Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes

Detalhes bibliográficos
Autor(a) principal: SANTOS, Wellington Leal dos
Data de Publicação: 2018
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Biblioteca Digital de Teses e Dissertações da UFRPE
Texto Completo: http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/7225
Resumo: Bioactive peptides, mainly derived from the enzymatic hydrolysis of milk casein, antioxidants, antihypertensives, antidiabetics, ability to isolate metals and antimicrobial capacity. The milk, in general, presents in its composition casein an important source of protein fragments with expressive biological activity. Thus, the objective was to investigate the biological potential of peptides derived from bovine casein, buffalo and caprine submitted to the proteolytic action of bromelain, papain, neutrase and trypsin in order to select the hydrolyzate with the highest antioxidant potential; fractionating the selected hydrolyzate and evaluating the antioxidant and antidiabetic potential of the fractions. It was possible to observe significant differences (p <0.05) between caseinates presenting a minimum degree of hydrolysis of 2% (bovine) and maximum of 85% (buffalo). In relation to the antioxidant activities, it was observed a distinct behavior of the caseinates against the different enzymatic treatments over 480 minutes. Hydrolysates presented a potential for sequestration of hydroxyl radicals (between 0 and 100%), superoxide (greater than 80%), ABTS (greater than 85%), DPPH (between 20 and 95%) and chelate iron (between 10 and 100%) and copper (between 14 and 80%); Regarding the antioxidant activities of the fractions from the selected species (buffalo), the hydroxyl and DPPH tests had a higher elimination potential in fractions of 3-10 kDa and <3 kDa, varying according to the enzymatic specificity, whereas the higher ABTS radical sequestration potential was observed in the fraction containing the total hydrolyzate. For the chelating activity of iron, it was observed more than 70% chelation in all the fractions, emphasizing the fractions <3 kDa. For copper chelation, values higher than 60% were observed in fractions >10 kDa. The anti-diabetic activity had a variable potential in relation to the α-glycosidase inhibition between the fractions, whereas α-amylase was better inhibited by the fraction <3 kDa. Antibacterial activity was observed between 3.28 and 100% inhibition against the microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential. The antihypertensive activity of the fractions remained between 39.35 and 89.58%, especially the peptide fraction H3. The proteases used in the hydrolysis of caseinates presented the potential to obtain hydrolysates with the three evaluated species of antioxidant protein fragments. In addition, they showed the capacity to produce fractions of hydrolysates with antioxidant potential, antidiabetic, antihypertensive and antimicrobial, therefore the ultrafiltration method proved effective in the fractionation of peptides with different molar masses. In this way, the total hydrolysates of the three species as well as the fractions of the selected species present potent antioxidant activity, which proves potential food application as a functional food, nutraceutical or as a natural food additive.
id URPE_d76073845b17e43385148161d3999fb3
oai_identifier_str oai:tede2:tede2/7225
network_acronym_str URPE
network_name_str Biblioteca Digital de Teses e Dissertações da UFRPE
repository_id_str
spelling MOREIRA, Keila AparecidaMOREIRA, Keila AparecidaRIBEIRO, Daniele SilvaSILVA, Lidiane Roberta Cruz dahttp://lattes.cnpq.br/6417801338031111SANTOS, Wellington Leal dos2018-05-07T14:01:15Z2018-02-27SANTOS, Wellington Leal dos. Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes. 2018. 102 f. Dissertação (Programa de Pós-Graduação em Biociência Animal) - Universidade Federal Rural de Pernambuco, Recife.http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/7225Bioactive peptides, mainly derived from the enzymatic hydrolysis of milk casein, antioxidants, antihypertensives, antidiabetics, ability to isolate metals and antimicrobial capacity. The milk, in general, presents in its composition casein an important source of protein fragments with expressive biological activity. Thus, the objective was to investigate the biological potential of peptides derived from bovine casein, buffalo and caprine submitted to the proteolytic action of bromelain, papain, neutrase and trypsin in order to select the hydrolyzate with the highest antioxidant potential; fractionating the selected hydrolyzate and evaluating the antioxidant and antidiabetic potential of the fractions. It was possible to observe