitis
Fonte: Evid. actual. práct. ambul;20(2):56-56, 2017. tab.
Idioma: es.
Descritores: Pancreatite/complicações
Hipertrigliceridemia/complicações
-Pâncreas/metabolismo
Triglicerídeos/sangue
Índice de Gravidade de Doença
Risco
Estudos de Coortes
Dinamarca
Amilases/metabolismo
Lipase/sangue
Infarto do Miocárdio/complicações
Limites: Humanos
Masculino
Feminino
Adulto
Pessoa de Meia-Idade
Idoso
Adulto Jovem
Tipo de Publ: Comentário
Responsável: AR2.1 - Biblioteca Central


  4 / 149 LILACS  
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Id: biblio-1224275
Autor: Baldo, Cristiani; Baggio, Lillian Maria; Oliveira, Marcos Roberto; Melo, Marcelo Rodrigues; Gasparin, Fabiana Guillen Moreira; Celligoi, Maria Antonia Pedrine Colabone.
Título: Utilization of agroindustrial byproducts for the production of lipase by a new strain of Pseudomonas sp / Utilização de subprodutos agroindustriais para a produção de lipase por uma nova cepa de Pseudomonas sp
Fonte: Semina cienc. biol. saude;41(2):165-176, jun./dez. 2020. Ilus.
Idioma: en.
Resumo: This study aimed to evaluate the production of lipases by a new strain of Pseudomonas sp. using fermentation medium containing byproducts of poultry meat or soybean oil industry. The results indicate that chicken fat and soybean gum induced 48.3 U/mL and 93.3 of lipase activity, respectively. However, the higher lipase production was obtained when the crude lecithin gum was used, archiving 272.6 U/ml of activity after 24 hours. The partial biochemical characterization of the enzyme showed that the optimum reaction conditions were pH 9.0 and 35 °C. The enzyme was stable at temperatures between 25 to 75 °C and at pH from 6 to 9. The enzyme also showed good stability in organic solvents, such as acetronitrile, hexane, ethanol and isopropanol. This study indicates that the byproducts tested are promising for the production of lipase and can contribute to the reduction of enzymatic production costs on a large scale, increase the value of these byproducts and reduce potential environmental impacts caused by its accumulation in nature.(AU)

Este estudo teve como objetivo avaliar a produção de lipases por uma nova cepa de Pseudomonas sp. utilizando meio de fermentação contendo subprodutos de industrialização de carne de frango e óleo de soja. Os resultados indicaram que a gordura de frango e a goma de soja induziram 48,3 U/mL e 93,3 U/ml de atividade lipásica, respectivamente. No entanto, a produção de lipase mais elevada foi obtida quando a goma de lecitina bruta foi utilizada, induzindo 272,6 U/ml de atividade após 24 horas. A caracterização bioquímica parcial da enzima mostrou que as condições de reação ótimas foram de pH 9,0 e 35 °C. A enzima foi estável nas temperaturas entre 25 a 75 °C e pH de 6 a 9. A enzima mostrou boa estabilidade em solventes orgânicos, tais como acetonitrila, hexano, etanol e isopropanol. Este estudo indicou que os subprodutos testados são promissores para a produção de lipase e podem contribuir para a redução dos custos de produção enzimática em larga escala, aumentar o valor desses subprodutos e reduzir potenciais impactos ambientais causados por sua acumulação na natureza.(AU)
Descritores: Pseudomonas
Lipase
-Lecitinas
Gorduras
Fermentação
Responsável: BR512.1 - Biblioteca Setorial do Centro de Ciências da Saúde


  5 / 149 LILACS  
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Texto completo SciELO Brasil
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Id: biblio-1132252
Autor: Aamri, Lamya El; Hafidi, Majida; Scordino, Fabio; Krasowska, Anna; Lebrihi, Ahmed; Orlando, Maria Grazia; Barresi, Cinzia; Criseo, Giuseppe; Barreca, Davide; Romeo, Orazio.
Título: Arthrographis curvata and Rhodosporidium babjevae as New Potential Fungal Lipase Producers for Biotechnological Applications
Fonte: Braz. arch. biol. technol;63:e20180444, 2020. graf.
Idioma: en.
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.
Descritores: Biotecnologia
Fungos/enzimologia
Lipase/biossíntese
Responsável: BR1.1 - BIREME


