Photo-Induced Modification of Food Protein Structure and Functionality

Manzocco, Lara

doi:10.1007/s12393-015-9110-6

Cited by 20 publications

(17 citation statements)

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“…The energy of the radiation absorbed by the chromophores is transferred between the initial sites of oxidation and the part of the protein that controls its structure and function. This transfer is primarily directed to sulphur-containing amino acids through hydrogen bonding networks and protein backbone [ 2 , 3 ]. As a result, side-chain oxidation, backbone fragmentation and/or formation of cross-links and aggregates occur, leading to a modification in both protein structure and properties [ 4 ].…”

Section: Introductionmentioning

confidence: 99%

Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures

Manzocco

Plazzotta

Calligaris

2020

Foods

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The capacity of UV-C light to induce glycation and modify functional properties of systems containing freeze-dried egg white proteins and carbohydrates with increasing molecular weight (i.e., glucose, maltose, trehalose and maltodextrin) was studied. Color changes induced by light exposure were taken as typical indicators of glycation. Samples were then analyzed for selected physical (critical concentration, particle size and viscosity), chemical (ovalbumin content) and technofunctional properties (gelling temperature and foaming capacity). The presence of sugars during exposure to UV-C light promoted intense browning and decreased ovalbumin content by circa 30%. Concomitantly, up to a 3-fold increase in critical concentration of the aqueous suspensions of the irradiated protein-carbohydrate powders and changes in particle size were detected. These modifications were consistent with the development of non-enzymatic browning reactions upon UV-C light irradiation. Photoinduced glycation was associated to a decrease in viscosity, a tendency to form gel at temperature lower by up to 8 °C and a better capacity of foam stabilization. The intensity of these changes seems to be affected by the nature of the carbohydrates reacting with proteins, with longer carbohydrates able to produce systems with higher foam stability capacity.

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Section: Introductionmentioning

confidence: 99%

Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures

Manzocco

Plazzotta

Calligaris

2020

Foods

Self Cite

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“…Light processing is based on the application of electromagnetic radiation in the nonionizing region of the spectrum between 170 and 1,100 nm, including UV‐C and pulsed light processing (Manzocco, ). UV‐C is the portion of the electromagnetic spectrum with wavelengths between 200 and 280 nm (Gómez‐López, Ragaert, Debevere, & Devlieghere, ), which can be obtained using low‐ or medium‐pressure mercury lamps as the light sources (Manzocco, ). UV‐C processing primarily relies on continuous nonthermal germicidal radiation to exert photochemical effects on biomolecules that are abundant in highly conjugated double‐bond systems, such as proteins and microbial DNA.…”

Section: Changes In Protein Functionality Due To Uv‐c and Pulsed Lighmentioning

confidence: 99%

“…UV‐C and pulsed light share similarities in their underlying mechanisms of photo‐induced damage to proteins (that is, chemical modification of protein molecules when exposed to light). When exposed to light, proteins undergo chemical modification known as protein photoreaction, which is associated with (i) the abundance of endogenous chromophores (for example, tryptophan, tyrosine, phenylalanine, and so on) within the protein structure, (ii) the ability of some proteins to bind exogenous chromophores, and (iii) their rapid reactivity with other excited state species (for example, singlet oxygen; Manzocco, ). Photooxidation of proteins can occur either by direct or indirect means (Davies & Truscott, ; Pattison, Rahmanto, & Davies, ).…”

Section: Changes In Protein Functionality Due To Uv‐c and Pulsed Lighmentioning

confidence: 99%

“…The former involves direct absorption of UV radiation by the protein or bound chromophore groups, whereas the latter involves indirect protein oxidation via the formation and subsequent reactions of singlet oxygen generated by the transfer of energy to ground state molecular oxygen. In addition to its photochemical effects, pulsed light has been reported to result in photothermal (that is, local heating upon intense pulsed light) and photophysical (that is, disturbance due to high peak power pulses) effects that can potentially result in structural damage to biomolecules (Gómez‐López et al., ; Manzocco, ).…”

Section: Changes In Protein Functionality Due To Uv‐c and Pulsed Lighmentioning

confidence: 99%

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Modifying the Functional Properties of Egg Proteins Using Novel Processing Techniques: A Review

