Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa.
77 Páginas.
- Autores:
-
Morales González, María Paula
Stepanian Martínez, Boghos Sneider
- Tipo de recurso:
- Trabajo de grado de pregrado
- Fecha de publicación:
- 2017
- Institución:
- Universidad de la Sabana
- Repositorio:
- Repositorio Universidad de la Sabana
- Idioma:
- spa
- OAI Identifier:
- oai:intellectum.unisabana.edu.co:10818/30083
- Acceso en línea:
- https://hdl.handle.net/10818/30083
- Palabra clave:
- Enzimas microbianas
Química farmacéutica -- Investigaciones
Agentes antibacteriales
Crecimiento bacterial
- Rights
- License
- Attribution-NonCommercial-NoDerivatives 4.0 International
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Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. |
| title |
Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. |
| spellingShingle |
Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. Enzimas microbianas Química farmacéutica -- Investigaciones Agentes antibacteriales Crecimiento bacterial |
| title_short |
Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. |
| title_full |
Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. |
| title_fullStr |
Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. |
| title_full_unstemmed |
Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. |
| title_sort |
Modelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa. |
| dc.creator.fl_str_mv |
Morales González, María Paula Stepanian Martínez, Boghos Sneider |
| dc.contributor.advisor.none.fl_str_mv |
Díaz Barrera, Luis Eduardo Cortázar Gómez, Jorge Eduardo |
| dc.contributor.author.none.fl_str_mv |
Morales González, María Paula Stepanian Martínez, Boghos Sneider |
| dc.subject.none.fl_str_mv |
Enzimas microbianas Química farmacéutica -- Investigaciones Agentes antibacteriales Crecimiento bacterial |
| topic |
Enzimas microbianas Química farmacéutica -- Investigaciones Agentes antibacteriales Crecimiento bacterial |
| description |
77 Páginas. |
| publishDate |
2017 |
| dc.date.accessioned.none.fl_str_mv |
2017-04-04T22:31:18Z |
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2017-04-04T22:31:18Z |
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2017 |
| dc.date.issued.none.fl_str_mv |
2017-04-04 |
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Tesis/Trabajo de grado - Pregrado |
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http://purl.org/coar/resource_type/c_7a1f |
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info:eu-repo/semantics/bachelorThesis |
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http://purl.org/redcol/resource_type/TP |
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Amena, S; Vishalakshi, N; Prabhakar, M; Dayanand, A; Lingappa, K. (2010). Production, purification and characterization of l-asparaginase from. Brazilian Journal of Microbiology, 41, 173¿178. Amena, S; Vishalakshi, N; Prabhakar, M; Dayanand, A; Lingappa, K. (2010). Production, purification and characterization of l-asparaginase from. Brazilian Journal of Microbiology, 41, 173¿178. Arrivukkarasan, S., Muthusivaramapandian, M., Aravindan, R., & Viruthagiri, T. (2010). Effect of Medium Composition and Kinetic Studies on Extracellular and Intracellular Production of Lasparaginase from Pectobacterium carotovorum. Food Science and Technology International, 16(2), 115¿125. http://doi.org/10.1177/1082013209353219 Bapat, P. M., Sohoni, S. V., Moses, T. A., & Wangikar, P. P. (2006). A cybernetic model to predict