Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano

Detalhes bibliográficos
Autor(a) principal: Leite, Hugo de Brito
Data de Publicação: 2016
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
Texto Completo: http://www.repositorio.ufc.br/handle/riufc/39345
Resumo: Peptidases are enzymes capable of performing cleavage of peptide bonds of other proteins and peptides. These enzymes exhibit a broad spectrum of applications because they are used from the food industry to the leather and skin processing and drug formulation. Peptidases also have been used in the dairy industry for the cheese production. The coagulation of milk caseins is the main step in the production of the cheese curds. Rennet or renin are consist of chymosin and when added to the milk they cause the first step of forming cheese, the coagulation. Due to restrictions of food intake using animal rennet because of eating habits (vegetarianism) or religious reasons (Judaism and Islamism) the search for coagulating enzymes alternatives to rennet has intensified. The present work aimed to evaluate the caseinolytic and coagulant activities of the milk of five different latex protein extracts for the production of cheese. The latex fractions obtained were dissolved in Tris-HCl 50 mM pH 6.5 buffer and submitted to total proteolytic activity assays with different activators, milk coagulation, total casein hydrolysis, and of κ-casein over time by SDS-PAGE on 15% polyacrylamide gels, establishing a protocol for cheese curd production and detecting peptidases after the production of cheese. Only the fractions of C. procera, C. grandiflora, and C. papaya showed proteolytic activity and milk coagulation activity. These peptidases were activated by DTT and L-cysteine. The milk coagulation time by latex peptidases is dose dependent with 60 µg being the optimum amount to coagulate 2 mL of milk. C. procera and C. grandiflora showed specific activity of milk coagulation close to the commercial rennet of animal origin. High concentrations of NaCl and CaCl2 did not affect the proteolytic activity and coagulation of milk. However, the pre-incubation of these samples at 75º C for 10 minutes completely eliminated their activities. Both proteolytic fractions proved to be capable of hydrolyzing κ-casein and producing peptides of 16 KDa similarly the commercial rennet. The cheeses generated by the latex peptidases had nice flavor, firm texture, scent and yield similar to cheeses produced with commercial chymosin. Also, no proteolytic activity was detected after the production of cheese. This way, the peptidases from C. procera and C. grandiflora can be used as an alternative to chymosin in the production of cheese curds.
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spelling Aplicação de peptidases laticíferas para produção de queijo coalho vegetarianoCaseínaQuimosinaPeptidasesCoalho vegetalCoagulação do leitePeptidases are enzymes capable of performing cleavage of peptide bonds of other proteins and peptides. These enzymes exhibit a broad spectrum of applications because they are used from the food industry to the leather and skin processing and drug formulation. Peptidases also have been used in the dairy industry for the cheese production. The coagulation of milk caseins is the main step in the production of the cheese curds. Rennet or renin are consist of chymosin and when added to the milk they cause the first step of forming cheese, the coagulation. Due to restrictions of food intake using animal rennet because of eating habits (vegetarianism) or religious reasons (Judaism and Islamism) the search for coagulating enzymes alternatives to rennet has intensified. The present work aimed to evaluate the caseinolytic and coagulant activities of the milk of five different latex protein extracts for the production of cheese. The latex fractions obtained were dissolved in Tris-HCl 50 mM pH 6.5 buffer and submitted to total proteolytic activity assays with different activators, milk coagulation, total casein hydrolysis, and of κ-casein over time by SDS-PAGE on 15% polyacrylamide gels, establishing a protocol for cheese curd production and detecting peptidases after the production of cheese. Only the fractions of C. procera, C. grandiflora, and C. papaya showed proteolytic activity and milk coagulation activity. These peptidases were activated by DTT and L-cysteine. The milk coagulation time by latex peptidases is