Utilization of agroindustrial byproducts for the production of lipase by a new strain of Pseudomonas sp.
DOI:
https://doi.org/10.5433/1679-0367.2020v41n2p165Palabras clave:
Crude lecithin gum, Chicken fat, Enzyme, FermentationResumen
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.Descargas
Los datos de descargas todavía no están disponibles.
Citas
Patel N, Rai D, Shivam, Shahane S, Mishra U. Lipases: Sources, Production, Purification, and Applications. Recent Pat Biotechnol. 2018;12:1-12. doi: 10.2174/1872208312666181029093333.
Rodrigues RC, Virgen-Ortíz JJ, Dos Santos JCS, Berenguer-Murcia Á, Alcantara AR, Barbosa O, Ortiz C, Fernandez-Lafuente R. Immobilization of lipases on hydrophobic supports: mmobilization mechanism, advantages, problems, and solutions. Biotechnol Adv. 2019;37(5):746-70. doi: 10.1016/j.biotechadv.2019.04.003.
Shuai W, Das RK, Naghdi M, Brar SK, Verma M. A review on the important aspects of lipase immobilization on nanomaterials. Biotechnol Appl Biochem. 2017;64(4):496-508. doi: 10.1002/bab.1515.
Villeneuve P, Muderhwa JM, Graille J, Haas, MJ. Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J Mol Catal B-Enzym. 2000;9(4-6):113-48. doi: 10.1016/S1381-1177(99)00107-1
Barros M, Fleuri LF, Macedo GA. Seed Lipase: sources, applications and properties a review. Braz J Chem Eng. 2010;27(1):15-29. doi: 0.1590/S0104-66322010000100002
Choudhury P, Bhunia B. Industrial application of lipase: a review. Biopharm J. 2015; 1(2): 41-7.
Treichel H, Oliveira D, Mazutti MA, Di Luccio M, Oliveira JV. A review on microbial lipases production. Food Bioproc Tech. 2010;3(2):182-96. doi: 0.1007/s11947-009-0202-2
Smaniotto A, Skovronski A, Rigo E, Tsai SM, Durrer A, Foltran LL, Treichel H. Concentration, characterization and application of lipases from Sporidiobolus pararoseus strain. Braz J Microbiol. 2014;45(1);294-302. doi: 10.1590/S1517-83822014000100043
Weisburg WG. Barns SM, Pelletier DA, Lane, DJ. 16S ribosomal DNA amplification for phylogenetic study. J Bacteriol. 1991;173(2):697-703. doi: 10.1128/jb.173.2.697-703.1991
Young JP, Downer HL, Eardly BD. Phylogeny of the phototrophic rhizobium strain BTAi1 by polymerase chain reaction-based sequencing of a 16S rRNA gene segment. J Bacteriol. 1991;173(7): 2271-7. doi: 10.1128/jb.173.7.2271-2277.1991
Menna P, Hungria M, Barcellos FG, Bangel EV, Hess PN, Martínez-Romero E. Molecular phylogeny based on the 16S rRNA gene of elite rhizobial strains used in Brazilian commercial inoculants. Syst Appl Microbiol. 2006;29(4):315-32. doi: 10.1016/j.syapm.2005.12.002
Winkler UK, Stuckmann M. Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. Journal of Bacteriology, 1979; 138(3):663-70.doi: 0021-9193/79/06-0663/08$02.00/0
Bisht D, Yadav SK, Gautam P, Darmwal NS. Simultaneous production of alcaline lipase and protease by antibiotic and heavy metal tolerant Pseudomonas aeroginosa. J Basic Microbiol. 2012;52:1-8.doi: 10.1002/jobm.201200157
Ruchi G, Anshu G, Khare SK. Lipase from solvent tolerant Pseudomonas aeruginosa strain: Production optimization by response surface methodology and application. Bioresour Technol. 2008;99(11):4796–802. https://doi.org/10.1016/j.biortech.2007.09.053
Centenaro, GS, Furlan VJM, Souza-Soares LA. Gordura de frango: alternativas tecnológicas e nutricionais. Semina Ciênc Agrár. 2008;29(3):619-30.
Said NW. Extrusion of alternative feed ingredients: An environmental and nutritional solution. J Appl Poult Res. 1996;5:395-407
Kiran GS, Shanmughapriya S, Jayalakshmi J, Selvin J, Gandhimathi, R., Sivaramakrishnan S, et al. Optimization of extracellular psychrophilic alkaline lipase produced by marine Pseudomonas sp. (MSI057). Bioproc Biosyst Eng. 2008;31(5):483-92. doi: 10.1007/s00449-007-0186-0
Marques TA, Baldo C, Borsato D, Buzato JB, Celligoi MAPC. Utilization of dairy effluent as alternative fermentation medium for microbial lipase production. Rom Biotechnol Lett. 2014;19(1):9042-50.