significant differences (p <0.05) between caseinates presenting a minimum degree of hydrolysis of 2% (bovine) and maximum of 85% (buffalo). In relation to the antioxidant activities, it was observed a distinct behavior of the caseinates against the different enzymatic treatments over 480 minutes. Hydrolysates presented a potential for sequestration of hydroxyl radicals (between 0 and 100%), superoxide (greater than 80%), ABTS (greater than 85%), DPPH (between 20 and 95%) and chelate iron (between 10 and 100%) and copper (between 14 and 80%); Regarding the antioxidant activities of the fractions from the selected species (buffalo), the hydroxyl and DPPH tests had a higher elimination potential in fractions of 3-10 kDa and <3 kDa, varying according to the enzymatic specificity, whereas the higher ABTS radical sequestration potential was observed in the fraction containing the total hydrolyzate. For the chelating activity of iron, it was observed more than 70% chelation in all the fractions, emphasizing the fractions <3 kDa. For copper chelation, values higher than 60% were observed in fractions >10 kDa. The anti-diabetic activity had a variable potential in relation to the α-glycosidase inhibition between the fractions, whereas α-amylase was better inhibited by the fraction <3 kDa. Antibacterial activity was observed between 3.28 and 100% inhibition against the microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential. The antihypertensive activity of the fractions remained between 39.35 and 89.58%, especially the peptide fraction H3. The proteases used in the hydrolysis of caseinates presented the potential to obtain hydrolysates with the three evaluated species of antioxidant protein fragments. In addition, they showed the capacity to produce fractions of hydrolysates with antioxidant potential, antidiabetic, antihypertensive and antimicrobial, therefore the ultrafiltration method proved effective in the fractionation of peptides with different molar masses. In this way, the total hydrolysates of the three species as well as the fractions of the selected species present potent antioxidant activity, which proves potential food application as a functional food, nutraceutical or as a natural food additive.Os peptídeos bioativos, principalmente oriundos da hidrólise enzimática da caseína do leite, apresentam efeitos antioxidantes, anti-hipertensivos, antidiabéticos, capacidade de se ligar a metais e capacidade antimicrobiana. O leite, de modo geral apresenta em sua composição a caseína uma fonte importante de fragmentos proteicos com atividade biológica expressiva, sendo assim, objetivou-se investigar o potencial biológico de peptídeos derivados da caseína bovina, bubalina e caprina submetidos à ação proteolítica da bromelina, papaína, neutrase e tripsinaa a fim de selecionar o hidrolisado com maior potencial antioxidante; fracionar o hidrolisado selecionado e avaliar o potencial antioxidante e antidiabético das frações. Foi possível observar diferenças significativas (p<0,05) entre os caseinatos apresentando grau de hidrólise mínimo de 2% (bovino) e máximo de 85% (bubalino). Em relação as atividades antioxidantes observaram-se comportamento distintos dos caseinatos frente aos diferentes tratamentos enzimáticos ao longo de 480 minutos. Os hidrolisados apresentaram potencial para o sequestro dos radicais hidroxila (entre 0 e 100%), superóxido (superior a 80%), 2,2’- azinobis-3-etilbenzotiazolina-6-ácido sulfônico - ABTS (superior a 85%), 2,2-difenil-1-picrilidrasil - DPPH (entre 20 e 95%) e quelar ferro (entre 10 e 100%) e cobre (entre 14 e 80%). No que se referente as atividades antioxidantes dos fracionados provenientes da espécie selecionada (bubalina), os testes hidroxila e DPPH apresentaram maior potencial de eliminação nas frações de 3-10 kDa e <3 kDa, variando de acordo com a especificidade enzimática, enquanto que o maior potencial de sequestro do radical ABTS foi observado na fração contendo o hidrolisado total. Para a atividade quelante de ferro foi observado quelação superior a 70% em todas as frações destacando-se as frações < 3 kDa. Já para quelação de cobre foram observados valores superiores a 60% nas frações >10 kDa. A atividade antidiabética apresentou potencial variável em relação a inibição da α-glicosidase entre as frações, enquanto que a α-amilase foi melhor inibida pela fração <3 kDa. Observou-se atividade antibacteriana entre 3,28 e 100% de inibição contra os micro-organismos testados, a fração <3 kDa apresentou maior potencial inibitório. A atividade anti-hipertensiva das frações manteve-se entre 39,35 e 89,58%, destacando-se a fração peptídica H3. As proteases empregadas na hidrólise dos caseinatos apresentaram potencial para