dose dependent with 60 µg being the optimum amount to coagulate 2 mL of milk. C. procera and C. grandiflora showed specific activity of milk coagulation close to the commercial rennet of animal origin. High concentrations of NaCl and CaCl2 did not affect the proteolytic activity and coagulation of milk. However, the pre-incubation of these samples at 75º C for 10 minutes completely eliminated their activities. Both proteolytic fractions proved to be capable of hydrolyzing κ-casein and producing peptides of 16 KDa similarly the commercial rennet. The cheeses generated by the latex peptidases had nice flavor, firm texture, scent and yield similar to cheeses produced with commercial chymosin. Also, no proteolytic activity was detected after the production of cheese. This way, the peptidases from C. procera and C. grandiflora can be used as an alternative to chymosin in the production of cheese curds.Peptidases são enzimas capazes de realizar a clivagem de ligações peptídicas de outras proteínas e peptídeos. Essas enzimas apresentam um amplo espectro de aplicações, pois são utilizadas desde a indústria alimentícia até mesmo no processamento de couro e pele e formulações de medicamentos. Peptidases também têm sido utilizadas na indústria de laticínios para a produção de queijos. A coagulação das caseínas do leite é a principal etapa na produção de queijos do tipo coalho. O coalho ou renina é composto por quimosina e quando adicionado ao leite produz a primeira etapa de formação do queijo, a coagulação. Devido a restrições de consumo de alimentos que utilizem o coalho animal por razões de hábitos alimentares (vegetarianismo) ou por razões religiosas (judaísmo e islamismo) a busca por enzimas coagulantes alternativas à quimosina tem intensificado. O presente trabalho objetivou avaliar as atividades caseinolítica e coagulante do leite de cinco diferentes extratos de proteínas laticíferas para a produção de queijo. As frações laticíferas obtidas foram dissolvidas em tampão Tris-HCl 50 mM pH 6,5 e submetidas aos seguintes ensaios: atividade proteolítica total, atividade proteolítica com diferentes ativadores, atividade de coagulação do leite, avaliação da hidrólise da caseína total por SDS-PAGE e avaliação da κ-caseína ao longo do tempo através de SDS-PAGE em géis de poliacrilamida 15%, estabelecimento de um protocolo de produção do queijo tipo coalho e detecção de peptidases após a produção do queijo. Somente as frações de C. procera, C. grandiflora e C. papaya exibiram atividade proteolítica e atividade coagulação do leite, estas peptidases foram ativadas por DTT e Lcisteína. O tempo de coagulação do leite pelas peptidases laticíferas foi dose-ependente, sendo 60 µg a quantidade ideal para coagular 2 mL de leite. C. procera e C. grandiflora apresentaram atividade específica de coagulação do leite idênticas ao coalho comercial de origem animal. Altas concentrações de NaCl e CaCl2 não afetaram a atividade proteolítica e de coagulação do leite. Entretanto, a pré-incubação dessas amostras a 75º C por 10 minutos eliminou completamente suas atividades. Ambas as frações proteolítica demonstraram-se capazes de hidrolisar a κ-caseína e produzir peptídeos de 16 KDa de maneira idêntica ao coalho comercial. Os queijos gerados com as peptidases laticíferas apresentaram sabor agradável, textura firme, aroma e rendimento similares aos queijos produzidos com a quimosina comercial. Também não foi detectada atividade proteolítica após a produção do queijo. Dessa forma, as peptidases de C. procera e C. grandiflora podem ser utilizadas como alternativa a quimosina na produção de queijo coalho.Freitas, Cleverson Diniz Teixeira deLeite, Hugo de Brito2019-02-04T17:23:29Z2019-02-04T17:23:29Z2016info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfLEITE, Hugo de Brito. Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano. 2016. 84 f. Dissertação (Mestrado em Bioquímica) - Universidade Federal do Ceará, Fortaleza, 2016.http://www.repositorio.ufc.br/handle/riufc/39345porreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFCinfo:eu-repo/semantics/openAccess2019-04-12T22:40:46Zoai:repositorio.ufc.br:riufc/39345Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2024-09-11T18:19:11.964700Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false
dc.title.none.fl_str_mv Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
title Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