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Texto completo SciELO Cuba
Texto completo
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Id: biblio-1156463
Autor: Salazar Carranza, Luz Angelica; Hinojoza Guerrero, Marilú Mercedes; Acosta Gaibor, Mónica Patricia; Escobar Torres, Alicia Filadelfia; Scrich Vázquez, Aldo Jesús.
Título: Caracterización, clasificación y usos de las enzimas lipasas en la producción industrial / Characterization, classification and uses of lipase enzymes in industrial production
Fonte: Rev. cuba. invest. bioméd;39(4):e620, oct.-dic. 2020.
Idioma: es.
Resumo: Introducción: La bioquímica, como ciencia particular dentro de las ciencias médicas, ha tenido un gran desarrollo. Las enzimas lipasas se obtienen de organismos vivos que abundan en la naturaleza y han sido utilizadas en la producción de alimentos, jabones, detergentes, aceites y otros productos industriales. Actualmente se han logrado nuevas clasificaciones de estas, subdivididas en grupos y subgrupos. Se aprecia además interés de utilizarlas en la producción de biodiesel y en la biotecnología y genética médica. Objetivo: Recopilar las principales consideraciones teóricas actualizadas acerca la caracterización, clasificación y usos de las enzimas lipasas. Método: La búsqueda y análisis de la información se realizó desde el primero de septiembre al 23 de diciembre de 2019, con un total de 50 artículos publicados en las bases de datos PubMed, Hinari, SciELO y Medline, mediante el gestor de búsqueda y administrador de referencias EndNote. se utilizaron 42 citas seleccionadas para realizar la revisión, de ellas 38 de los últimos cinco años. Conclusiones: Las enzimas lipasas son proteínas que catalizan procesos biológicos. son activas en un amplio rango de sustrato, realizan reacciones de síntesis, hidrólisis o de intercambio de grupos. Poseen diversas actividades catalíticas, son menos costosas y menos contaminantes, se obtienen en gran cantidad, se producen de forma regular. Son estables y su proceso de producción es más factible y seguro. Se caracterizan por su capacidad de catalizar reacciones de acidólisis, alcohólisis, aminólisis, esterificación, interesterificación y transesterificación, entre otras características(AU)

Introduction: Biochemistry has experienced great development as a particular medical science. Lipase enzymes are obtained from living organisms which are abundant in nature, and have been used in the manufacture of foods, soap, detergents, oils and other industrial products. New classifications are now available of lipase enzymes, and they have been subdivided into groups and subgroups. An interest is also noticed in using them for biodiesel production and in biotechnology and medical genetics. Objective: Collect the main updated theoretical considerations about the characterization, classification and uses of lipase enzymes. Method: The search for and analysis of the information extended from 1 September to 23 December 2019, for a total 50 papers published in the databases PubMed, Hinari, SciELO and Medline, using the search engine and reference manager EndNote. Forty-two citations were selected for the review, 38 of which were from the last five years. Conclusions: Lipase enzymes are proteins that catalyze biological processes. They are active in a wide range of substrates, performing synthesis reactions, hydrolysis or group exchanges. They display a variety of catalytic activities, are less costly and less contaminating, are obtained in large quantities and are produced in a regular manner. They are stable and their production process is more feasible and safer. They are characterized by their ability to catalyze reactions of acidolysis, alcoholysis, aminolysis, esterification, interesterification and transesterification, among other characteristics(AU)
Descritores: Bioquímica
Biotecnologia
-Enzimas/análise
Lipase/farmacocinética
Limites: Humanos
Tipo de Publ: Revisão
Responsável: CU1.1 - Biblioteca Médica Nacional