obtenção de hidrolisados com as três espécies avaliadas de fragmentos proteicos antioxidantes. Além disso, apresentaram a capacidade de produzir frações de hidrolisados com potencial antioxidante, antidiabético, anti-hipertensivo e antimicrobiano, portanto o método de ultrafiltração se mostrou eficaz no fracionamento de peptídeos com diferentes massas molares. Desta forma pode-se evidenciar que os hidrolisados totais das três espécies bem como as frações da espécie bubalina apresentam potente atividade antioxidante, o que indica potencial aplicação alimentar seja como alimento funcional, nutracêutico ou como aditivo alimentício natural.Submitted by Mario BC (mario@bc.ufrpe.br) on 2018-05-07T14:01:15Z No. of bitstreams: 1 Wellington Leal dos Santos.pdf: 1782649 bytes, checksum: a908ed132b6c98cca5dadf40a3923f48 (MD5)Made available in DSpace on 2018-05-07T14:01:15Z (GMT). No. of bitstreams: 1 Wellington Leal dos Santos.pdf: 1782649 bytes, checksum: a908ed132b6c98cca5dadf40a3923f48 (MD5) Previous issue date: 2018-02-27Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPESapplication/pdfporUniversidade Federal Rural de PernambucoPrograma de Pós-Graduação em Biociência AnimalUFRPEBrasilDepartamento de Morfologia e Fisiologia AnimalAtividade biológicaPeptídeoCaseína do leiteRuminanteHidrolisado proteicoCIENCIAS AGRARIAS::MEDICINA VETERINARIAProspecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesis-1510757014399315592600600600600-89223641879873962044536702642350173192075167498588264571info:eu-repo/semantics/openAccessreponame:Biblioteca Digital de Teses e Dissertações da UFRPEinstname:Universidade Federal Rural de Pernambuco (UFRPE)instacron:UFRPEORIGINALWellington Leal dos Santos.pdfWellington Leal dos Santos.pdfapplication/pdf1782649http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/7225/2/Wellington+Leal+dos+Santos.pdfa908ed132b6c98cca5dadf40a3923f48MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-82165http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/7225/1/license.txtbd3efa91386c1718a7f26a329fdcb468MD51tede2/72252023-06-13 16:54:24.31oai:tede2: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Biblioteca Digital de Teses e Dissertaçõeshttp://www.tede2.ufrpe.br:8080/tede/PUBhttp://www.tede2.ufrpe.br:8080/oai/requestbdtd@ufrpe.br ||bdtd@ufrpe.bropendoar:2023-06-13T19:54:24Biblioteca Digital de Teses e Dissertações da UFRPE - Universidade Federal Rural de Pernambuco (UFRPE)false
dc.title.por.fl_str_mv Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
title Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
spellingShingle Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
SANTOS, Wellington Leal dos
Atividade biológica
Peptídeo
Caseína do leite
Ruminante
Hidrolisado proteico
CIENCIAS AGRARIAS::MEDICINA VETERINARIA
title_short Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
title_full Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
title_fullStr Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
title_full_unstemmed Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
title_sort Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes
author SANTOS, Wellington Leal dos
author_facet SANTOS, Wellington Leal dos
author_role author
dc.contributor.advisor1.fl_str_mv MOREIRA, Keila Aparecida
dc.contributor.referee1.fl_str_mv MOREIRA, Keila Aparecida
dc.contributor.referee2.fl_str_mv RIBEIRO, Daniele Silva
dc.contributor.referee3.fl_str_mv SILVA, Lidiane Roberta Cruz da
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/6417801338031111
dc.contributor.author.fl_str_mv SANTOS, Wellington Leal dos
contributor_str_mv MOREIRA, Keila Aparecida
MOREIRA, Keila Aparecida
RIBEIRO, Daniele Silva
SILVA, Lidiane Roberta Cruz da
dc.subject.por.fl_str_mv Atividade biológica
Peptídeo
Caseína do leite
Ruminante
Hidrolisado proteico
topic Atividade biológica
Peptídeo
Caseína do leite
Ruminante
Hidrolisado proteico
CIENCIAS AGRARIAS::MEDICINA VETERINARIA
dc.subject.cnpq.fl_str_mv CIENCIAS AGRARIAS::MEDICINA VETERINARIA
description Bioactive peptides, mainly derived from the enzymatic hydrolysis of milk casein, antioxidants, antihypertensives, antidiabetics, ability to isolate metals and antimicrobial capacity. The milk, in general, presents in its composition casein an important source of protein fragments with expressive biological activity. Thus, the objective was to investigate the biological potential of peptides derived from bovine casein, buffalo and caprine submitted to the proteolytic action of bromelain, papain, neutrase and trypsin in order to select the hydrolyzate with the highest antioxidant potential; fractionating the selected hydrolyzate and evaluating the antioxidant and antidiabetic potential of the fractions. It