logo RIMA
logo UFRRJ

  1. Repositório de Múltiplos Acervos da UFRRJ
  2. Teses e Dissertações
  3. Programa de Pós-Graduação em Química
  4. Mestrado em Química
Please use this identifier to cite or link to this item: https://rima.ufrrj.br/jspui/handle/20.500.14407/14625
Full metadata record
DC FieldValueLanguage
dc.contributor.authorCruz, Wellington Oliveira da
dc.date.accessioned2023-12-22T03:03:42Z-
dc.date.available2023-12-22T03:03:42Z-
dc.date.issued2011-09-16
dc.identifier.citationCRUZ, Wellington Oliveira da. Caracterização de α-amilase de Alphitobius diaperinus (Coleoptera, Tenebrionidae): efeito de diferentes rações de aves e dos inibidores de Phaseolus vulgaris. 2011. 50 f. Dissertação (Mestrado em Química) - Instituto de Ciências Exatas, Universidade Federal Rural do Rio de Janeiro, Seropédica, 2011.por
dc.identifier.urihttps://rima.ufrrj.br/jspui/handle/20.500.14407/14625-
dc.description.abstractCRUZ, Wellington Oliveira. Caracterização de ɑ-amilase de Alphitobius diaperinus (Coleoptera, Tenebrionidae): Efeito de Diferentes Rações de Aves e dos Inibidores de Phaseolus Vulgaris. 2011. 50 p Dissertação (Mestrado em Química, Área de Concentração Bioquímica). Instituto de Ciências Exatas, Departamento de Química, Universidade Federal Rural do Rio de Janeiro, Seropédica, RJ, 2011. Alphitobius diaperinus, conhecido como cascudinho de cama aviária, é uma das principais pragas avícolas. Ele utiliza o substrato das aves rico em proteínas e carboidratos como fonte de alimento, colonizando toda a área de produção, encontrando um ambiente favorável para sua proliferação. Este inseto causa problemas sanitários e econômicos, afetando a saúde e o crescimento das aves e atuando também como transmissor de microrganismos tais como baactérias, protozoários e vírus. Neste trabalho foi identificada a presença de uma α-amilase no extrato bruto de larvas e adultos de Alphitobius diaperinus. Esta enzima digestiva é responsável pela degradação de amido utilizado como combustível na obtenção de energia, sendo extremamente importante para sobrevivência de muitos insetos. A α-amilase foi parcialmente purificada por precipitação em sulfato de amônio (25-75 %) em coluna cromatográfica Sephadex G (50-80), revelando em gel de poliacrilamida uma única banda com peso molecular de aproximadamente 30 KDa. Sua pureza enzimática foi confirmada através de ensaio de atividade pelo método 3,5-dinitrosalicílico alcalino (DNS), observando-se um aumento de 7.2 vezes em relação ao extrato bruto. A α-amilase ensaiada apresentou uma atividade máxima em pH 5.0 e pH 5.6 e uma temperatura de atividade ótima de 50ºC. A atividade máxima da α-amilase de A. diaperinus foi alcançada na presença de 0.02 mM de CaCl2, e inibida com o aumento da concentração deste reagente. A atividade enzimática da α-amilase de A. diaperinus, foi significativamente inibida pelo inibidor α-AIs, (inibidores tipo lectina) de Phaseolus vulgaris, sugerindo que estes podem ser utilizados como importantes ferramentas biológicas no controle e desenvolvimento de A. diaperinus através da redução da atividade digestiva destas pragas devido a atuação desses inibidores sobre a ação catalisadora de amilases, enzimas fundamentais para a digestão de amidopor
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior, CAPES.por
dc.formatapplication/pdf*
dc.languageporpor
dc.publisherUniversidade Federal Rural do Rio de Janeiropor
dc.rightsAcesso Abertopor
dc.subjectAlphitobius diaperinuspor
dc.subjectα-amylase. Inhibitor α-AIs.por
dc.subjectα-amilasepor