the effect of freely available nitrogen substrate on rifamycin B production in complex media. Applied Microbiology and Biotechnology, 72(4), 662¿670. http://doi.org/10.1007/s00253-006-0341-6 Bazaraa, W., Alian, A., El-Shimi, N., & Mohamed, R. (2016). Purification and characterization of extracellular glutaminase from Aspergillus oryzae NRRL 32567. Biocatalysis and Agricultural Biotechnology, 6, 76¿81. http://doi.org/10.1016/j.bcab.2016.02.009 Bhunia, B., Basak, B., & Dey, A. (2012). A review on production of serine alkaline protease by Bacillus spp . J. Biochem Tech, 3(4), 448¿457 Boqué, R., & Maroto, A. (2004). El Análisis De La Varianza (Anova ). Universitat Rovira I Virgili., 1¿6. Bruns, R. E., Scarminio, I. S., & Neto, B. B. (2006). Statistical Design ¿ Chemometrics. El sevier Science Cavazzuti, M. (2013). Optimization Methods: From Theory to Design Scientific and Technological Aspects in Mechanics. http://doi.org/10.1007/978-3-642-31187-1 Chohan, S. M., & Rashid, N. (2013). TK1656, a thermostable lasparaginase from Thermococcus kodakaraensis, exhibiting highest ever reported enzyme activity. Journal of Bioscience and Bioengineering, 116(4), 438¿43. http://doi.org/10.1016/j.jbiosc.2013.04.005 Chow, Y., & Ting, A. S. Y. (2014). Endophytic l-asparaginase-producing fungi from plants associated with anticancer properties. Journal of Advanced Research. http://doi.org/10.1016/j.jare.2014.07.005 Crump, A. (2014). The advent of ivermectin: People, partnerships, and principles. Trends in Parasitology, 30(9), 423¿425. http://doi.org/10.1016/j.pt.2014.07.001 Derst, C., Henseling, J., & Röhm, K. H. (2000). Engineering the substrate specificity of Escherichia coli asparaginase. II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Science¿: A Publication of the Protein Society, 9(10), 2009¿17. http://doi.org/10.1110/ps.9.10.2009 Deshpande, N., Choubey, P., & Agashe, M. (2014). Studies on optimization of growth parameters for L-asparaginase production by streptomyces ginsengisoli. The Scientific World Journal, 2014, 1¿7. Dhevagi, P., & Poorani, E. (2006). Isolation and characterization of L - asparaginase from marine actinomycetes. Indian Journal of Biotechnology, 5(December 2003), 514¿520. Dias, F. F. G., & Sato, H. H. (2016). Sequential optimization strategy for maximum L-asparaginase production from Aspergillus oryzae CCT 3940. Biocatalysis and Agricultural Biotechnology, 6, 33¿39. http://doi.org/10.1016/j.bcab.2016.02.006 El-naggar, N. E., Deraz, S. F., Soliman, H. M., & El-deeb, N. M. (2016). Purification, characterization, cytotoxicity and anticancer activities of L-asparaginase , anti-colon cancer protein, from the newly isolated alkaliphilic Streptomyces fradiae NEAE-82. Scientific Reports, 1¿16. http://doi.org/10.1038/srep32926 El-naggar, N. E., Moawad, H., El-shweihy, N. M., & El-ewasy, S. M. (2015). Optimization of Culture Conditions for Production of the AntiLeukemic Glutaminase Free L-Asparaginase by Newly Isolated Streptomyces olivaceus NEAE-119 Using Response Surface Methodology. BioMed Research International, 2015. http://doi.org/10.1155/2015/627031 El-sayed, S. T., Fyiad, A. a, & Gamal-eldeen, A. M. (2012). Immobilization , Properties and Anti-tumor Activity of L-asparaginase of Vicia faba and Phaseoulus vulgaris Seeds. Australian Journal of Basic and Applied Sciences, 6(3), 785¿794. Farag, A. M., Hassan, S. W., Beltagy, E. A., & El-Shenawy, M. A. (2015). Optimization of production of anti-tumor l-asparaginase by free and immobilized