Ramani A, Kennedy LJ, Ramakrishnan M, Sekaran G. Purification, characterization and application of acidic lipase from Pseudomonas gessardii using beef tallow as a substrate for fats and oil hydrolysis. Process Biochem. 2010;45(10),1683-91. doi: 10.1016/j.procbio.2010.06.023
Salihu A, Alam MZ, Abdulkarim MI, Salleh HM. Optimization of lipase production by Candida cylindracea in palm oil mill effluent based medium using statistical experimental design. J Mol Catal B-Enzym. 2011;69(1-2):66-73. doi: 10.1016/j.molcatb.2010.12.012
Asih DR, Alam MZ, Salleh MN, Salihu A. Pilot-scale production of lipase using palm oil mill effluent as a basal medium and its immobilization by selected materials. J Oleo Sci. 2014;63(8):779-85. doi: 10.5650/jos.ess13187
Jinwal U, Roy U, Chowdhury A, Bhaduri A, Roy PK. Purification and characterization of an alkaline lipase from a newly isolated Pseudomonas mendoncina PK-12Cs and chemoselective hydrolysis of fatty acid ester. Bioorg Med Chem. 2003;11(6):1041-1046. doi: 10.1016/S0968-0896(02)00516-3
Karadzic I, Masui A, Zivkovic LI, Fujiwara N. Purification and characterization of an alkaline lipase from Pseudomonas aeruginosa isolated from putrid mineral cutting oil as component of metalworking fluid. J. Biosci Bioeng. 2006;102: 82-9. doi: 10.1263/jbb.102.82
Dandavate V, Jinjala J, Keharia H, Madamwar D. Production, partial purification and characterization of organic solvente tolerant lipase from Burkholderia multivorans V2 and its application for ester synthesis, Bioresour Technol. 2009;100(13):3374-81. doi: 10.1016/j.biortech.2009.02.011
Rodrigues RC, Virgen-Ortíz JJ, Dos Santos JCS, Berenguer-Murcia Á, Alcantara AR, Barbosa O, Ortiz C, Fernandez-Lafuente R. Immobilization of lipases on hydrophobic supports: mmobilization mechanism, advantages, problems, and solutions. Biotechnol Adv. 2019;37(5):746-70. doi: 10.1016/j.biotechadv.2019.04.003.
Shuai W, Das RK, Naghdi M, Brar SK, Verma M. A review on the important aspects of lipase immobilization on nanomaterials. Biotechnol Appl Biochem. 2017;64(4):496-508. doi: 10.1002/bab.1515.
Villeneuve P, Muderhwa JM, Graille J, Haas, MJ. Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J Mol Catal B-Enzym. 2000;9(4-6):113-48. doi: 10.1016/S1381-1177(99)00107-1
Barros M, Fleuri LF, Macedo GA. Seed Lipase: sources, applications and properties a review. Braz J Chem Eng. 2010;27(1):15-29. doi: 0.1590/S0104-66322010000100002
Choudhury P, Bhunia B. Industrial application of lipase: a review. Biopharm J. 2015; 1(2): 41-7.
Treichel H, Oliveira D, Mazutti MA, Di Luccio M, Oliveira JV. A review on microbial lipases production. Food Bioproc Tech. 2010;3(2):182-96. doi: 0.1007/s11947-009-0202-2
Smaniotto A, Skovronski A, Rigo E, Tsai SM, Durrer A, Foltran LL, Treichel H. Concentration, characterization and application of lipases from Sporidiobolus pararoseus strain. Braz J Microbiol. 2014;45(1);294-302. doi: 10.1590/S1517-83822014000100043
Weisburg WG. Barns SM, Pelletier DA, Lane, DJ. 16S ribosomal DNA amplification for phylogenetic study. J Bacteriol. 1991;173(2):697-703. doi: 10.1128/jb.173.2.697-703.1991
Young JP, Downer HL, Eardly BD. Phylogeny of the phototrophic rhizobium strain BTAi1 by polymerase chain reaction-based sequencing of a 16S rRNA gene segment. J Bacteriol. 1991;173(7): 2271-7. doi: 10.1128/jb.173.7.2271-2277.1991
Menna P, Hungria M, Barcellos FG, Bangel EV, Hess PN, Martínez-Romero E. Molecular phylogeny based on the 16S rRNA gene of elite rhizobial strains used in Brazilian commercial inoculants. Syst Appl Microbiol. 2006;29(4):315-32. doi: 10.1016/j.syapm.2005.12.002
Winkler UK, Stuckmann M. Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. Journal of Bacteriology, 1979; 138(3):663-70.doi: 0021-9193/79/06-0663/08$02.00/0
Bisht D, Yadav SK, Gautam P, Darmwal NS. Simultaneous production of alcaline lipase and protease by antibiotic and heavy metal tolerant Pseudomonas aeroginosa. J Basic Microbiol. 2012;52:1-8.doi: 10.1002/jobm.201200157
Ruchi G, Anshu G, Khare SK. Lipase from solvent tolerant Pseudomonas aeruginosa strain: Production optimization by response surface methodology and application. Bioresour Technol. 2008;99(11):4796–802. https://doi.org/10.1016/j.biortech.2007.09.053
Centenaro, GS, Furlan VJM, Souza-Soares LA. Gordura de frango: alternativas tecnológicas e nutricionais. Semina Ciênc Agrár. 2008;29(3):619-30.