dc.subjectInibidor α-AIspor
dc.titleCaracterização de α-amilase de Alphitobius diaperinus (Coleoptera, Tenebrionidae): efeito de diferentes rações de aves e dos inibidores de Phaseolus vulgarispor
dc.typeDissertaçãopor
dc.description.abstractOtherCRUZ, Wellington Oliveira. Characterization of Alphitobius diaperinus (Coleoptera, Tenebrionidae) ɑ-amylase: Effect of Different Birds Diet and Inhibitors from Phaseolus vulgaris. 2011. 50 p Dissertação (Mestrado em Química, Área de Concentração Bioquímica). Instituto de Ciências Exatas, Departamento de Química, Universidade Federal Rural do Rio de Janeiro, Seropédica, RJ, 2011. Alphitobius diaperinus known as mealworm of poultry litter, is one of the main poultry pests. It uses high protein and carbohydrates substrate of birds as a food source, colonizing all the production area finding a favorable environment for its proliferation. This insect causes sanitary and economic problems, affecting not only healthy and growth of the poultry but also acting as a microorganisms transmitter like bacterias, protozoas and virus. In this work it was identified an α-amylase activity in crude extracts of A. diaperinus larvae and adults. This enzyme is responsible for starch degradation used as a energy source extremely important for survival of many insects. The α-amylase was partially purified by ammonium sulfate precipitation (25-75%) in a chromatographic Sephadex column G (50-80), polyacrylamide gel revealed only one band with molecular weight of approximately 30 kDa, its purity was confirmed by the method of enzyme activity assay dinitrosalicylic 3.5-alkaline (DNS) was increased 7.2 times when compared with the crude extract. The α-amylase assays presented a maximum activity at a pH 5.0 and pH 5.6 and an optimal activity temperature of 50 ° C. The maximum activity of α-amylase A. diaperinus was achieved in the presence of 0.02 mM CaCl2, and inhibited by increasing this reaction concentration. The enzymatic activity of A. diaperinus α-amylase was significantly inhibited by amylase inhibitor α-AIs (lectin-like inhibitor) of Phaseolus vulgaris, suggesting that this inhibitors can be used as an important tool in biological control and development of these pests by reducing the digestion reducing amylase activity which plays an important role in the starch digestionpor
dc.contributor.advisor1Pontes, Emerson Guedes
dc.contributor.advisor1ID4553410796por
dc.contributor.advisor1Latteshttp://lattes.cnpq.br/1562085358907265por
dc.creator.ID7573604750por
dc.creator.Latteshttp://lattes.cnpq.br/5335761763028967por
dc.publisher.countryBrasilpor
dc.publisher.departmentInstituto de Ciências Exataspor
dc.publisher.initialsUFRRJpor
dc.publisher.programPrograma de Pós-Graduação em Químicapor
dc.relation.referencesARENDS, J.J. Control, management of the litter beetle. Poultry Digest, v.44, p.172-176, (1987). ALKAZAZ, M.; DESSEAUX, V.; MARCHIS-MOUREN, G.;PAYAN, F.; FOREST, E.; SANTIMONE, M. The mechanism of porcine pancreatic alpha-amylase. Kinetic evidence for two additional carbohydrate-binding sites. European Journal Biochemistry, 241, 787-796, (1996). AXTELL, R. C. Department of Entomology, orth Carolina State University, Raleigh, NC 2., p. 7695-7613, (1999). BAKER, J. E. Properties of amylases from midguts of larvae of Sitophilus zeamais and Sitophilus granaries. Insect Biochemistry, 13: p.421-428, (1983). BERNFELD, P. Amylase α and β. Methods in Enzymology 1 p.149–158, (1955). BOOTH, R. G.; COX , M. L.; MADGE , R. B. II Guides to insects of importance to man. 3. Coleoptcra. Londres, International journal Entomology: 384p, (1990). BOŽIĆ, N.; VUJČIĆ, Z.; NENADOVIĆ, V.; IVANOVIĆ, J. Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera: Cerambycidae) larvae. Comparative Biochemistry and Physiology: 134B, p. 231– 234, (2003). BUONOCORE, V.; POERIO, E.; PACE, W.; PETRUCCI, T.; SILANO, V.; TOMASI, M. Interaction of Tenebrio molitor L. ɑ-amylase with wheat our protein inhibitor. FEBS Letters: 67, p. 202 - 206, (1976). C. BOMPARD-GILLES.; P. ROUSSEAU.; P. ROUGE.; F. PAYAN. Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme– inhibitor complex, Structure: v.4, p.1441– 1452, (1996). CAMPOS, F.A.P.; XAVIER-FILHO, J.; SILVA, C. P.; ARY, M. B. Resolution and partial characterization of proteinases and α-amylases from midguts of larvae of the Bruchid beetle Callosobruchos maculatus. Comparative Biochemistry and Physiology: 92B, p. 51-57, (1989). CHERNAKI, A. M.; ALMEIDA, L. M. Morfologia dos estágios imaturos e do adulto de Alphitobius diaperinus (Panzer) (Coleoptera, Tenebrionidae). Revista brasileira de Zoologia: V.18 (2): p. 351 – 363, (2001). CHERNAKI, A. M.; ALMEIDA, L. M. Exigências Térmicas, Período de Desenvolvimento e Sobrevivência de Imaturos de Alphitobius diaperinus (Panzer) (Coleoptera: Tenebrionidae). eotropical Entomology: 30 (3) p.365-368, (2001). 46 CHERNAKI-LEFFER, A.M.; LAZZARI, F. A.; LAZZARI, S. M. N.; ALMEIDA, L. M. Controle do cascudinho. Avicultura Industrial: 1094: p. 22-25, (2001). CHIPOULET, J.M.; CHARARAS, C. Survey and Electrophoretical Separation of the Glycosidases of Rhagium inquisitor (Coleoptera: Cerambycidae) larvae. Comparative Biochemistry and Physiology: 80B: p. 241–246, (1985). CRISTOFOLETTI, P.T.; RIBEIRO, A.F.; TERRA, W. R. Apocrine secretion of amylase and exocytosis of trypsin along the midgut of Tenebrio molitor larvae. Journal of Insect Physiology: 47: p. 143-155, (2001). DE LAS CASAS, E.; POMEROY, B. S.; HAREIN, P. K. Infection and quantitative recovery of Salmonella Typhimurium and Escherichia Coli from within the lesser mealworm, Alphitobius Diaperinus (Panzer). Poultry Science: 47(6): p. 1871-5, (1968). DOJNOV, B. Purification and properties of midgut α-amilase isolated form from Morimus funereus larvae. Comparative Biochemistry and Physiology, 149, p.153- 160, (2008). DUNFORD, J. C.; KAUFMAN, P. E. Lesser Mealworm, Litter Beetle, Alphitobius diaperinus (Panzer) (Insecta: Coleoptera): Service, Institute of Food and Agricultural Sciences: University of Florida. Published March, Revised: June (2006). EIDSON, C.S.; SCHMITTLE, S. C.; LAL, J. B.; GOODE, R. B. The role of darkling beetle (Alphitobius diaperinus) in the transmission of acute leukosis in chickens. Poultry Science : 44: p. 1366-1367, (1965). F.M. LAJOLO.; F. FINARDO FILHO. Partial characterization of the amylase inhibitor of black beans (Phaseolus vulgaris), variety Rico 23, Journal of Agricutural Food Chemistry: 33, p.132–138, (1985). FALOMO, A. The Pheromone Biology of the Lesser Mealworm Alphitobius diaperinus (Panzer), (Coleoptera: Tenebrionidae). Thesis, University of Wisconsin-Madison: (1986). FENG, G. H.; RICHARDSON, M.; CHEN, M. S.; KRAMER, K. J.; MORGAN, T. D.; AND REECK, G. R. α-amylase inhibitors from wheat: sequences and patterns of inhibition of insects and human α-amylases. Insect Biochemistry: Mol. Biol.26 (5): p. 419–426, (1996). FINARDI-FILHO, E.; MIRKOV, M. J.; CHRISPEELS, A. Putative precursor protein in the evolution of the bean α-amylase inhibitor. Phitochemistry: 43, p. 57-62, (1996). FRANCO, O. L.; RIGDEN, D. J.; MELO, F. R.; BLOCH J. R. C.; SILVA, C. P.; GROSSI DE SÁ, M. F. Activity of wheat α- amylase inhibitors towards bruchid α- amylases and structural explanation of observed specificities. European Journal Biochemistry: 267 (8), p. 1466-1473, (2000). 