marine Aspergillus terreus. Egyptian Journal of Aquatic Research, 41(4), 295¿302. http://doi.org/10.1016/j.ejar.2015.10.002 Fu, C. H., & Sakamoto, K. M. (2007). PEG-asparaginase. Expert Opinion on Pharmacotherapy, 8(12), 1977¿84. http://doi.org/10.1517/14656566.8.12.1977 García, H., & Vázquez, R. (1998). Cuantificación De Proteínas: Una Revisión. BioTecnologia (Vol. 3). Gonçalves Dias, F. F., Soares de Castro, R. J., Ohara, A., Nishide, T. G., Bagagl Pavan, M., & Sato, H. H. (2015). Simplex centroid mixture design to improve l-asparaginase production in solid-state fermentation using agroindustrial wastes. Biocatalysis and Agricultural Biotechnology, 4(4), 528¿534. http://doi.org/10.1016/j.bcab.2015.09.011 Gulati, R., Saxena, R. K., & Gupta, R. (1997). A rapid plate assay for screening L-asparaginase producing micro-organisms. Letters in Applied Microbiology, 24(1), 23¿26 Gunst, R. F. (1996). Response surface methodology: process and product optimization using designed experiments. Technometrics, 38(3), 284¿ 286. http://doi.org/10.2307/1270613 Hatanaka, T., Usuki, H., Arima, J., Uesugi, Y., Yamamoto, Y., Kumagai, Y., ¿ Mukaihara, T. (2011). Extracellular production and characterization of two Streptomyces L-asparaginases. Applied Biochemistry and Biotechnology, 163(7), 836¿844. Hunger, S. P., Lu, X., Devidas, M., Camitta, B. M., Gaynon, P. S., Winick, N. J., ¿ Carroll, W. L. (2012). Improved survival for children and adolescents with acute lymphoblastic leukemia between 1990 and 2005: a report from the children¿s oncology group. Journal of Clinical Oncology¿: Official Journal of the American Society of Clinical Oncology, 30(14), 1663¿9. http://doi.org/10.1200/JCO.2011.37.8018 Husain, I., Sharma, A., Kumar, S., & Malik, F. (2016). Purification and characterization of glutaminase free asparaginase from Pseudomonas otitidis: Induce apoptosis in human leukemia MOLT-4 cells. Biochimie, 121, 38¿51. http://doi.org/10.1016/j.biochi.2015.11.012 Kavitha, A., & Vijayalakshmi, M. (2010a). Optimization and Purifi cation of L -Asparaginase Produced by Streptomyces tendae TK-VL _ 333. Journal of Biosciences, 65, 528¿531. Kavitha, A., & Vijayalakshmi, M. (2010b). Optimization and purification of L-asparaginase produced by Streptomyces tendae TK-VL_333. Zeitschrift Fur Naturforschung - Section C Journal of Biosciences, 65 C(7¿8), 528¿531. |
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Amena, S; Vishalakshi, N; Prabhakar, M; Dayanand, A; Lingappa, K. (2010). Production, purification and characterization of l-asparaginase from. Brazilian Journal of Microbiology, 41, 173¿178. Arrivukkarasan, S., Muthusivaramapandian, M., Aravindan, R., & Viruthagiri, T. (2010). Effect of Medium Composition and Kinetic Studies on Extracellular and Intracellular Production of Lasparaginase from Pectobacterium carotovorum. Food Science and Technology International, 16(2), 115¿125. http://doi.org/10.1177/1082013209353219 Bapat, P. M., Sohoni, S. V., Moses, T. A., & Wangikar, P. P. (2006). A cybernetic model to predict the effect of freely available nitrogen substrate on rifamycin B production in complex media. Applied Microbiology and Biotechnology, 72(4), 662¿670. http://doi.org/10.1007/s00253-006-0341-6 Bazaraa, W., Alian, A., El-Shimi, N., & Mohamed, R. (2016). Purification and characterization of extracellular glutaminase from Aspergillus oryzae NRRL 32567. Biocatalysis and Agricultural Biotechnology, 6, 76¿81. http://doi.org/10.1016/j.bcab.2016.02.009 