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[PMID]:29194017
[Au] Autor:Abdul Manan FM; Attan N; Widodo N; Aboul-Enein HY; Wahab RA
[Ad] Endereço:a Department of Chemistry, Faculty of Science , Universiti Teknologi Malaysia , Skudai , Malaysia.
[Ti] Título:Rhizomucor miehei lipase immobilized on reinforced chitosan-chitin nanowhiskers support for synthesis of eugenyl benzoate.
[So] Source:Prep Biochem Biotechnol;48(1):92-102, 2018 Jan 02.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An alternative environmentally benign support was prepared from chitosan-chitin nanowhiskers (CS/CNWs) for covalent immobilization of Rhizomucor miehei lipase (RML) to increase the operational stability and recyclability of RML in synthesizing eugenyl benzoate. The CS/CNWs support and RML-CS/CNWs were characterized using X-ray diffraction, fluorescent microscopy, and Fourier transform infrared spectroscopy. Efficiency of the RML-CS/CNWs was compared to the free RML to synthesize eugenyl benzoate for parameters: reaction temperature, stirring rate, reusability, and thermal stability. Under optimal experimental conditions (50°C, 250 rpm, catalyst loading 3 mg/mL), a twofold increase in yield of eugenyl benzoate was observed for RML-CS/CNWs as compared to free RML, with the former achieving maximum yield of the ester at 62.1% after 5 hr. Results demonstrated that the strategy adopted to prepare RML-CS/CNWs was useful, producing an improved and prospectively greener biocatalyst that supported a sustainable process to prepare eugenyl benzoate. Moreover, RML-CS/CNWs are biodegradable and perform esterification reactions under ambient conditions as compared to the less eco-friendly conventional acid catalyst. This research provides a facile and promising approach for improving activity of RML in which the resultant RML-CS/CNWs demonstrated good operational stability for up to eight successive esterification cycles to synthesize eugenyl benzoate.
[Mh] Termos MeSH primário: Benzoatos/metabolismo
Quitina/química
Quitosana/química
Enzimas Imobilizadas/metabolismo
Eugenol/análogos & derivados
Lipase/metabolismo
Rhizomucor/enzimologia
[Mh] Termos MeSH secundário: Benzoatos/química
Estabilidade Enzimática
Enzimas Imobilizadas/química
Esterificação
Eugenol/metabolismo
Microbiologia Industrial
Lipase/química
Nanoestruturas/química
Rhizomucor/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoates); 0 (Enzymes, Immobilized); 1398-61-4 (Chitin); 3T8H1794QW (Eugenol); 9012-76-4 (Chitosan); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1405021


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[PMID]:28946274
[Au] Autor:Morales-Medina R; Munio M; Guadix A; Guadix EM; Camacho F
[Ad] Endereço:Department of Chemical Engineering, University of Granada, 18071 Granada, Spain. Electronic address: rocio_morales@ugr.es.
[Ti] Título:A lumped model of the lipase catalyzed hydrolysis of sardine oil to maximize polyunsaturated fatty acids content in acylglycerols.
[So] Source:Food Chem;240:286-294, 2018 Feb 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The aim of this work was to produce diacylglycerols (DAG) and monoacylglycerols (MAG) with a high content of polyunsaturated fatty acids (PUFA). Rhizomucor miehei lipase mediated-hydrolysis of sardine oil was conducted at several water activities. The system was mechanistically modeled to predict the time evolution of the concentration of triacylglycerols, DAG, MAG and free fatty acids (FFA) and the concentration of saturated, mono- and polyunsaturated fatty acids. The release of the first fatty acid from the triacylglycerol was independent on the unsaturation degree. Contrary, the hydrolysis of the second one was highly affected by the degree of unsaturation, PUFA being the fatty acids that showed the highest resistance to hydrolysis. MAG percentage was maximum (7mol%) at lower water activities, while DAG content was favored at higher water activities (35mol%), achieving a 2-fold concentration of DHA.