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Id: biblio-1157399
Autor: Tiscornia Osvaldo Manuel; Rodríguez Ricardo Raúl; Sussemil Carlota; Otero Graciela; Negri Gustavo Alberto; Waisman Hipólito; López Mingorance Fabiana Norma; Tiscornia Wasserman Patricia Graciela.
Título: Streptozotocin-induced diabetes, bile-pancreatic secretion and insulo-pancreon-axis interaction / Streptozotocin-induced diabetes, bile-pancreatic secretion and insulo-pancreon-axis interaction.
Fonte: Acta gastroenterol. latinoam;43(4):294-300, 2013 Dec.
Idioma: es.
Resumo: The present tests were undertaken in order to analyze in male Wistar rats the changes in the exocrine and endocrine pancreas and on the interactions that normally evolve in the insulo-pancreon-axis. To evaluate this by a single i.p. Boots secretin injection, glycemia (G), amylasemia (A) and lipasemia (L) were determined. In bile-pancreatic secretion, we analyzed, pre and post-secretin, the following parameters: volume (V), bicarbonate output (BO), amylase output (AO) and lipase output (LO). Three groups of tests were done: a) control (C); b) streptozotocin-treated non-diabetic-rats (St-ND) and c) streptozotocin-treated diabetic animals (St-D) which showed morning glycemia values higher than 16.0 mmol/l. Four months later, under Tiopental i.p anesthesia, a bile-pancreatic fistula was done. Following a 30 min basal period, Boots secretin (20 CU/kg) was i.p injected. Bile-pancreatic secretion put in evidence a significant fall of BO in both St-ND and St-D series. In controls, AO revealed a post-secretin increase of 160

, while in the St-D rats showed a depression of 41

. The behavior of L was different, being augmented (+27

) in the C, while in the St-D rats the response was significantly higher (+95

). In bile-pancreatic-secretion, the fall of BO and AO in the St-ND and St-D series in respect to the C, are probably consequence of the diminishing potentiating effects exerted normally by insulin on the secretin-induced water and bicarbonate secretion of the pancreon units. In contrast, the rising of LO in the St-D, an expression of an enhancing pancreocyte's synthesis and secretion of lipase. The blood changes of A (depression) and of L (increase) in respect to the C values, although without reaching significant level, mirror those observed in bile-pancreatic secretion.
Descritores: Bile/metabolismo
Diabetes Mellitus Experimental/metabolismo
Pâncreas/metabolismo
-Amilases/metabolismo
Animais
Diabetes Mellitus Experimental/enzimologia
Estreptozocina
Lipase/metabolismo
Masculino
Ratos
Ratos Wistar
Secretina/metabolismo
Tipo de Publ: Artigo de Revista
Responsável: AR5.1 - Centro de Gestión del Conocimiento y las Comunicaciónes


  8 / 149 LILACS  
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Id: biblio-1052260
Autor: Huang, Lin; Zheng, Dong; Zhao, Yatong; Ma, Jieying; Li, Yanzhen; Xu, Zehua; Shan, Mengying; Shao, Shulin; Guo, Qingwen; Zhang, Jie; Lu, Fuping; Liu, Yihan.
Título: Improvement of the alkali stability of Penicillium cyclopium lipase by error-prone PCR
Fonte: Electron. j. biotechnol;39:91-97, may. 2019. ilus, graf, tab.
Idioma: en.
Projeto: National Key R&D Program of China; . National Natural Science Foundation of China; . China Postdoctoral Science Foundation; . Natural Science Foundation of Tianjin City.
Resumo: BACKGROUND: Lipases are extensively exploited in lots of industrial fields; cold-adapted lipases with alkali-resistance are especially desired in detergent industry. Penicillium cyclopium lipase I (PCL) might be suitable for applications of detergent industry due to its high catalytic efficiency at low temperature and relatively good alkali stability. In this study, to better meet the requirements, the alkali stability of PCL was further improved via directed evolution with error-prone PCR. RESULTS: The mutant PCL (N157F) with an improved alkali stability was selected based on a high-throughput activity assay. After incubating at pH 11.0 for 120 min, N157F retained 70% of its initial activity, which was 23% higher than that of wild type PCL. Combined with the three-dimensional structure analysis, N157F exhibited an improved alkali stability under the high pH condition due to the interactions of hydrophilicity and ß-strand propensity. Conclusions: This work provided the theoretical foundation and preliminary data for improving alkali stability of PCL to meet the industrial requirements, which is also beneficial to improving alkali-tolerance ability of other industrial enzymes via molecular modification.
Descritores: Penicillium/enzimologia
Estabilidade Enzimática
Indústria de Detergentes
Lipase/metabolismo
-Penicillium/isolamento & purificação
Penicillium/genética
Reação em Cadeia da Polimerase/métodos
Temperatura Baixa
Álcalis
Biocatálise
Interações Hidrofóbicas e Hidrofílicas
Concentração de Íons de Hidrogênio
Lipase/isolamento & purificação
Lipase/genética
Mutação
Responsável: CL1.1 - Biblioteca Central