Bhunia, B., Basak, B., & Dey, A. (2012). A review on production of serine alkaline protease by Bacillus spp . J. Biochem Tech, 3(4), 448¿457 Boqué, R., & Maroto, A. (2004). El Análisis De La Varianza (Anova ). Universitat Rovira I Virgili., 1¿6. Bruns, R. E., Scarminio, I. S., & Neto, B. B. (2006). Statistical Design ¿ Chemometrics. El sevier Science Cavazzuti, M. (2013). Optimization Methods: From Theory to Design Scientific and Technological Aspects in Mechanics. http://doi.org/10.1007/978-3-642-31187-1 Chohan, S. M., & Rashid, N. (2013). TK1656, a thermostable lasparaginase from Thermococcus kodakaraensis, exhibiting highest ever reported enzyme activity. Journal of Bioscience and Bioengineering, 116(4), 438¿43. http://doi.org/10.1016/j.jbiosc.2013.04.005 Chow, Y., & Ting, A. S. Y. (2014). Endophytic l-asparaginase-producing fungi from plants associated with anticancer properties. Journal of Advanced Research. http://doi.org/10.1016/j.jare.2014.07.005 Crump, A. (2014). The advent of ivermectin: People, partnerships, and principles. Trends in Parasitology, 30(9), 423¿425. http://doi.org/10.1016/j.pt.2014.07.001 Derst, C., Henseling, J., & Röhm, K. H. (2000). Engineering the substrate specificity of Escherichia coli asparaginase. II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Science¿: A Publication of the Protein Society, 9(10), 2009¿17. http://doi.org/10.1110/ps.9.10.2009 Deshpande, N., Choubey, P., & Agashe, M. (2014). Studies on optimization of growth parameters for L-asparaginase production by streptomyces ginsengisoli. The Scientific World Journal, 2014, 1¿7. Dhevagi, P., & Poorani, E. (2006). Isolation and characterization of L - asparaginase from marine actinomycetes. Indian Journal of Biotechnology, 5(December 2003), 514¿520. Dias, F. F. G., & Sato, H. H. (2016). Sequential optimization strategy for maximum L-asparaginase production from Aspergillus oryzae CCT 3940. Biocatalysis and Agricultural Biotechnology, 6, 33¿39. http://doi.org/10.1016/j.bcab.2016.02.006 El-naggar, N. E., Deraz, S. F., Soliman, H. M., & El-deeb, N. M. (2016). Purification, characterization, cytotoxicity and anticancer activities of L-asparaginase , anti-colon cancer protein, from the newly isolated alkaliphilic Streptomyces fradiae NEAE-82. Scientific Reports, 1¿16. http://doi.org/10.1038/srep32926 El-naggar, N. E., Moawad, H., El-shweihy, N. M., & El-ewasy, S. M. (2015). Optimization of Culture Conditions for Production of the AntiLeukemic Glutaminase Free L-Asparaginase by Newly Isolated Streptomyces olivaceus NEAE-119 Using Response Surface Methodology. BioMed Research International, 2015. http://doi.org/10.1155/2015/627031 El-sayed, S. T., Fyiad, A. a, & Gamal-eldeen, A. M. (2012). Immobilization , Properties and Anti-tumor Activity of L-asparaginase of Vicia faba and Phaseoulus vulgaris Seeds. Australian Journal of Basic and Applied Sciences, 6(3), 785¿794. Farag, A. M., Hassan, S. W., Beltagy, E. A., & El-Shenawy, M. A. (2015). Optimization of production of anti-tumor l-asparaginase by free and immobilized marine Aspergillus terreus. Egyptian Journal of Aquatic Research, 41(4), 295¿302. http://doi.org/10.1016/j.ejar.2015.10.002 Fu, C. H., & Sakamoto, K. M. (2007). PEG-asparaginase. Expert Opinion on Pharmacotherapy, 8(12), 1977¿84. http://doi.org/10.1517/14656566.8.12.1977 García, H., & Vázquez, R. (1998). Cuantificación De Proteínas: Una Revisión. BioTecnologia (Vol. 3). Gonçalves Dias, F. F., Soares de Castro, R. J., Ohara, A., Nishide, T. G., Bagagl