[Mh] Termos MeSH primário: Óleos de Peixe/metabolismo
Lipase/metabolismo
[Mh] Termos MeSH secundário: Animais
Ácidos Graxos
Ácidos Graxos Insaturados
Peixes
Glicerídeos
Hidrólise
Rhizomucor
Triglicerídeos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Fatty Acids, Unsaturated); 0 (Fish Oils); 0 (Glycerides); 0 (Triglycerides); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE


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[PMID]:28573851
[Au] Autor:Sánchez DA; Tonetto GM; Ferreira ML
[Ad] Endereço:Planta Piloto de Ingeniería Química (PLAPIQUI), Universidad Nacional del Sur (UNS)-CONICET , Camino La Carrindanga Km 7, CC 717, 8000 Bahía Blanca, Argentina.
[Ti] Título:Screening of Lipases with Unusual High Activity in the sn-2 Esterification of 1,3-Dicaprin under Mild Operating Conditions.
[So] Source:J Agric Food Chem;65(24):5010-5017, 2017 Jun 21.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work, the synthesis of acylglycerides with high nutritional value was carried out by enzymatic esterification at sn-2 position of 1,3-dicaprin with palmitic acid. A comparative study of the performance of several biocatalysts according to the obtained products was carried out. The results obtained with several of the biocatalysts evaluated are very interesting, and it would be possible to use them to obtain a mixture of acylglycerides to act as a fat substitute. The final product was composed of about 90% of nutritionally attractive glycerides. These glycerides were medium-chain length triglycerides, medium-long chain triglycerides (mainly triglycerides with medium chain fatty acids at sn-1 and sn-3 positions and long chain fatty acid at sn-2 position), and 1,3-diglycerides. Pseudomonas fluorescens lipase and Burkholderia cepacia lipase immobilized on chitosan demonstrated unusual high activity in the sn-2 esterification of 1,3-dicaprin with palmitic acid at 45 °C and 12 h with 33% yield to 1,3-dicaproyl-2-palmitoyl glycerol. Burkholderia cepacia lipase has the advantage of being immobilized; however, BCL/chitosan has the advantages of being immobilized and therefore its easy recovery from the reaction media.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Burkholderia cepacia/enzimologia
Diglicerídeos/química
Proteínas Fúngicas/química
Lipase/química
Pseudomonas fluorescens/enzimologia
Rhizomucor/enzimologia
[Mh] Termos MeSH secundário: Biocatálise
Enzimas Imobilizadas/química
Esterificação
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Diglycerides); 0 (Enzymes, Immobilized); 0 (Fungal Proteins); 17598-93-5 (1,3-didecanoylglycerol); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170703
[Lr] Data última revisão:
170703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01327


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[PMID]:28110660
[Au] Autor:Fernandez-Lopez L; Pedrero SG; Lopez-Carrobles N; Gorines BC; Virgen-Ortíz JJ; Fernandez-Lafuente R
[Ad] Endereço:Departamento de biocatálisis. Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain.
[Ti] Título:Effect of protein load on stability of immobilized enzymes.
[So] Source:Enzyme Microb Technol;98:18-25, 2017 Mar.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Different lipases have been immobilized on octyl agarose beads at 1mg/g and at maximum loading, via physical interfacial activation versus the octyl layer on the support. The stability of the preparations was analyzed. Most biocatalysts had the expected result: the apparent stability increased using the highly loaded preparations, due to the diffusional limitations that reduced the initial observed activity. However, lipase B from Candida antarctica (CALB) was significantly more stable using the lowly loaded preparation than the maximum loaded one. This negative effect of the enzyme crowding on enzyme stability was found in inactivations at pH 5, 7 or 9, but not in inactivations in the presence of organic solvents. The immobilization using ethanol to reduce the immobilization rate had no effect on the stability of the lowly loaded preparation, while the highly loaded enzyme biocatalysts increased their stabilities, becoming very similar to that of the lowly loaded preparation. Results suggested that CALB molecules immobilized on octyl agarose may be closely packed together due to the high immobilization rate and this produced some negative interactions between immobilized enzyme molecules during enzyme thermal inactivation. Slowing-down the immobilization rate may be a solution for this unexpected problem.