  9 / 149 LILACS  
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Id: biblio-1052027
Autor: Delgado-García, Mariana; Flores-Gallegos, Adriana C; Kirchmayr, Manuel; Rodríguez, Jorge A; Mateos-Díaz, Juan C; Aguilar, Cristobal N; Muller, Marcelo; Camacho-Ruíz, Rosa M.
Título: Bioprospection of proteases from Halobacillus andaensis for bioactive peptide production from fish muscle protein
Fonte: Electron. j. biotechnol;39:52-60, may. 2019. ilus, tab, graf.
Idioma: en.
Resumo: BACKGROUND: Biologically active peptides produced from fish wastes are gaining attention because their health benefits. Proteases produced by halophilic microorganisms are considered as a source of active enzymes in high salt systems like fish residues. Hence, the aim of this study was the bioprospection of halophilic microorganisms for the production of proteases to prove their application for peptide production. RESULTS: Halophilic microorganisms were isolated from saline soils of Mexico and Bolivia. An enzymatic screening was carried out for the detection of lipases, esterases, pHB depolymerases, chitinases, and proteases. Most of the strains were able to produce lipases, esterases, and proteases, and larger hydrolysis halos were detected for protease activity. Halobacillus andaensis was selected to be studied for proteolytic activity production; the microorganism was able to grow on gelatin, yeast extract, skim milk, casein, peptone, fish muscle (Cyprinus carpio), and soy flour as protein sources, and among these sources, fish muscle protein was the best inducer of proteolytic activity, achieving a protease production of 571 U/mL. The extracellular protease was active at 50°C, pH 8, and 1.4 M NaCl and was inhibited by phenylmethylsulfonyl fluoride. The proteolytic activity of H. andaensis was used to hydrolyze fish muscle protein for peptide production. The peptides obtained showed a MW of 5.3 kDa and a radical scavenging ability of 10 to 30% on 2,2-diphenyl-1-picrylhydrazyl and 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) and a ferric reducing ability of plasma. Conclusion: The use of noncommercial extracellular protease produced by H. andaensis for biologically active peptide production using fish muscle as the protein source presents a great opportunity for high-value peptide production.
Descritores: Peptídeo Hidrolases/metabolismo
Peptídeos/metabolismo
Proteínas de Peixes/metabolismo
Halobacillus/enzimologia
-Solo
Bactérias/isolamento & purificação
Bolívia
Esterases
Salinidade
Hidrólise
Lipase
México
Proteínas Musculares
Antioxidantes
Responsável: CL1.1 - Biblioteca Central


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Texto completo SciELO Brasil
Texto completo
Id: lil-757366
Autor: Bolsoni-Lopes, Andressa; Alonso-Vale, Maria Isabel C.
Título: Lipolysis and lipases in white adipose tissue – An update
Fonte: Arch. endocrinol. metab. (Online);59(4):335-342, Aug. 2015. ilus.
Idioma: en.
Resumo: Lipolysis is defined as the sequential hydrolysis of triacylglycerol (TAG) stored in cell lipid droplets. For many years, it was believed that hormone-sensitive lipase (HSL) and monoacylglycerol lipase (MGL) were the main enzymes catalyzing lipolysis in the white adipose tissue. Since the discovery of adipose triglyceride lipase (ATGL) in 2004, many studies were performed to investigate and characterize the actions of this lipase, as well as of other proteins and possible regulatory mechanisms involved, which reformulated the concept of lipolysis. Novel findings from these studies include the identification of lipolytic products as signaling molecules regulating important metabolic processes in many non-adipose tissues, unveiling a previously underestimated aspect of lipolysis. Thus, we present here an updated review of concepts and regulation of white adipocyte lipolysis with a special emphasis in its role in metabolism homeostasis and as a source of important signaling molecules.
Descritores: Tecido Adiposo Branco/enzimologia
Lipase/metabolismo
Lipólise/fisiologia
-Tecido Adiposo Branco/fisiologia
Lipase/fisiologia
Limites: Humanos
Tipo de Publ: Revisão
Responsável: BR1.1 - BIREME



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