Pavan, M., & Sato, H. H. (2015). Simplex centroid mixture design to improve l-asparaginase production in solid-state fermentation using agroindustrial wastes. Biocatalysis and Agricultural Biotechnology, 4(4), 528¿534. http://doi.org/10.1016/j.bcab.2015.09.011 Gulati, R., Saxena, R. K., & Gupta, R. (1997). A rapid plate assay for screening L-asparaginase producing micro-organisms. Letters in Applied Microbiology, 24(1), 23¿26 Gunst, R. F. (1996). Response surface methodology: process and product optimization using designed experiments. Technometrics, 38(3), 284¿ 286. http://doi.org/10.2307/1270613 Hatanaka, T., Usuki, H., Arima, J., Uesugi, Y., Yamamoto, Y., Kumagai, Y., ¿ Mukaihara, T. (2011). Extracellular production and characterization of two Streptomyces L-asparaginases. Applied Biochemistry and Biotechnology, 163(7), 836¿844. Hunger, S. P., Lu, X., Devidas, M., Camitta, B. M., Gaynon, P. S., Winick, N. J., ¿ Carroll, W. L. (2012). Improved survival for children and adolescents with acute lymphoblastic leukemia between 1990 and 2005: a report from the children¿s oncology group. Journal of Clinical Oncology¿: Official Journal of the American Society of Clinical Oncology, 30(14), 1663¿9. http://doi.org/10.1200/JCO.2011.37.8018 Husain, I., Sharma, A., Kumar, S., & Malik, F. (2016). Purification and characterization of glutaminase free asparaginase from Pseudomonas otitidis: Induce apoptosis in human leukemia MOLT-4 cells. Biochimie, 121, 38¿51. http://doi.org/10.1016/j.biochi.2015.11.012 Kavitha, A., & Vijayalakshmi, M. (2010a). Optimization and Purifi cation of L -Asparaginase Produced by Streptomyces tendae TK-VL _ 333. Journal of Biosciences, 65, 528¿531. Kavitha, A., & Vijayalakshmi, M. (2010b). Optimization and purification of L-asparaginase produced by Streptomyces tendae TK-VL_333. Zeitschrift Fur Naturforschung - Section C Journal of Biosciences, 65 C(7¿8), 528¿531. 264047 TE09018 |
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Díaz Barrera, Luis EduardoCortázar Gómez, Jorge EduardoMorales González, María PaulaStepanian Martínez, Boghos SneiderIngeniero Químico2017-04-04T22:31:18Z2017-04-04T22:31:18Z20172017-04-04Amena, S; Vishalakshi, N; Prabhakar, M; Dayanand, A; Lingappa, K. (2010). Production, purification and characterization of l-asparaginase from. Brazilian Journal of Microbiology, 41, 173¿178.Amena, S; Vishalakshi, N; Prabhakar, M; Dayanand, A; Lingappa, K. (2010). Production, purification and characterization of l-asparaginase from. Brazilian Journal of Microbiology, 41, 173¿178.Arrivukkarasan, S., Muthusivaramapandian, M., Aravindan, R., & Viruthagiri, T. (2010). Effect of Medium Composition and Kinetic Studies on Extracellular and Intracellular Production of Lasparaginase from Pectobacterium carotovorum. Food Science and Technology International, 16(2), 115¿125. http://doi.org/10.1177/1082013209353219Bapat, P. M., Sohoni, S. V., Moses, T. A., & Wangikar, P. P. (2006). A cybernetic model to predict the effect of freely available nitrogen substrate on rifamycin B production in complex media. Applied Microbiology and Biotechnology, 72(4), 662¿670. http://doi.org/10.1007/s00253-006-0341-6Bazaraa, W., Alian, A., El-Shimi, N., & Mohamed, R. (2016). Purification and characterization of extracellular glutaminase from Aspergillus oryzae NRRL 32567. Biocatalysis and Agricultural Biotechnology, 6, 76¿81. http://doi.org/10.1016/j.bcab.2016.02.009Bhunia, B., Basak, B., & Dey, A. (2012). A review on production of serine