Said NW. Extrusion of alternative feed ingredients: An environmental and nutritional solution. J Appl Poult Res. 1996;5:395-407
Kiran GS, Shanmughapriya S, Jayalakshmi J, Selvin J, Gandhimathi, R., Sivaramakrishnan S, et al. Optimization of extracellular psychrophilic alkaline lipase produced by marine Pseudomonas sp. (MSI057). Bioproc Biosyst Eng. 2008;31(5):483-92. doi: 10.1007/s00449-007-0186-0
Marques TA, Baldo C, Borsato D, Buzato JB, Celligoi MAPC. Utilization of dairy effluent as alternative fermentation medium for microbial lipase production. Rom Biotechnol Lett. 2014;19(1):9042-50.
Ramani A, Kennedy LJ, Ramakrishnan M, Sekaran G. Purification, characterization and application of acidic lipase from Pseudomonas gessardii using beef tallow as a substrate for fats and oil hydrolysis. Process Biochem. 2010;45(10),1683-91. doi: 10.1016/j.procbio.2010.06.023
Salihu A, Alam MZ, Abdulkarim MI, Salleh HM. Optimization of lipase production by Candida cylindracea in palm oil mill effluent based medium using statistical experimental design. J Mol Catal B-Enzym. 2011;69(1-2):66-73. doi: 10.1016/j.molcatb.2010.12.012
Asih DR, Alam MZ, Salleh MN, Salihu A. Pilot-scale production of lipase using palm oil mill effluent as a basal medium and its immobilization by selected materials. J Oleo Sci. 2014;63(8):779-85. doi: 10.5650/jos.ess13187
Jinwal U, Roy U, Chowdhury A, Bhaduri A, Roy PK. Purification and characterization of an alkaline lipase from a newly isolated Pseudomonas mendoncina PK-12Cs and chemoselective hydrolysis of fatty acid ester. Bioorg Med Chem. 2003;11(6):1041-1046. doi: 10.1016/S0968-0896(02)00516-3
Karadzic I, Masui A, Zivkovic LI, Fujiwara N. Purification and characterization of an alkaline lipase from Pseudomonas aeruginosa isolated from putrid mineral cutting oil as component of metalworking fluid. J. Biosci Bioeng. 2006;102: 82-9. doi: 10.1263/jbb.102.82
Dandavate V, Jinjala J, Keharia H, Madamwar D. Production, partial purification and characterization of organic solvente tolerant lipase from Burkholderia multivorans V2 and its application for ester synthesis, Bioresour Technol. 2009;100(13):3374-81. doi: 10.1016/j.biortech.2009.02.011
Descargas
Publicado
2020-07-07
Cómo citar
1.
Baldo C, Baggio LM, Oliveira MR, Melo MR, Gasparin FGM, Celligoi MAPC. Utilization of agroindustrial byproducts for the production of lipase by a new strain of Pseudomonas sp. Semin. Cienc. Biol. Saude [Internet]. 7 de julio de 2020 [citado 21 de noviembre de 2024];41(2):165-76. Disponible en: https://ojs.uel.br/revistas/uel/index.php/seminabio/article/view/36728
Número
Sección
Artigos
Licencia
Derechos de autor 2020 Semina: Ciências Biológicas e da Saúde
Esta obra está bajo una licencia internacional Creative Commons Atribución-NoComercial 4.0.
Semina: Ciências Biológicas e da Saúde adota para suas publicações a licença CC-BY-NC, sendo os direitos autorais do autor, em casos de republicação recomendamos aos autores a indicação de primeira publicação nesta revista.
Esta licença permite copiar e redistribuir o material em qualquer meio ou formato, remixar, transformar e desenvolver o material, desde que não seja para fins comerciais. E deve-se atribuir o devido crédito ao criador.
As opiniões emitidas pelos autores dos artigos são de sua exclusiva responsabilidade.
A revista se reserva o direito de efetuar, nos originais, alterações de ordem normativa, ortográfica e gramatical, com vistas a manter o padrão culto da língua e a credibilidade do veículo. Respeitará, no entanto, o estilo de escrever dos autores. Alterações, correções ou sugestões de ordem conceitual serão encaminhadas aos autores, quando necessário.
Este obra está licenciado com uma Licença Creative Commons Atribuição-NãoComercial 4.0 Internacional.