Liu

Oey

Bremer

et al. 2019

Comp Rev Food Sci Food Safe

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Egg proteins can be used in a wide range of food products, owing to their excellent foaming, emulsifying, and gelling properties. Another important functional property is the susceptibility of egg proteins to enzymatic hydrolysis, as protein digestion is closely related to its nutritional value. These functional properties of egg proteins are likely to be changed during food processing. Conventional thermal processing can easily induce protein denaturation and aggregation and consequently reduce the functionality of egg proteins due to the presence of heat‐labile proteins. Accordingly, there is interest from the food industry in seeking novel nonthermal or low‐thermal techniques that sustain protein functionality. To understand how novel processing techniques, including high hydrostatic pressure, pulsed electric fields, ionizing radiation, ultraviolet light, pulsed light, ultrasound, ozone, and high pressure homogenization, affect protein functionality, this review introduces the mechanisms involved in protein structure modification and describes the structure–functionality relationships. Novel techniques differ in their mechanisms of protein structure modification and some have been shown to improve protein functionality for particular treatment conditions and product forms. Although there is considerable industrial potential for the use of novel techniques, further studies are required to make them a practical reality, as the processing of egg proteins often involves other influencing factors, such as different pH and the presence of other food additives (for example, salts, sugar, and polysaccharides).

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“…aumento nos tióis livres acessíveis após exposição da β-lactoglobulina à luz na região do UV-C em 254 nm. Além disso, a formação de tióis livres para proteínas expostas a luz na região do UV-C (200-280 nm) é um fato bem consolidado na literatura (MANZOCCO, 2015;NEVES-PETERSEN et al, 2009) e ocorre, principalmente, para proteínas que tem um triptofano espacialmente próximo a uma ponte de dissulfeto. Para as medidas de tióis livres acessíveis foi usado o DTNB que reage estequiometricamente com os tióis livres acessíveis ao solvente presentes na proteína.…”

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Processamento UV-C de proteínas do soro do leite: Efeitos na estrutura e digestibilidade

Silva¹

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pela dedicada orientação e paciência. Aos meus pais Silvia e Tadeu, pela dedicação, por lutarem incessantemente para que eu tivesse uma vida melhor, investirem e apoiarem a minha educação. Tudo que sou e tenho devo a vocês, que são exemplo e inspiração. Ao meu irmão Gustavo que me ensina a ter coragem e disciplina para vencer a mim mesma e procurar ser uma pessoa melhor. Ao meu namorado Jean, pelo apoio nos momentos difíceis, alegria que preenche meus dias e generosidade que me inspira. A minha amiga Aline, por me inspirar a ser melhor, pelos conselhos e auxílio nos experimentos deste trabalho. A minha amiga Larissa, que me incentivou a iniciar essa jornada e me ajudou a completála com mais leveza. Aos meus familiares e amigos, por me darem suporte sempre. Aos colegas do Grupo de Química Inorgânica e Analítica, especialmente a Jéssica, Marcella, Luiz, e Felipe pela amizade e auxílio nos experimentos. Aos queridos amigos do laboratório da cachaça, especialmente ao Lucas, pelo carinho e amizade. As técnicas Silmara e Jennifer pela paciência e pelo suporte oferecido neste trabalho. Ao Prof. Dr. Júlio César Borges e ao Grupo LBBP, pela estrutura fornecida na realização da espectroscopia por CD e gel filtração analítica. Agradeço especialmente a Vanessa, Silvia, Noeli e Amanda, pelo auxílio e disponibilidade. Ao Prof. Dr. Frank N. Crespilho, Grupo de Bioeletroquímica e Interfaces, especialmente Lucyano, pela estrutura fornecida na realização do FTIR-ATR. Aos funcionários do IQSC e da USP São Carlos. Ao CNpQ pela concessão da bolsa de mestrado. RESUMO SILVA, Juliana Fracola. Processamento UV-C de proteínas do soro do leite: Efeitos na estrutura e digestibilidade. 2019. 86 f. Dissertação (Mestrado

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Photo-Induced Modification of Food Protein Structure and Functionality

Cited by 20 publications

References 96 publications

Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures

Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures

Modifying the Functional Properties of Egg Proteins Using Novel Processing Techniques: A Review

Processamento UV-C de proteínas do soro do leite: Efeitos na estrutura e digestibilidade

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