Made available in DSpace on 2016-03-07T19:20:56Z (GMT). No. of bitstreams: 0
Previous issue date: 2015-06-24. Added 1 bitstream(s) on 2016-03-07T19:24:45Z : No. of bitstreams: 1
000849834_20170624.pdf: 1817877 bytes, checksum: 6529269723628cd64b4ebb458eb00ecc (MD5) Bitstreams deleted on 2017-06-30T13:45:02Z: 000849834_20170624.pdf,. Added 1 bitstream(s) on 2017-06-30T13:45:55Z : No. of bitstreams: 1
000849834.pdf: 4488346 bytes, checksum: 33829b4f27a436cb052b3a5f1ed811f3 (MD5) Bitstreams deleted on 2017-08-24T16:17:00Z: 000849834.pdf,. Added 1 bitstream(s) on 2017-08-24T16:17:47Z : No. of bitstreams: 1
000849834.pdf: 4488346 bytes, checksum: 33829b4f27a436cb052b3a5f1ed811f3 (MD5) / Os fungos endofíticos são micro-organismos que vivem nos espaços intercelulares das plantas e são reconhecidos por seu potencial na produção de importantes produtos de interesse biotecnológico, tal como as enzimas. Estas vem sendo amplamente utilizadas nos setor industrial pois catalisam reações com maior especificidade que as formas convencionais de reações químicas, fazendo assim dos fungos endofíticos uma alternativa promissora na produção desses biocatalisadores. Desta forma, este trabalho teve como objetivo a prospecção de enzimas de interesse biotecnológico como lipase, esterase, epóxido-hidrolase, nitrilase, acilase, protease e amidase em fungos endofíticos e a avaliação da sua aplicação biotecnológica, com enfoque na utilização do extrato bruto contendo lipase em processos de biorremediação e transesterificação. Setenta e cinco fungos endofíticos foram submetidos à prospecção de atividade biocatalítica, onde 66 apresentaram atividade lipases/ esterases, 16 epóxido hidrolase, 24 acilases, 50 proteases, 10 nitrilase e 64 amidase. Foram encontrados fungos com satisfatória atividade biocatalítica frente a diferentes metodologias e substratos, mostrando a grande versatilidade dos endófitos na produção de enzimas. O fungo Mycosphaerella coacervata foi selecionado para avaliação da atividade e caracterização parcial da lipase extracelular em extrato bruto. O micro-organismo apresentou produção máxima da enzima quando cultivado por 48 horas a 28oC (486 U/L), e se manteve estável até 6 meses estocada a - 2oC. O extrato bruto contendo a enzima apresentou atividade máxima a 37oC em pH 8,0. A estabilidade térmica foi observada na faixa de 30 a 60oC (atividade residual acima de 80%) e sua estabilidade ao pH entre 6,0 e 9,0.(atividade residual superior a 80%). A enzima se manteve estável (atividade residual acima de 90%) na presença de acetona, metanol... / The endophytic fungi are microorganisms that live in the intercellular spaces of plants and are known for their potential for the production of important products of biotechnological interest, such as enzymes. These have been widely used in industry because they catalyze reactions with greater specificity than conventional forms of chemical reactions, thereby making the endophytic fungus a promising alternative to produce these biocatalysts. Thus, this study aimed to prospect for enzymes of biotechnological interest as lipase, esterase, epoxide hydrolase, nitrilase, acylase, amidase and protease in endophytic fungi and evaluate their biotechnological applications, focusing on the use of the crude extract containing lipase in the transesterification process and bioremediation. Seventy five endophytic fungi were submitted to prospecting biocatalytic activity, where 66 showed lipase / esterase activity, 16 epoxide hydrolase, 24 acylases, 50 proteases, 10 nitrilase and 64 amidase. Fungi with satisfactory biocatalytic activity against different methodologies and substrates were found, showing the versatility of endophytes in the production of enzymes. The fungi Mycosphaerella coacervata was selected to evaluate the activity and partial characterization of extracellular lipase crude extract. The microorganism showed maximum enzyme production when grown for 48 hours at 28°C (486 U / L), and remained stable up to 6 months stored at -2°C. The crude extract containing the enzyme showed maximum activity at 37°C at pH 8.0. The thermal stability was observed in the range of 30 to 60°C (residual activity above 80%) and its stability at the pH between 6.0 and 9.0 (residual activity exceeding 80%). The enzyme was stable (residual activity above 90%) in the presence of acetone, methanol, ethanol, isopropanol and hexane at concentrations of 20 and 50%. Good stability was observed also in relation to different...
Identifer | oai:union.ndltd.org:IBICT/oai:repositorio.unesp.br:11449/136030 |
Date | 24 June 2015 |
Creators | Lisboa, Helen Cristina Fávero [UNESP] |
Contributors | Universidade Estadual Paulista (UNESP), Martins, Daniela Alonso Bocchini [UNESP] |
Publisher | Universidade Estadual Paulista (UNESP) |
Source Sets | IBICT Brazilian ETDs |
Language | Portuguese |
Detected Language | Portuguese |
Type | info:eu-repo/semantics/publishedVersion, info:eu-repo/semantics/doctoralThesis |
Format | 222 f. : il. - |
Source | Aleph, reponame:Repositório Institucional da UNESP, instname:Universidade Estadual Paulista, instacron:UNESP |
Rights | info:eu-repo/semantics/openAccess |
Relation | -1, -1 |
Page generated in 0.0016 seconds