[Mh] Termos MeSH primário: Enzimas Imobilizadas/metabolismo
Lipase/metabolismo
[Mh] Termos MeSH secundário: Ascomicetos/enzimologia
Biocatálise
Biotecnologia
Estabilidade Enzimática
Enzimas Imobilizadas/antagonistas & inibidores
Enzimas Imobilizadas/química
Proteínas Fúngicas/antagonistas & inibidores
Proteínas Fúngicas/química
Proteínas Fúngicas/metabolismo
Cinética
Lipase/antagonistas & inibidores
Lipase/química
Rhizomucor/enzimologia
Sefarose/análogos & derivados
Solventes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Fungal Proteins); 0 (Solvents); 69106-60-1 (octyl-sepharose CL-4B); 9012-36-6 (Sepharose); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (lipase B, Candida antarctica)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170124
[St] Status:MEDLINE


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[PMID]:28067789
[Au] Autor:Virgen-Ortíz JJ; Pedrero SG; Fernandez-Lopez L; Lopez-Carrobles N; Gorines BC; Otero C; Fernandez-Lafuente R
[Ad] Endereço:CONACYT-Centro de Investigación en Alimentación y Desarrollo, A.C. (CIAD)-Centro de Innovación y Desarrollo Agroalimentario de Michoacán, A.C. (CIDAM), Km. 8 Antigua Carretera a Pátzcuaro s/n, C.P. 58341 Morelia, Michoacán, Mexico. juanvirgen@hotmail.com.
[Ti] Título:Desorption of Lipases Immobilized on Octyl-Agarose Beads and Coated with Ionic Polymers after Thermal Inactivation. Stronger Adsorption of Polymers/Unfolded Protein Composites.
[So] Source:Molecules;22(1), 2017 Jan 05.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Lipases from (isoform B) and (CALB and RML) have been immobilized on octyl-agarose (OC) and further coated with polyethylenimine (PEI) and dextran sulfate (DS). The enzymes just immobilized on OC supports could be easily released from the support using 2% SDS at pH 7, both intact or after thermal inactivation (in fact, after inactivation most enzyme molecules were already desorbed). The coating with PEI and DS greatly reduced the enzyme release during thermal inactivation and improved enzyme stability. However, using OC-CALB/RML-PEI-DS, the full release of the immobilized enzyme to reuse the support required more drastic conditions: a pH value of 3, a buffer concentration over 2 M, and temperatures above 45 °C. However, even these conditions were not able to fully release the thermally inactivated enzyme molecules from the support, being necessary to increase the buffer concentration to 4 M sodium phosphate and decrease the pH to 2.5. The formation of unfolded protein/polymers composites seems to be responsible for this strong interaction between the octyl and some anionic groups of OC supports. The support could be reused five cycles using these conditions with similar loading capacity of the support and stability of the immobilized enzyme.
[Mh] Termos MeSH primário: Candida/enzimologia
Enzimas Imobilizadas/química
Lipase/química
Rhizomucor/enzimologia
Sefarose/química
[Mh] Termos MeSH secundário: Adsorção
Reagentes para Ligações Cruzadas/química
Sulfato de Dextrana/química
Inibidores Enzimáticos/química
Proteínas Fúngicas/química
Polietilenoimina/química
Polímeros
Desdobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (Enzyme Inhibitors); 0 (Enzymes, Immobilized); 0 (Fungal Proteins); 0 (Polymers); 9002-98-6 (Polyethyleneimine); 9012-36-6 (Sepharose); 9042-14-2 (Dextran Sulfate); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE


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[PMID]:28028882
[Au] Autor:Raftari M; Ghafourian S; Abu Bakar F
[Ad] Endereço:Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
[Ti] Título:Simultaneous lactic acidification and coagulation by using recombinant Lactococcus lactis strain.