spellingShingle Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
Leite, Hugo de Brito
Caseína
Quimosina
Peptidases
Coalho vegetal
Coagulação do leite
title_short Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
title_full Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
title_fullStr Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
title_full_unstemmed Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
title_sort Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano
author Leite, Hugo de Brito
author_facet Leite, Hugo de Brito
author_role author
dc.contributor.none.fl_str_mv Freitas, Cleverson Diniz Teixeira de
dc.contributor.author.fl_str_mv Leite, Hugo de Brito
dc.subject.por.fl_str_mv Caseína
Quimosina
Peptidases
Coalho vegetal
Coagulação do leite
topic Caseína
Quimosina
Peptidases
Coalho vegetal
Coagulação do leite
description Peptidases are enzymes capable of performing cleavage of peptide bonds of other proteins and peptides. These enzymes exhibit a broad spectrum of applications because they are used from the food industry to the leather and skin processing and drug formulation. Peptidases also have been used in the dairy industry for the cheese production. The coagulation of milk caseins is the main step in the production of the cheese curds. Rennet or renin are consist of chymosin and when added to the milk they cause the first step of forming cheese, the coagulation. Due to restrictions of food intake using animal rennet because of eating habits (vegetarianism) or religious reasons (Judaism and Islamism) the search for coagulating enzymes alternatives to rennet has intensified. The present work aimed to evaluate the caseinolytic and coagulant activities of the milk of five different latex protein extracts for the production of cheese. The latex fractions obtained were dissolved in Tris-HCl 50 mM pH 6.5 buffer and submitted to total proteolytic activity assays with different activators, milk coagulation, total casein hydrolysis, and of κ-casein over time by SDS-PAGE on 15% polyacrylamide gels, establishing a protocol for cheese curd production and detecting peptidases after the production of cheese. Only the fractions of C. procera, C. grandiflora, and C. papaya showed proteolytic activity and milk coagulation activity. These peptidases were activated by DTT and L-cysteine. The milk coagulation time by latex peptidases is dose dependent with 60 µg being the optimum amount to coagulate 2 mL of milk. C. procera and C. grandiflora showed specific activity of milk coagulation close to the commercial rennet of animal origin. High concentrations of NaCl and CaCl2 did not affect the proteolytic activity and coagulation of milk. However, the pre-incubation of these samples at 75º C for 10 minutes completely eliminated their activities. Both proteolytic fractions proved to be capable of hydrolyzing κ-casein and producing peptides of 16 KDa similarly the commercial rennet. The cheeses generated by the latex peptidases had nice flavor, firm texture, scent and yield similar to cheeses produced with commercial chymosin. Also, no proteolytic activity was detected after the production of cheese. This way, the peptidases from C. procera and C. grandiflora can be used as an alternative to chymosin in the production of cheese curds.
publishDate 2016
dc.date.none.fl_str_mv 2016
2019-02-04T17:23:29Z
2019-02-04T17:23:29Z
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.uri.fl_str_mv LEITE, Hugo de Brito. Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano. 2016. 84 f. Dissertação (Mestrado em Bioquímica) - Universidade Federal do Ceará, Fortaleza, 2016.
http://www.repositorio.ufc.br/handle/riufc/39345
identifier_str_mv LEITE, Hugo de Brito. Aplicação de peptidases laticíferas para produção de queijo coalho vegetariano. 2016. 84 f. Dissertação (Mestrado em Bioquímica) - Universidade Federal do Ceará, Fortaleza, 2016.
url http://www.repositorio.ufc.br/handle/riufc/39345
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dc.source.none.fl_str_mv reponame:Repositório Institucional da Universidade Federal do Ceará (UFC)
instname:Universidade Federal do Ceará (UFC)
instacron:UFC
instname_str Universidade Federal do Ceará (UFC)
instacron_str UFC
institution UFC
reponame_str Repositório Institucional da Universidade Federal do Ceará (UFC)
collection Repositório Institucional da Universidade Federal do Ceará (UFC)
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