Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica
Autor(a) principal: | |
---|---|
Data de Publicação: | 2022 |
Tipo de documento: | Tese |
Idioma: | por |
Título da fonte: | Biblioteca Digital de Teses e Dissertações da UFRPE |
Texto Completo: | http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/9692 |
Resumo: | By-products from the fishing industry are rich in biological compounds, such as proteases, and their recovery has technical advantages over chemical ones and has wide industrial applications, mainly in medicines, cosmetics, food, textiles and animal feed, due to its property of high activity over a wide pH range and at different temperatures. Several techniques for recovery, identification and purification of enzymes capable of cleaving the peptide bonds of collagen molecules and subsequently degrading them into small peptides from these residues have been used, such as the semipurification technique by aqueous two-phase system (SDFA) which was applied to neglected mullet (Mugil liza) waste (viscera) for the treatment of enzymes with collagenolytic activity. The crude extract (EB) obtained from the intestinal viscera of Mullet (Mugil liza) showed the following activities: total protein 1.02 U/mg; collagenolytic activity: 152.0 U/mg volumetric; 161 U/mg specific collagenolytic activity; 7.35 U/mL of proteolytic/proteasic activity; and, finally, 14.2 mg/mL of specific proteolytic activity. In the two-phase PEG/citrate aqueous system, according to the 2³ factorial design, using the variables Partition coefficient (K), Yield (Y), and Purification factor (FP), it was possible to observe that the extraction yields (Y ) obtained ranged from 89 to 124.34% and from 242.11 to 435.61% for protease and proteases with collagenolytic activity, respectively. The results showed the advantage of this semi-purification technique regarding the extraction and purification of collagenolytic enzymes with industrial application. The fish collagen peptides, highlighted in the integrative review, are important in the global collagen peptides market and are important in the development of biomaterials that constitute pharmaceutical, cosmetic and food products. , properties, preparation methods, and applications in different industries. It specifically encompasses collagen peptides applied in the pharmaceutical, cosmetics and food industries. In addition, it emphasizes the regulatory aspects of commercial collagen peptide by highlighting information related to certain ingredients. Also covering patents and existing commercial collagen peptide products with indications. This review provides information on collagen peptides with industrial applications covering essential aspects for future research in this specific field. |
id |
URPE_4943663f7d01dfb0aa11b13e27217d02 |
---|---|
oai_identifier_str |
oai:tede2:tede2/9692 |
network_acronym_str |
URPE |
network_name_str |
Biblioteca Digital de Teses e Dissertações da UFRPE |
repository_id_str |
|
spelling |
PORTO, Ana Lúcia FigueiredoOLIVEIRA, Vagne de MeloBATISTA, Juanize Matias da SilvaCUNHA, Márcia Nieves Carneiro daBEZERRA, Raquel Pedrozahttp://lattes.cnpq.br/3148035787129095SILVA, Quésia Jemima da2024-07-24T19:59:44Z2022-08-11SILVA, Quésia Jemima da. Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica. 2022. 106 f. Tese (Programa de Pós-Graduação em Biociência Animal) - Universidade Federal Rural de Pernambuco, Recife.http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/9692By-products from the fishing industry are rich in biological compounds, such as proteases, and their recovery has technical advantages over chemical ones and has wide industrial applications, mainly in medicines, cosmetics, food, textiles and animal feed, due to its property of high activity over a wide pH range and at different temperatures. Several techniques for recovery, identification and purification of enzymes capable of cleaving the peptide bonds of collagen molecules and subsequently degrading them into small peptides from these residues have been used, such as the semipurification technique by aqueous two-phase system (SDFA) which was applied to neglected mullet (Mugil liza) waste (viscera) for the treatment of enzymes with collagenolytic activity. The crude extract (EB) obtained from the intestinal viscera of Mullet (Mugil liza) showed the following activities: total protein 1.02 U/mg; collagenolytic activity: 152.0 U/mg volumetric; 161 U/mg specific collagenolytic activity; 7.35 U/mL of proteolytic/proteasic activity; and, finally, 14.2 mg/mL of specific proteolytic activity. In the two-phase PEG/citrate aqueous system, according to the 2³ factorial design, using the variables Partition coefficient (K), Yield (Y), and Purification factor (FP), it was possible to observe that the extraction yields (Y ) obtained ranged from 89 to 124.34% and from 242.11 to 435.61% for protease and proteases with collagenolytic activity, respectively. The results showed the advantage of this semi-purification technique regarding the extraction and purification of collagenolytic enzymes with industrial application. The fish collagen peptides, highlighted in the integrative review, are important in the global