alkaline protease by Bacillus spp . J. Biochem Tech, 3(4), 448¿457Boqué, R., & Maroto, A. (2004). El Análisis De La Varianza (Anova ). Universitat Rovira I Virgili., 1¿6.Bruns, R. E., Scarminio, I. S., & Neto, B. B. (2006). Statistical Design ¿ Chemometrics. El sevier ScienceCavazzuti, M. (2013). Optimization Methods: From Theory to Design Scientific and Technological Aspects in Mechanics. http://doi.org/10.1007/978-3-642-31187-1Chohan, S. M., & Rashid, N. (2013). TK1656, a thermostable lasparaginase from Thermococcus kodakaraensis, exhibiting highest ever reported enzyme activity. Journal of Bioscience and Bioengineering, 116(4), 438¿43. http://doi.org/10.1016/j.jbiosc.2013.04.005Chow, Y., & Ting, A. S. Y. (2014). Endophytic l-asparaginase-producing fungi from plants associated with anticancer properties. Journal of Advanced Research. http://doi.org/10.1016/j.jare.2014.07.005Crump, A. (2014). The advent of ivermectin: People, partnerships, and principles. Trends in Parasitology, 30(9), 423¿425. http://doi.org/10.1016/j.pt.2014.07.001Derst, C., Henseling, J., & Röhm, K. H. (2000). Engineering the substrate specificity of Escherichia coli asparaginase. II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Science¿: A Publication of the Protein Society, 9(10), 2009¿17. http://doi.org/10.1110/ps.9.10.2009Deshpande, N., Choubey, P., & Agashe, M. (2014). Studies on optimization of growth parameters for L-asparaginase production by streptomyces ginsengisoli. The Scientific World Journal, 2014, 1¿7.Dhevagi, P., & Poorani, E. (2006). Isolation and characterization of L - asparaginase from marine actinomycetes. Indian Journal of Biotechnology, 5(December 2003), 514¿520.Dias, F. F. G., & Sato, H. H. (2016). Sequential optimization strategy for maximum L-asparaginase production from Aspergillus oryzae CCT 3940. Biocatalysis and Agricultural Biotechnology, 6, 33¿39. http://doi.org/10.1016/j.bcab.2016.02.006El-naggar, N. E., Deraz, S. F., Soliman, H. M., & El-deeb, N. M. (2016). Purification, characterization, cytotoxicity and anticancer activities of L-asparaginase , anti-colon cancer protein, from the newly isolated alkaliphilic Streptomyces fradiae NEAE-82. Scientific Reports, 1¿16. http://doi.org/10.1038/srep32926El-naggar, N. E., Moawad, H., El-shweihy, N. M., & El-ewasy, S. M. (2015). 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Zeitschrift Fur Naturforschung - Section C Journal of Biosciences, 65 C(7¿8), 528¿531.https://hdl.handle.net/10818/30083264047TE0901877 Páginas.¿Uno de los principales tratamientos para el cáncer es la quimioterapia sistémica y se ha demostrado que la L-asparaginasa es potencialmente útil para combatir algunos tipos de cáncer. La L-asparaginasa ha sido muy efectiva en el tratamiento de leucemia linfocítica aguda (ALL por sus siglas en inglés). Las enzimas microbianas son preferibles sobre las enzimas de plantas o animales por su producción a nivel extracelular que facilita la purificación disminuyendo así los costos de dicha producción. Las Actinobacterias son ampliamente empleadas para la obtención de varios compuestos de aplicación farmacéutica, en especial Streptomyces spp. han demostrado que pueden producir L-asparaginasa. En este trabajo, se determinó la influencia de diferentes fuentes de carbono y de nitrógeno en la mejora de la actividad de L-asparaginasa de cinco cepas de Streptomyces. También se empleó una estrategia secuencial de mejora de algunos factores de fermentación para determinar el efecto de