47 FRANCO, O. L.; RIGDEN, D. J.; MELO, F. R.; GROSSI DE SÁ, M. F. Plant α- amylase inhibitors and their interaction with insect α-amylases, European Journal Biochemistry: 269, p. 397–412, (2002). FRANCO. O. L.; MELO, F. R.; MENDES, P. A.; PAES, N. S.; YOKOYAMA, M.; COUTINHO, M. V.; BLOCH JR, C.; GROSSI DE SÁ. Characterization of two Acanthoscelides obtectus α-amylases and their inactivation by wheat inhibitors, J. Journal of Agricutural Food Chemistry: 53, p. 1585–1590, (2005). FRELS, J. M.; RUPNOW, J. H. Purification and partial characterization of two α- amylase inhibitors from black bean (Phaseolus Vulgaris). Jounal of Agricutural Food Chemistry: 8, p. 281-301,(1984). GIRI, P. A.; KACHOLE, S. M. Detection of electrophoretically separated amylase inhibitors in starch – polyacrylamide gels. Journal of Chromatography A: 752, p. 261-264, (1996). GOODWIN, M. A.; WALTMAN, W. D. Transmission of Eimeria, viruses and bacteria to chicks: darkling beetles Alphitobius diaperinus as vector of pathogens. Journal of Applied Poultry Research: 5, p. 51-55, (1996). GROSSI DE SÁ, M. F.; MIRKOV, T. E.; ISHIMOTO, M.; COLUCCI, G.; BATEMAN, K. S.; CHRISPEELS, M. J. Molecular characterization of a bean α- amylase inhibitor that inhibits the α-amylase of the Mexican bean weevil Zabrotes subfasciatus. Planta: 203, p. 295–303, (1997). HO, M. F.; WHITAKER, J. R. Purification and partial characterization of white kidney beans (Phaseolus Vulgaris) α-amylase inhibitors from two experimental cultivars. Journal Food Biochemistry: 17, p. 15 – 33, (1993). HO, M. F.; YIN, X.; FILHO, F. F.; LAJOLO, F.; WHITAKER, J. R. Naturally occurring α-amylase inhibitors: Structure/function relationships. In Protein Structure- Function Relationships in Foods; Yada, R. Y.; Jackman, R. L.; Smith, J. L.; Eds.; Bishopbriggs, Blackie, Academic and Professional: Glasgow, Scotland, pp 89-119, (1994). HONAVAR, P. M.; SHIH, C. V.; LIENER, I. E. Inhibition of the Growth of Rats by Purified Hemaglutinin Fractions Isolated from Phaseolus vulgaris. Department of Agricultural Biochemistry, University of Minnesota,St. Paul, Minnesota, Journal utrition: 77, p. 109-114, (1962). ISHIMOTO, M.; CHRISPEELS, M. J. Protective mechanisms of the Mexican bean weevil against high levels of α-amylase inhibitor in the common bean, Phaseolus vulgaris. Plant Physiology: 111, p. 393-401, (1996). JANECEK, S. Structural Features and Evolutionary Relationships in the α-Amylase Family. In: Glycoenzymes (Eds. M. Ohnishi, T. Hayashi, S. Ishijima, T. Kuriki), pp. 19-54, Japan Scientific Societies Press: Tokyo, (2000). 48 KASAHARA, K.; HAYASHI, K.; ARAKAWA, T.; PHILO, J. S.; WEN, J.; HARA, S.; YAMAGUCHI, H. Complete sequence, subunit structure, and complexes with pancreatic α-amylase of an α-amylase inhibitor from Phaseolus vulgaris white kidney beans, Journal Biochemistry: 120, p. 177–183, (1996). KRAULIS, P .J. Molscript: a program to produce both detailed and schematic plots of protein structures. Journal of Applied Crystallography: 24, p. 946 – 950, (1991). LAEMMLI, U. K.; Cleavage of structural proteins during the assembly of the bacteriophage T4. ature: 227, p. 680–685, (1970). LEMOS, F. J. A.; CAMPOS, F. A. P.; SILVA, C. P.; XAVIER-FILHO, J. Proteinases and amylases of larval midgut of