collagen peptides market and are important in the development of biomaterials that constitute pharmaceutical, cosmetic and food products. , properties, preparation methods, and applications in different industries. It specifically encompasses collagen peptides applied in the pharmaceutical, cosmetics and food industries. In addition, it emphasizes the regulatory aspects of commercial collagen peptide by highlighting information related to certain ingredients. Also covering patents and existing commercial collagen peptide products with indications. This review provides information on collagen peptides with industrial applications covering essential aspects for future research in this specific field.Subprodutos da indústria pesqueira são ricos em compostos biológicos, como as proteases, e a recuperação destas têm vantagens técnicas sobre as químicas e têm amplas aplicações industriais, principalmente, em medicamentos, cosméticos, alimentos, têxteis e alimentação animal, devido a sua propriedade de alta atividade em uma ampla faixa de pH e em diferentes temperaturas. Várias técnicas de recuperação, identificação e purificação de enzimas capazes clivar as ligações peptídicas das moléculas de colágeno e subsequentemente degrada-las em pequenos peptídeos a partir desses resíduos, tem sido utilizadas, como a técnica de semipurificação por sistema de duas fases aquosa (SDFA) que foi aplicada nos resíduo (vísceras) negligenciados da Tainha (Mugil liza) para tratamento de enzimas com atividade colagenolíticas. O extrato bruto (EB) obtido a partir das vísceras intestinais da Tainha (Mugil liza) apresentou as seguintes atividades: proteínas totais 1,02 U/mg; atividade colagenolítica: 152,0 U/mg volumetrica; 161 U/mg de atividade colagenolitica especifica; 7,35 U/mL de atividade proteolítica/proteasica; e, por fim, 14,2 mg/mL de atividade proteolítica especifica. No sistema de duas fases aquosa PEG/citrato, de acordo com o planejamento fatorial 2³, utilizando as variáveis Coeficiente de partição (K), Rendimento (Y), e Fator de purificação (FP) foi possível observar que os rendimentos da extração (Y) obtidos variaram de 89 a 124,34% e de 242,11 a 435,61% para protease e proteases com atividade colagenolítica, respectivamente. Os resultados mostraram a vantagem desta técnica de semipurificação no que se refere a extração e purificação de enzimas colagenolíticas com aplicação industrial. Os peptídeos de colágeno de peixe, destacados na revisão integrativa, são importantes no mercado global de peptídeos de colágeno e tem importancia no desenvolvimento de biomateriais que constituem produtos farmacêuticos, cosméticos e alimenticíos com isso a revisão reúne diferentes aspectos do peptídeo de colágeno, como classificação, propriedades, métodos de preparação, e aplicações em diferentes indústrias. Engloba especificamente os peptídeos de colágenos aplicados na indústria farmacêutica, de cosméticos e de alimentos. Além disso, enfatiza os aspectos regulatórios do peptídeo de colágeno comercial destacando as informações relacionadas a determinados ingredientes. Abrangendo também patentes e produtos de peptídeos de colágeno comerciais existentes com indicações. Esta revisão traz informações sobre peptídeos de colágeno com aplicações industriais abrangendo aspectos essenciais para realização de futuras pesquisas neste campo específico.Submitted by (ana.araujo@ufrpe.br) on 2024-07-24T19:59:44Z No. of bitstreams: 1 Quesia Jemima da Silva.pdf: 1290988 bytes, checksum: 32e57d480751dd24bccb797335c44944 (MD5)Made available in DSpace on 2024-07-24T19:59:44Z (GMT). No. of bitstreams: 1 Quesia Jemima da Silva.pdf: 1290988 bytes, checksum: 32e57d480751dd24bccb797335c44944 (MD5) Previous issue date: 2022-08-11Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPESapplication/pdfporUniversidade Federal Rural de PernambucoPrograma de Pós-Graduação em Biociência AnimalUFRPEBrasilDepartamento de Morfologia e Fisiologia AnimalIndústria pesqueiraTainha (Peixe)Resíduos de animaisProteaseColagenasesPurificação de enzimaCIENCIAS AGRARIAS::MEDICINA VETERINARIAObtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológicainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/doctoralThesis-1510757014399315592600600600600-89223641879873962044536702642350173192075167498588264571info:eu-repo/semantics/openAccessreponame:Biblioteca Digital de Teses e Dissertações da UFRPEinstname:Universidade Federal Rural de Pernambuco (UFRPE)instacron:UFRPEORIGINALQuesia Jemima da Silva.pdfQuesia Jemima da Silva.pdfapplication/pdf1290988http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/9692/2/Quesia+Jemima+da+Silva.pdf32e57d480751dd24bccb797335c44944MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-82165http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/9692/1/license.txtbd3efa91386c1718a7f26a329fdcb468MD51tede2/96922024-07-24 16:59:44.084oai: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:2024-07-24T19:59:44Biblioteca Digital de Teses e Dissertações da UFRPE - Universidade Federal Rural de Pernambuco (UFRPE)false |
dc.title.por.fl_str_mv |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica |
title |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica |
spellingShingle |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica SILVA, Quésia Jemima da Indústria pesqueira Tainha (Peixe) Resíduos de animais Protease Colagenases Purificação de enzima CIENCIAS AGRARIAS::MEDICINA VETERINARIA |
title_short |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica |
title_full |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica |
title_fullStr |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica |
title_full_unstemmed |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica |
title_sort |
Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica |
author |
SILVA, Quésia Jemima da |
author_facet |
SILVA, Quésia Jemima da |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
PORTO, Ana Lúcia Figueiredo |
dc.contributor.advisor-co1.fl_str_mv |
OLIVEIRA, Vagne de Melo |
dc.contributor.referee1.fl_str_mv |
BATISTA, Juanize Matias da Silva |
dc.contributor.referee2.fl_str_mv |
CUNHA, Márcia Nieves Carneiro da |
dc.contributor.referee3.fl_str_mv |
BEZERRA, Raquel Pedroza |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/3148035787129095 |
dc.contributor.author.fl_str_mv |
SILVA, Quésia Jemima da |
contributor_str_mv |
PORTO, Ana Lúcia Figueiredo OLIVEIRA, Vagne de Melo BATISTA, Juanize Matias da Silva CUNHA, Márcia Nieves Carneiro da BEZERRA, Raquel Pedroza |
dc.subject.por.fl_str_mv |
Indústria pesqueira Tainha (Peixe) Resíduos de animais Protease Colagenases Purificação de enzima |
topic |
Indústria pesqueira Tainha (Peixe) Resíduos de animais Protease Colagenases Purificação de enzima CIENCIAS AGRARIAS::MEDICINA VETERINARIA |
dc.subject.cnpq.fl_str_mv |
CIENCIAS AGRARIAS::MEDICINA VETERINARIA |
description |
By-products from the fishing industry are rich in biological compounds, such as proteases, and their recovery has technical advantages over chemical ones and has wide industrial applications, mainly in medicines, cosmetics, food, textiles and animal feed, due to its property of high activity over a wide pH range and at different temperatures. Several techniques for recovery, identification and purification of enzymes capable of cleaving the peptide bonds of collagen molecules and subsequently degrading them into small peptides from these residues have been used, such as the semipurification technique by aqueous two-phase system (SDFA) which was applied to neglected mullet (Mugil liza) waste (viscera) for the treatment of enzymes with collagenolytic activity. The crude extract (EB) obtained from the intestinal viscera of Mullet (Mugil liza) showed the following activities: total protein 1.02 U/mg; collagenolytic activity: 152.0 U/mg volumetric; 161 U/mg specific collagenolytic activity; 7.35 U/mL of proteolytic/proteasic activity; and, finally, 14.2 mg/mL of specific proteolytic activity. In the two-phase PEG/citrate aqueous system, according to the 2³ factorial design, using the variables Partition coefficient (K), Yield (Y), and Purification factor (FP), it was possible to observe that the extraction yields (Y ) obtained ranged from 89 to 124.34% and from 242.11 to 435.61% for protease and proteases with collagenolytic activity, respectively. The results showed the advantage of this semi-purification technique regarding the extraction and purification of collagenolytic enzymes with industrial application. The fish collagen peptides, highlighted in the integrative review, are important in the global collagen peptides market and are important in the development of biomaterials that constitute pharmaceutical, cosmetic and food products. , properties, preparation methods, and applications in different industries. It specifically encompasses collagen peptides applied in the pharmaceutical, cosmetics and food industries. In addition, it emphasizes the regulatory aspects of commercial collagen peptide by highlighting information related to certain ingredients. Also covering patents and existing commercial collagen peptide products with indications. This review provides information on collagen peptides with industrial applications covering essential aspects for future research in this specific field. |
publishDate |
2022 |
dc.date.issued.fl_str_mv |
2022-08-11 |
dc.date.accessioned.fl_str_mv |
2024-07-24T19:59:44Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/doctoralThesis |
format |
doctoralThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
SILVA, Quésia Jemima da. Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica. 2022. 106 f. Tese (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/tede2/9692 |
identifier_str_mv |
SILVA, Quésia Jemima da. Obtenção de proteases por particionamento dos resíduos de tainha (Mugil liza) visando sua aplicação biotecnológica. 2022. 106 f. Tese (Programa de Pós-Graduação em Biociência Animal) - Universidade Federal Rural de Pernambuco, Recife. |
url |
http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/9692 |
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/tede2/9692/2/Quesia+Jemima+da+Silva.pdf http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/9692/1/license.txt |
bitstream.checksum.fl_str_mv |
32e57d480751dd24bccb797335c44944 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_ |
1810102212993482752 |