la concentración de la fuente de carbono y la fuente de nitrógeno, la temperatura de incubación y el pH del medio en la actividad de la Lasparaginasa de tres Streptomyces. Se determinó que la fuente de carbono y de nitrógeno que mejoraba la actividad de la cepa fueron lactosa y extracto de levadura y L-asparagina respectivamente.spaUniversidad de La SabanaIngeniero QuímicoFacultad de IngenieríaAttribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/http://purl.org/coar/access_right/c_16ecUniversidad de La SabanaIntellectum Repositorio Universidad de La SabanaEnzimas microbianasQuímica farmacéutica -- InvestigacionesAgentes antibacterialesCrecimiento bacterialModelamiento del efecto de algunos factores en la fermentación de Streptomyces spp. Aislados de las riberas del rio Guaviare sobre la producción de la enzima l-asparaginasa.Tesis/Trabajo de grado - Pregradohttp://purl.org/coar/resource_type/c_7a1fhttp://purl.org/coar/version/c_970fb48d4fbd8a85Textoinfo:eu-repo/semantics/bachelorThesishttp://purl.org/redcol/resource_type/TPPublicationORIGINALMaría Paula Morales González (Tesis).pdfMaría Paula Morales González (Tesis).pdfVer documento en PDFapplication/pdf5307727https://intellectum.unisabana.edu.co/bitstreams/7bdf9f62-c680-52b7-e053-7e0910accd73/downloadede908296d00e6c14bd9b415f71cf4d1MD51trueCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-81223https://intellectum.unisabana.edu.co/bitstreams/7bdf9f62-c681-52b7-e053-7e0910accd73/download7c9ab7f006165862d8ce9ac5eac01552MD52falseAdministratorREADAnonymousREADLICENSElicense.txtlicense.txttext/plain; charset=utf-8498https://intellectum.unisabana.edu.co/bitstreams/7bdf9f62-c55e-52b7-e053-7e0910accd73/downloadf52a2cfd4df262e08e9b300d62c85cabMD53falseAdministratorREADAnonymousREADMaría Paula Morales González (Carta).pdfMaría Paula Morales González (Carta).pdfapplication/pdf990116https://intellectum.unisabana.edu.co/bitstreams/7bdf9f62-c55f-52b7-e053-7e0910accd73/download8244d07cc629236ba925c59562304375MD54falseTEXTMaría Paula Morales González (Tesis).pdf.txtMaría Paula Morales González (Tesis).pdf.txtExtracted Texttext/plain139277https://intellectum.unisabana.edu.co/bitstreams/7bdf9f62-c688-52b7-e053-7e0910accd73/downloadb05f575f9ab1e8f5524b498a46966d40MD55falseTHUMBNAILMaría Paula Morales González (Tesis).pdf.jpgMaría Paula Morales González (Tesis).pdf.jpgGenerated Thumbnailimage/jpeg7035https://intellectum.unisabana.edu.co/bitstreams/c3b52dcd-0494-4def-9630-f68b2371e1e2/downloadff0c75a55cbe6622bd9f774114522658MD56false10818/30083oai:intellectum.unisabana.edu.co:10818/300832025-12-15 12:36:20.548http://creativecommons.org/licenses/by-nc-nd/4.0/Attribution-NonCommercial-NoDerivatives 4.0 Internationalrestrictedhttps://intellectum.unisabana.edu.coIntellectum Repositorio Universidad de La Sabanacontactointellectum@unisabana.edu.coPGEgcmVsPSJsaWNlbnNlIiBocmVmPSJodHRwOi8vY3JlYXRpdmVjb21tb25zLm9yZy9saWNlbnNlcy9ieS1uYy1uZC8zLjAvIj48aW1nIGFsdD0iTGljZW5jaWEgQ3JlYXRpdmUgQ29tbW9ucyIgc3R5bGU9ImJvcmRlci13aWR0aDowIiBzcmM9Imh0dHA6Ly9pLmNyZWF0aXZlY29tbW9ucy5vcmcvbC9ieS1uYy1uZC8zLjAvODh4MzEucG5nIiAvPjwvYT48YnIgLz5Fc3RlIDxzcGFuIHhtbG5zOmRjdD0iaHR0cDovL3B1cmwub3JnL2RjL3Rlcm1zLyIgaHJlZj0iaHR0cDovL3B1cmwub3JnL2RjL2RjbWl0eXBlL1RleHQiIHJlbD0iZGN0OnR5cGUiPm9icmE8L3NwYW4+IGVzdMOhIGJham8gdW5hIDxhIHJlbD0ibGljZW5zZSIgaHJlZj0iaHR0cDovL2NyZWF0aXZlY29tbW9ucy5vcmcvbGljZW5zZXMvYnktbmMtbmQvMy4wLyI+bGljZW5jaWEgQ3JlYXRpdmUgQ29tbW9ucyBSZWNvbm9jaW1pZW50by1Ob0NvbWVyY2lhbC1TaW5PYnJhRGVyaXZhZGEgMy4wIFVucG9ydGVkPC9hPi4K |