Zabrotes subfasciatus reared on cowpea (Vigna unguiculata) seeds. Entomologia Experimentalis et Applicata: 56, 219–227, (1990). LESCHEN, R. A. B.; STEELMAN, C. D. Alphitobius diaperinus (Coleoptera: Tenebrionidae) larve and adult mouthparts. Entomological ews: v. 99, n. 4, p. 221- 224, (1988). LOMBRAÑA, M.; SUÁREZ, P.; SAN JUAN, F. Two forms of α-amylase in mantle tissue of Mytilus galloprovincialis: purification and molecular properties of form II. Comparative Biochemistry Physiology: 142B, 56–66, (2005). LOMÔNACO, C.; PRADO, A. P. Estrutura comunitária e dinâmica populacional da fauna de dípteros e seus inimigos naturais em granjas avícolas. Anais da Sociedade Entomológica do Brasil: 23 (I), p 71-80, (1994). LOWRY O. H.; ROSEBROUGH N. J.; FARR A. L.; RANDALL R. J. Protein measurement with the Folin phenol reagent - Journal Biological Chemistry: 265-275, (1951). MARSHALL, J. J.; LAUDA, C. M. Purification and properties of phaseolamin, an inhibitor of α-amylase, from the kidney bean, Phaseolus vulgaris. Journal Biological Chemistry: 250, p. 8030-8037, (1975). MORENO, J.; CHRISPEELS, M. J. A lectin gene encodes the α-amylase inhibitor of the common bean. Proceedings of the ational Academy of Sciences: USA 86, p. 7885-7889, (1989). NODAN, R O.; TSAI, S. M.; GILBERTEON, R. L.; GEPTS, P. Towards an integrated linkage map of common bean 2. Development of an RFLP-based linkage map. Theor. Appl. Genet: 85, p. 513-520, (1993). PAYAN, F. Structural basis for the inhibition of mammalian and insect α-amylases by plant protein inhibitors, Biochimica et Biophysica Acta: 1696, p. 171-180, (2004). PODOLER, H.; APPLEBAUM, S.W.; The α-amylase of the beetle Callosobruchus chinensis. Biochemistry Faculty of Agriculture: The Hebrew University, Rehovot, Israel, 121, p. 321–325, (1971). 49 PREISS, F. J.; DAVIDSON, J. A. Characters for Separating Late-Stage Larvae, Pupae, and Adults of Alphitobius diaperinus and A. laevigatus (Coleoptera: Tenebrionidae) Source: Annals of the Entomological Society of America: Volume 63, Number 3, 15, pp. 807-808, May (1970). PUEYO, J. J.; HUNT, D. C.; CHRISPEELS, M. J. Activation of bean (Phaseolus vulgaris) α-amylase inhibitor requires proteolytic processing of the pro-protein. Plant Physiology: 101, p. 1341-1348, (1993). RICHARDSON, M. Seed storage protein: the enzyme inhibitor, In: Methods in Plant Biochemistr: New York: Acad Press, v. 5 p. 295 – 305, (1991). ROUGE, P.; BARRE, A.; CAUSSE, H.; CHATELAIN, C.; PORTHE, G. Arcelin and α-amylase inhibitor from the seeds of common bean (Phaseolus Vulgaris ) are truncated lectins. Biochemical Systematics and Ecology: 21, p. 695-703, (1993). SARIN, K. Digestive enzymes in immature and adult stages of Alphitobius diaperinus. Entomological society of Japan: 41, p. 10-17, (1973). SILVA C. P.; TERRA W. R.; XAVIER-FILHO, J.; GROSSI DE SÁ, M. F.; LOPES, A. R.; PONTES, E. G. Digestion in larvae of Callosobruchus maculatus and Zabrotes subfasciatus (Coleoptera: Bruchidae) with emphasis on α-amylases and oligosaccharidases. Insect Biochemistry and Molecular Biology: 29, p. 355–366, (1999). SILVA D. P.; CASADO-FILHO, E. L.; CORREA, A. S.; FARIAS L. R.; BLOCH J. R. C.; GROSSI-DE-SÁ M. F.; MENDES P. A.; QUIRNO B. F.; NORONHA E. F.; FRANCO O. L.; Identification of an α-amylase inhibitor from Pterodon pubescens with ability to inhibit cowpea weevil digestive enzymes, Journal Agricultural Food Chemistry: 55,4382–4387, 2007. SILVA, C. P.; TERRA, W. R.; XAVIER-FILHO, J.; GROSSI-DE-SÁ, M. F.; ISEJIMA, E. M.; DAMATTA, R. A.; MIGUENS, F. C.; BIFANO, T. D.; Digestion