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Master's Dissertation
DOI
https://doi.org/10.11606/D.75.2019.tde-03102019-090331
Document
Author
Full name
Juliana Fracola da Silva
E-mail
Institute/School/College
Knowledge Area
Date of Defense
Published
São Carlos, 2019
Supervisor
Committee
Cardoso, Daniel Rodrigues (President)
Bezerra, Rosângela Maria Neves
Cavallini, Daniela Cardoso Umbelino
Colnago, Luiz Alberto
Title in Portuguese
Processamento UV-C de proteínas do soro do leite: Efeitos na estrutura e digestibilidade
Keywords in Portuguese
α-lactoalbumina
β-lactoglobulina
digestibilidade
luz UV-C
proteínas do soro
Abstract in Portuguese

O aumento na expectativa de vida e rápido crescimento da proporção de idosos gera desafios e oportunidades quando se trata de condições fisiológicas relacionadas ao envelhecimento. A sarcopenia, perda de massa e resistência muscular, é uma doença comum entre a população sênior e está associada com a baixa ingestão e digestibilidade de nutrientes. Assim, a indústria de laticínios busca desenvolver novos produtos que atendam a demanda nutricional diária de idosos e ainda que tenham características sensoriais específicas para eles. No caso dos produtos derivados do leite sabe-se que as proteínas majoritárias do soro (α-lactoalbumina e β-lactoglobulina) têm sua digestão incompleta e apresentam potencial alergênico, podendo contribuir para um déficit nutricional. Neste contexto, este trabalho objetivou investigar os efeitos do tratamento com luz UV-C (266 nm) na estrutura da α-lactoalbumina e β-lactoglobulina e o impacto nas suas digestibilidades. As proteínas irradiadas por 2 h com luz monocromática (266 nm) foram submetidas à digestão gástrica in vitro simulando adultos jovens e idosos. As alterações na estrutura das proteínas foram estudas por técnicas espectroscópicas (UV-Vis, CD-UV, FTIR, RMN 1H e fluorescência), cromatografia líquida, e eletroforese (SDS-PAGE). Observou-se modificações na estrutura secundária e terciária da β-lactoglobulina, redução de pontes de dissulfeto, e formação do fotoproduto N-formilquinurenina (NFK). A irradiação aumentou a digestibilidade desta proteína em 50 pontos percentuais para idosos e 25 pontos percentuais para adultos jovens. Além disso, o perfil de peptídeos liberados após digestão para α-lactoalbumina e β-lactoglobulina tratadas com luz UV-C é diferente em comparação do perfil de peptídeos da proteína nativa.

Title in English
UV-C Processing of milk whey proteins: Effects on structure and digestibility
Keywords in English
α-lactalbumin
β-lactoglobulin
digestibility
whey protein
Abstract in English

The worldwide increasing proportion of senior citizen is a major concern due to age-related condition. Sarcopenia is defined as the loss of muscle mass and function and is closely associated with malnutrition and decline of nutrient intake in elderly. Dairy industry has the potential to tailor products that may provide the intake of the required daily nutritional value combined with sensory characteristics with seniors as target market. However, the major whey proteins (α-lactalbumin and β-lactoglobulin) exhibit incomplete digestion leading to a decrease in the nutritional value and can cause allergies. In this context, this work aimed to investigate the effects of UV-C light treatment (266 nm) on protein structure and the impact on digestibility. Proteins were irradiated for 2 h with monochromatic light (266 nm) and then submitted to gastric digestion in vitro simulating health adults and elderly. In order to analyze the changes in the protein structure, spectroscopic techniques (UV-Vis, CD-UV, FTIR, 1H NMR, and fluorescence), liquid chromatography, and electrophoresis (SDS-PAGE) were employed. Changes in the secondary and tertiary structure of β-lactoglobulin, reduction of its disulphide bridges and formation of N-formylquinurenine as an photoproduct (NFK) were observed. These changes increased the digestibility of light irradiated protein by 50% for elderly and 25% for health adults. In addition, the peptide profile released after protein digestion is different for light treated proteins in comparision to native protein.

 
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Publishing Date
2019-10-15
 
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