[So] Source:J Appl Microbiol;122(4):1009-1019, 2017 Apr.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: This study was an attempt to create a novel milk clotting procedure using a recombinant bacterium capable of milk coagulation. METHODS AND RESULTS: The Rhizomucor pusillus proteinase (RPP) gene was sub-cloned into a pALF expression vector. The recombinant pALF-RPP vector was then electro-transferred into Lactococcus lactis. Finally, the milk coagulation ability of recombinant L. lactis carrying a RPP gene was evaluated. Nucleotide sequencing of DNA insertion from the clone revealed that the RPP activity corresponded to an open reading frame consisting of 1218 bp coding for a 43·45 kDa RPP protein. The RPP protein assay results indicated that the highest RPP enzyme expression with 870 Soxhlet units (SU) per ml and 7914 SU/OD were obtained for cultures which were incubated at pH 5·5 and 30°C. Interestingly, milk coagulation was observed after 205 min of inoculating milk with recombinant L. lactis carrying the RPP gene. CONCLUSION: The recombinant L. lactis carrying RPP gene has the ability to function as a starter culture for acidifying and subsequently coagulating milk by producing RPP as a milk coagulant agent. SIGNIFICANCE AND IMPACT OF THE STUDY: Creating a recombinant starter culture bacterium that is able to coagulate milk. It is significant because the recombinant L. lactis has the ability to work as a starter culture and milk coagulation agent.
[Mh] Termos MeSH primário: Lactococcus lactis/genética
Leite
Peptídeo Hidrolases/genética
[Mh] Termos MeSH secundário: Animais
Ácido Láctico/metabolismo
Lactococcus lactis/metabolismo
Peptídeo Hidrolases/metabolismo
Proteínas Recombinantes/metabolismo
Rhizomucor/enzimologia
Rhizomucor/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 33X04XA5AT (Lactic Acid); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170525
[Lr] Data última revisão:
170525
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1111/jam.13388


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[PMID]:27988409
[Au] Autor:Andrey DO; Kaiser L; Emonet S; Erard V; Chalandon Y; van Delden C
[Ad] Endereço:Service of Infectious Diseases, Department of Medical Specialties, Geneva University Hospitals, Rue Gabrielle-Perret-Gentil 4, 1211 Geneva 14, Switzerland. Electronic address: diego.andrey@hcuge.ch.
[Ti] Título:Cerebral Rhizomucor Infection Treated by Posaconazole Delayed-Release Tablets in an Allogeneic Stem Cell Transplant Recipient.
[So] Source:Int J Infect Dis;55:24-26, 2017 Feb.
[Is] ISSN:1878-3511
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Mucormycosis (zygomycosis) is an emerging fungal disease in allogeneic hematopoietic stem cell transplant (allo-HSCT) recipients. A 30-year-old woman diagnosed with acute myelomonocytic leukemia and needing allo-HSCT presented pulmonary and cerebral infection due to Rhizomucor pusillus. This fungal infection was treated with surgical treatment and posaconazole delayed-release tablets. This strategy allowed reaching high drug levels that could not be obtained with the posaconazole solution.
[Mh] Termos MeSH primário: Antifúngicos/uso terapêutico
Leucemia Mielomonocítica Aguda/cirurgia
Mucormicose/tratamento farmacológico
Mucormicose/microbiologia
Transplante de Células-Tronco
Triazóis/uso terapêutico
[Mh] Termos MeSH secundário: Adulto
Preparações de Ação Retardada
Evolução Fatal
Feminino
Seres Humanos
Hospedeiro Imunocomprometido
Leucemia Mielomonocítica Aguda/imunologia
Mucormicose/diagnóstico
Mucormicose/imunologia
Rhizomucor/efeitos dos fármacos
Comprimidos
Transplante Homólogo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Delayed-Action Preparations); 0 (Tablets); 0 (Triazoles); 6TK1G07BHZ (posaconazole)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161219
[St] Status:MEDLINE


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[PMID]:27780957
[Au] Autor:Takó M; KotogÁn A; Papp T; Kadaikunnan S; Alharbi NS; VÁgvölgyi C
[Ad] Endereço:Department of Microbiology, Faculty of Science and Informatics, University of Szeged, H-6726 Szeged, Közép fasor 52, Hungary.
[Ti] Título:Purification and Properties of Extracellular Lipases with Transesterification Activity and 1,3-Regioselectivity from and .
[So] Source:J Microbiol Biotechnol;27(2):277-288, 2017 Feb 28.