of legume starch granules by larvae of Zabrotes subfasciatus (Coleoptera: Bruchidae) and the induction of α- mylases in response to different diets. Insect Biochemistry and Insect Molecular Biology: 31, p. 41–50, (2001). SIVAKUMAR, S.; MOHAN, M.; FRANCO, O. L.; THAYUMANAVAN, B. Inhibition of insect pest α-amilase by little and finger millet inhibitors. Pesticide Biochemistry and Physiology: v. 85, n. 3, p. 155-160,(2006). SNEDEKER, C. F. K.; MOULTHROP, I. M. Some studies on the infectious bursal agent. Avian diseases: n. 11, p.519-528, (1967). STROBL, S.; MASKOS, K.; BETZ, M.; WIEGAND, G.; HUBER, R.; GOMIS-RUÈ TH, F. X.; GLOCKSHUBER, R. Crystal structure of yellow mealworm α-amylase at 1.64 A Ê resolution. Journal of Molecular Biology: 278, p. 617-628, (1998). 50 TERRA, W. R.; FERREIRA, C. Insect digestive enzyme: properties, compartmentalization and function. Comparative Biochemistry and Physiology: Part B 109: p. 1-62, (1994). TERRA, W. R.; FERREIRA, C.; JORDÃO, B. P.; DILLON, R. J. Digestive enzymes. In: Biology of the Insect Midgut. Edited by Lehane, M. J.; Billingsley, P. F. Chapman and Hall: London, pp. 153–194, (1996). VALLEE, B. L.; STEIN, E. A.; SUMERWELL, W. N.; FISCHER, E. H. Metal content of α-amylase of various origins. Journal Biological Chemistry: 234, p. 2901–2905, (1959). VIOLET, M.; MEUNIER, J. C. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase. Biochemical journal: v. 263, p. 665-670, (1989). WILSON, T. H.; MINNER, F. D. Influence of temperature on development of the lesser mealworm Alphitobius diaperinus. Journal of Kansas Entomology Society: 42, p. 294-303, (1968). YOUNG, N. M.; THIBAULT, P.; WATSON, D. C; CHRISPEELS, M. J. Posttranslational processing of two α-amylase inhibitors and an arcelin from the common bean, Phaseolus vulgaris. FEBS Letters: 446, p. 203-206, (1999). ZIEGLER, P. Partial purification and characterization of the major endo amylase of mature pea leaves. Plant Physiology: 86, p. 659–666, (1988).por
dc.subject.cnpqQuímicapor
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/4585/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/19214/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/25512/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/31919/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/38320/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/44706/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/51094/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.thumbnail.urlhttps://tede.ufrrj.br/retrieve/57568/2011%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpg*
dc.originais.urihttps://tede.ufrrj.br/jspui/handle/jspui/1145
dc.originais.provenanceSubmitted by Sandra Pereira (srpereira@ufrrj.br) on 2016-08-02T11:48:25Z No. of bitstreams: 1 2011 - Wellington Oliveira da Cruz.pdf: 7968929 bytes, checksum: 9dd68ee567386fa437d5f3438c9db428 (MD5)eng
dc.originais.provenanceMade available in DSpace on 2016-08-02T11:48:25Z (GMT). No. of bitstreams: 1 2011 - Wellington Oliveira da Cruz.pdf: 7968929 bytes, checksum: 9dd68ee567386fa437d5f3438c9db428 (MD5) Previous issue date: 2011-09-16eng
Appears in Collections:Mestrado em Química

Se for cadastrado no RIMA, poderá receber informações por email.
Se ainda não tem uma conta, cadastre-se aqui!

Files in This Item:
File Description SizeFormat 
2011 - Wellington Oliveira da Cruz.pdf2011 - Wellington Oliveira da Cruz7.78 MBAdobe PDFThumbnail
View/Open
Show simple item record


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.