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Master's Dissertation
DOI
https://doi.org/10.11606/D.75.2022.tde-28042022-112713
Document
Author
Full name
Keila Nascimento Cavalcante
E-mail
Institute/School/College
Knowledge Area
Date of Defense
Published
São Carlos, 2022
Supervisor
Committee
Cardoso, Daniel Rodrigues (President)
Ahrné, Lilia Maria
Cavallini, Daniela Cardoso Umbelino
Title in Portuguese
Efeitos da tecnologia não-térmica de processamento (UV-C) na hidrólise da β-Lactoglobulina por Tripsina: perfil de peptídeos e transporte transepitelial de peptídeos bioativos em monocamadas de células de Caco-2
Keywords in Portuguese
β-Lactoglobulina
hidrólise
peptídeos bioativos
processamento não térmico
transporte transepitelial
UV-C
Abstract in Portuguese
A β-Lactoglobulina é a proteína majoritária no soro do leite, apresenta baixa digestibilidade in vivo, e elevado potencial alergênico. O emprego de tecnologias de processamento não-térmico vem ganhando interesse na indústria de alimentos, se destacam por serem economicamente viáveis, além de não causarem perdas de nutrientes, comumente observado no processamento de pasteurização. A luz UV-C pode ser capaz de induzir mudanças na conformacionais de proteínas, alterando sua suscetibilidade a enzimas proteolíticas. Nesse contexto, esse trabalho teve como objetivo, comparar os efeitos da irradiação por UV-C com o processo térmico, avaliando mudanças conformacionais na β-lactoglobulina, grau de hidrólise (DH) tríptica, perfil de peptídeos, e o transporte transepitelial dos peptídeos em modelos de células de Caco-2. Foi observado um aumento significativo na constante de velocidade de hidrólise da β-lactoglobulina irradiada com luz UV-C, em comparação a proteína nativa e processada termicamente, sugerindo que os sítios de clivagem na cadeia proteíca se encontram mais expostos. O perfil de massas de peptídeos nos hidrolisados da β-lactoglobulina irradiada com luz UV-C apresenta uma maior diversidade e teor de peptídeos em comparação aos hidrolisado da proteína nativa e pasteurizada. Nos hidrolisados trípiticos da β-lactoglobulina, irradiada com luz UV-C, foram encontrados seis peptídeos bioativos, fβ-LG (f31-36, f57-76, f87-91, f91-99, f118-121, e f158-164). O transporte transepitelial em modelos de células de Caco-2, mostrou de baixa a médio transporte/absorção in vivo para os peptídeos bioativos f87-91, f91-99 e f158-164. O uso da luz UV-C se mostra uma alternativa de grande relevância frente ao tratamento térmico, elevando significativamente o grau de hidrólise tríptica, promovendo a formação e peptídeos bioativos, e diminuindo o potencial alergênico dos hidrolisados.
Title in English
β-Lactoglobulin by Trypsin: Peptide Profile and Transepithelial Transport of Derived Bioactive Peptides in Caco-2 Cell Monolayers
Keywords in English
β-Lactoglobulin
bioactive peptides
hydrolysis
non-thermal processing
transepithelial transport
UV-C
Abstract in English
β-Lactoglobulin is the major protein in whey, has low in vivo digestibility, and has high allergenic potential. The use of non-thermal processing technologies has been gaining interest in the food industry, they stand out for being economically viable, in addition to not causing nutrient losses, as commonly observed in the pasteurization processing. UV-C light may be able to induce conformation changes in proteins, altering their susceptibility to proteolytic enzymes. In this context, this work aimed to compare the effects of UV-C irradiation with the thermal process, evaluating conformational changes in β-lactoglobulin, degree of hydrolysis (DH) by trypsin, peptide profile, and transepithelial transport of peptides in Caco-2 cell models. A significant increase in the hydrolysis rate constant of β-lactoglobulin irradiated with UV-C light was observed, compared to native and thermally processed protein, suggesting that the protein backbone cleavage sites are more exposed. The peptide mass profile in β-lactoglobulin hydrolysates irradiated with UV-C light shows greater diversity and peptide content compared to native and pasteurized protein hydrolysates. In the tryptic hydrolysates of β-lactoglobulin, irradiated with UV-C light, six bioactive peptides were found, fβ-LG (f31-36, f57-76, f87-91, f91-99, f118-121, and f158-164). Transepithelial transport in Caco-2 cell models showed low to the intermediate in vivo transport and absorption for the bioactive peptides f87-91, f91-99, and f158-164. The use of UV-C light is a very relevant compared with thermal processing of whey, ensuring microbiological safety, significantly increasing the degree of tryptic hydrolysis, promoting the formation of bioactive peptides, and reducing the allergenic potential of hydrolysates.
 
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Publishing Date
2022-05-02
 
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