was possible to observe significant differences (p <0.05) between caseinates presenting a minimum degree of hydrolysis of 2% (bovine) and maximum of 85% (buffalo). In relation to the antioxidant activities, it was observed a distinct behavior of the caseinates against the different enzymatic treatments over 480 minutes. Hydrolysates presented a potential for sequestration of hydroxyl radicals (between 0 and 100%), superoxide (greater than 80%), ABTS (greater than 85%), DPPH (between 20 and 95%) and chelate iron (between 10 and 100%) and copper (between 14 and 80%); Regarding the antioxidant activities of the fractions from the selected species (buffalo), the hydroxyl and DPPH tests had a higher elimination potential in fractions of 3-10 kDa and <3 kDa, varying according to the enzymatic specificity, whereas the higher ABTS radical sequestration potential was observed in the fraction containing the total hydrolyzate. For the chelating activity of iron, it was observed more than 70% chelation in all the fractions, emphasizing the fractions <3 kDa. For copper chelation, values higher than 60% were observed in fractions >10 kDa. The anti-diabetic activity had a variable potential in relation to the α-glycosidase inhibition between the fractions, whereas α-amylase was better inhibited by the fraction <3 kDa. Antibacterial activity was observed between 3.28 and 100% inhibition against the microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential. The antihypertensive activity of the fractions remained between 39.35 and 89.58%, especially the peptide fraction H3. The proteases used in the hydrolysis of caseinates presented the potential to obtain hydrolysates with the three evaluated species of antioxidant protein fragments. In addition, they showed the capacity to produce fractions of hydrolysates with antioxidant potential, antidiabetic, antihypertensive and antimicrobial, therefore the ultrafiltration method proved effective in the fractionation of peptides with different molar masses. In this way, the total hydrolysates of the three species as well as the fractions of the selected species present potent antioxidant activity, which proves potential food application as a functional food, nutraceutical or as a natural food additive.
publishDate 2018
dc.date.accessioned.fl_str_mv 2018-05-07T14:01:15Z
dc.date.issued.fl_str_mv 2018-02-27
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.citation.fl_str_mv SANTOS, Wellington Leal dos. Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes. 2018. 102 f. Dissertação (Programa de Pós-Graduação em Biociência Animal) - Universidade Federal Rural de Pernambuco, Recife.
dc.identifier.uri.fl_str_mv http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/7225
identifier_str_mv SANTOS, Wellington Leal dos. Prospecção e avaliação das atividades biológicas dos peptídeos obtidos a partir da proteólise do caseinato de ruminantes. 2018. 102 f. Dissertação (Programa de Pós-Graduação em Biociência Animal) - Universidade Federal Rural de Pernambuco, Recife.
url http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/7225
dc.language.iso.fl_str_mv por
language por
dc.relation.program.fl_str_mv -1510757014399315592
dc.relation.confidence.fl_str_mv 600
600
600
600
dc.relation.department.fl_str_mv -8922364187987396204
dc.relation.cnpq.fl_str_mv 453670264235017319
dc.relation.sponsorship.fl_str_mv 2075167498588264571
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Federal Rural de Pernambuco
dc.publisher.program.fl_str_mv Programa de Pós-Graduação em Biociência Animal
dc.publisher.initials.fl_str_mv UFRPE
dc.publisher.country.fl_str_mv Brasil
dc.publisher.department.fl_str_mv Departamento de Morfologia e Fisiologia Animal
publisher.none.fl_str_mv Universidade Federal Rural de Pernambuco
dc.source.none.fl_str_mv reponame:Biblioteca Digital de Teses e Dissertações da UFRPE
instname:Universidade Federal Rural de Pernambuco (UFRPE)
instacron:UFRPE
instname_str Universidade Federal Rural de Pernambuco (UFRPE)
instacron_str UFRPE
institution UFRPE
reponame_str Biblioteca Digital de Teses e Dissertações da UFRPE
collection Biblioteca Digital de Teses e Dissertações da UFRPE
bitstream.url.fl_str_mv http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/7225/2/Wellington+Leal+dos+Santos.pdf
http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/7225/1/license.txt
bitstream.checksum.fl_str_mv a908ed132b6c98cca5dadf40a3923f48
bd3efa91386c1718a7f26a329fdcb468
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
repository.name.fl_str_mv Biblioteca Digital de Teses e Dissertações da UFRPE - Universidade Federal Rural de Pernambuco (UFRPE)
repository.mail.fl_str_mv bdtd@ufrpe.br ||bdtd@ufrpe.br
_version_ 1800311480768266240