[Is] ISSN:1738-8872
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:NRRL 5282 and NRRL 1526 can produce lipases with high synthetic activities in wheat bran-based solid-state culture. In this study, the purification and biochemical characterization of the lipolytic activities of these lipases are presented. SDS-PAGE indicated a molecular mass of about 55 and 35 kDa for the purified and enzymes, respectively. -Nitrophenyl palmitate ( NPP) hydrolysis was maximal at 40°C and pH 7.0 for the lipase, and at 30°C and pH 5.2 for the enzyme. The enzymes showed almost equal affinity to NPP, but the of the lipase was about 1.13 times higher than that determined for using the same substrate. For both enzymes, a dramatic loss of activity was observed in the presence of 5 mM Hg , Zn , or Mn , 10 mM -bromosuccinimide or sodium dodecyl sulfate, and 5-10% (v/v) of hexanol or butanol. At the same time, they proved to be extraordinarily stable in the presence of -hexane, cyclohexane, -heptane, and isooctane. Moreover, isopentanol up to 10% (v/v) and propionic acid in 1 mM concentrations increased the NPP hydrolyzing activity of lipase. Both enzymes had 1,3-regioselectivity, and efficiently hydrolyzed -nitrophenyl ( NP) esters with C8-C16 acids, exhibiting maximum activity towards NP-caprylate ( ) and pNP-dodecanoate ( ). The purified lipases are promising candidates for various biotechnological applications.
[Mh] Termos MeSH primário: Lipase/isolamento & purificação
Lipase/metabolismo
Rhizomucor/enzimologia
Rhizopus/enzimologia
[Mh] Termos MeSH secundário: Bromosuccinimida/farmacologia
Butanóis/farmacologia
Caprilatos/farmacologia
Eletroforese em Gel de Poliacrilamida
Esterificação
Heptanos/farmacologia
Hexanos/farmacologia
Hexanóis/farmacologia
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Lauratos/farmacologia
Lipase/química
Manganês/farmacologia
Mercúrio/farmacologia
Nitrobenzenos/farmacologia
Palmitatos/metabolismo
Propionatos/farmacologia
Rhizomucor/genética
Rhizopus/genética
Dodecilsulfato de Sódio/farmacologia
Zinco/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-nitrophenyl dodecanoate); 0 (Butanols); 0 (Caprylates); 0 (Heptanes); 0 (Hexanes); 0 (Hexanols); 0 (Laurates); 0 (Nitrobenzenes); 0 (Palmitates); 0 (Propionates); 1492-30-4 (4-nitrophenyl palmitate); 1956-10-1 (4-nitrophenyloctanoate); 2DDG612ED8 (n-hexane); 368GB5141J (Sodium Dodecyl Sulfate); 42Z2K6ZL8P (Manganese); 456148SDMJ (n-heptane); EC 3.1.1.3 (Lipase); FXS1BY2PGL (Mercury); J41CSQ7QDS (Zinc); JHU490RVYR (propionic acid); K8G1F2UCJF (Bromosuccinimide)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170328
[Lr] Data última revisão:
170328
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161027
[St] Status:MEDLINE
[do] DOI:10.4014/jmb.1608.08005


  9 / 256 MEDLINE  
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[PMID]:27341522
[Au] Autor:Isah AA; Mahat NA; Jamalis J; Attan N; Zakaria II; Huyop F; Wahab RA
[Ad] Endereço:a Department of Chemistry, Faculty of Science , Universiti Teknologi Malaysia , Johor Bahru , Johor , Malaysia.
[Ti] Título:Synthesis of geranyl propionate in a solvent-free medium using Rhizomucor miehei lipase covalently immobilized on chitosan-graphene oxide beads.
[So] Source:Prep Biochem Biotechnol;47(2):199-210, 2017 Feb 07.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The chemical route of producing geranyl propionate involves the use of toxic chemicals, liberation of unwanted by-products as well as problematic separation process. In view of such problems, the use of Rhizomucor miehei lipase (RML) covalently bound onto activated chitosan-graphene oxide (RML-CS/GO) support is suggested. Following analyses using Fourier transform infrared spectroscopy, field emission scanning electron microscopy, transmission electron microscopy, and thermogravimetry, properties of the RML-CS/GO were characterized. A response surface methodological approach using a 3-level-four-factor (incubation time, temperature, substrate molar ratio, and stirring rate) Box-Behnken design was used to optimize the experimental conditions to maximize the yield of geranyl propionate. Results revealed that 76 ± 0.02% of recovered protein had yielded 7.2 ± 0.04 mg g and 211 ± 0.3% U g of the maximum protein loading and esterification activity, respectively. The actual yield of geranyl propionate (49.46%) closely agreed with the predicted value (49.97%) under optimum reaction conditions (temperature: 37.67°C, incubation time: 10.20 hr, molar ratio (propionic acid:geraniol): 1:3.28, and stirring rate: 100.70 rpm) and hence, verifying the suitability of this approach. Since the method is performed under mild conditions, the RML-CS/GO biocatalyst may prove to be an environmentally benign alternative for producing satisfactory yield of geranyl propionate.
[Mh] Termos MeSH primário: Quitosana/química
Enzimas Imobilizadas/química
Grafite/química
Lipase/química
Propionatos/síntese química
Rhizomucor/enzimologia
[Mh] Termos MeSH secundário: Meios de Cultura
Microscopia Eletrônica de Varredura
Microscopia Eletrônica de Transmissão
Óxidos/química
Solventes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (Enzymes, Immobilized); 0 (Oxides); 0 (Propionates); 0 (Solvents); 7782-42-5 (Graphite); 9012-76-4 (Chitosan); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160625
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2016.1201681


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[PMID]:28025649
[Au] Autor:Trindade LV; Desagiacomo C; Polizeli ML; Damasio AR; Lima AM; Gomes E; Bonilla-Rodriguez GO
[Ad] Endereço:Instituto de Biociências, Letras e Ciências Exatas, Universidade Estadual Paulista (UNESP), São José do Rio Preto, SP, Brazil.
[Ti] Título:Biochemical Characterization, Thermal Stability, and Partial Sequence of a Novel Exo-Polygalacturonase from the Thermophilic Fungus A13.36 Obtained by Submerged Cultivation.
[So] Source:Biomed Res Int;2016:8653583, 2016.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This work reports the production of an exo-polygalacturonase (exo-PG) by A13.36 in submerged cultivation (SmC) in a shaker at 45°C for 96 h. A single pectinase was found and purified in order to analyze its thermal stability, by salt precipitation and hydrophobic interaction chromatography. The pectinase has an estimated Mw of approximately 43.5-47 kDa and optimum pH of 4.0 but is stable in pH ranging from 3.5 to 9.5 and has an optimum temperature of 61°C. It presents thermal stability between 30 and 60°C, has 70% activation in the presence of Ca , and was tested using citrus pectin with a degree of methyl esterification (DE) of 26%. for irreversible denaturation was 125.5 kJ/mol with positive variations of entropy and enthalpy for that and Δ values were around 50 kJ/mol. The hydrolysis of polygalacturonate was analyzed by capillary electrophoresis which displayed a pattern of sequential hydrolysis (exo). The partial identification of the primary sequence was done by MS MALDI-TOF and a comparison with data banks showed the highest identity of the sequenced fragments of exo-PG from with an exo-pectinase from . Pectin hydrolysis showed a sigmoidal curve for the Michaelis-Menten plot.
[Mh] Termos MeSH primário: Proteínas Fúngicas
Poligalacturonase
Rhizomucor
[Mh] Termos MeSH secundário: Estabilidade Enzimática
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Proteínas Fúngicas/isolamento & purificação
Proteínas Fúngicas/secreção
Temperatura Alta
Concentração de Íons de Hidrogênio
Poligalacturonase/química
Poligalacturonase/genética
Poligalacturonase/isolamento & purificação
Poligalacturonase/secreção
Rhizomucor/enzimologia
Rhizomucor/genética
Rhizomucor/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); EC 3.2.1.15 (Polygalacturonase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE
[do] DOI:10.1155/2016/8653583



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