Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation

Ghosh, Rajib R.; Kar, Turban; Dutta, Bibhas Kumar; Pathak, Adrija; Rakshit, Rupali; Basak, R. K.; Das, Asish R.; Waheeda, K.; Basak, Pijush; Bhattacharyya, Maitree

doi:10.1007/s13765-018-0351-y

Cited by 5 publications

(2 citation statements)

References 28 publications

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“…The drying method determined some structural changes in carbohydrates, as indicated by the differences registered in the absorption spectra region IV, compared to raw sample, where the peak at 1075 cm −1 is no more well-defined. The sample pretreated by UV irradiation followed by HAD showed notable changes in the region II of the IR absorption spectra (amide I and II), in particular for amide II band associated to N-H bending of secondary amides (the peak at 1554 cm −1 disappeared) and C-N stretching of peptide bond, probably due to protein conformational changes [37,38].…”

Section: Evaluation Of Chemical Changes In Dried Mushrooms Using the ...mentioning

confidence: 99%

Influence of Convective and Vacuum-Type Drying on Quality, Microstructural, Antioxidant and Thermal Properties of Pretreated Boletus edulis Mushrooms

et al. 2022

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Freshly harvested Boletus edulis mushrooms are subjected to rapid loss of quality due to the high moisture content and enzymatic activity. Drying time, quality characteristics, microstructural and thermal properties were studied in mushrooms ground to puree subjected to hot air drying (HAD), freeze drying (FD) and centrifugal vacuum drying (CVD). The influence of hot water blanching and UV-C pretreatments was additionally investigated. The rehydration ability of mushroom powders was improved by FD, especially without pretreatment or combined to UV-C exposure. The HAD and CVD, with no pretreatment or combined to UV-C, ensured good preservation of phenolics and antioxidant activity of dried mushrooms. The total difference in color of mushroom pigments extracted in acetone was lower in samples dried by CVD and higher in ones by FD. Blanching before HAD produced whiter product probably due to the reduced polyphenoloxidase activity. Scanning Electron Microscopy (SEM) analysis showed fewer physical changes in FD-samples. Heat-induced structural changes were noticed by Differential Scanning Calorimetry (DSC), Thermogravimetry (TG) and Derivative Thermogravimetry (DTG) analysis, in particular of biopolymers, confirmed by ATR-FTIR analysis. Based on our complex approach, the UV pretreatment of mushrooms could be a better alternative to water blanching. Centrifugal vacuum emerged as a new efficient drying method in terms of bioactive compounds, color and thermal stability, while FD led to better rehydration ability and microstructure.

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Section: Evaluation Of Chemical Changes In Dried Mushrooms Using the ...mentioning

confidence: 99%

Influence of Convective and Vacuum-Type Drying on Quality, Microstructural, Antioxidant and Thermal Properties of Pretreated Boletus edulis Mushrooms

et al. 2022

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“…A concentração analítica das soluções proteicas foi calculada por meio de espectroscopia de absorção eletrônica utilizando o valor de absortividade molar de ɛ280nm=1,76 x 10 4 L mol -1 cm -1 para a β-lactoglobulina e ɛ280nm= 2,846 x 10 4 L mol -1 cm -1 para a α-lactoalbumina (GILL e HIPPEL, 1989…”

Section: Determinação Da Concentração Analíticaunclassified

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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An insight into the structural analysis of α-crystallin of habitat-specific fish: a computational approach

Chakraborty

Ganguli

et al. 2023

J Proteins Proteom

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α-crystallin is a major eye lens protein, comprising up to 40% of total lens protein. It is composed of two subunits, αA and αB and share a common central domain of about 90 residues with variable N-and C-terminal extensions. For the establishment of an evolutionary inter-relationship, an elucidation of the structure and alignment of protein sequences is crucial. In the present study, a bioinformatics approach was adopted to explore the possible structure, sequence and phylogenetic diversity of α-crystallin (both subunits αA and αB) from ten habitat-speci c sh species, (freshwater and saltwater) and compared with a standard sequence of Bos taurus species. The sequence of Bos taurus was predicted to be a close homologue of the sh species. Homology modelling has been performed in order to generate a possible '3D' structure of the crystallin proteins using SWISS-MODEL. Our analysis shows that the secondary structures of bovine α-crystallin revealed no considerable differences as compared to that of the crystallins of the habitat-speci c sh and that the presence of β-sheets was predominant in all structures. Though no signi cant differences in the αA subunits were revealed yet some structural variations were observed for αB subunits which had been con rmed by MSA analysis. The 3D structure of the protein hasn't been elucidated yet so a computational analysis estimated no major differences in structures of crystallin for either bovine or the sh species except that saltwater sh proteins possess more favourable states and higher reliabilities. In agreement with previous literature, α-crystallin has a molecular weight of 20kDa approx. and a theoretical pI of 5.75; 55.1% of its sequence is composed of hydrophilic amino acids and it is a cytosolic protein. Considerable improvement of the currently available tools is being done for a detailed understanding of the structure/function relationships of α-crystallin proteins.

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Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation

Cited by 5 publications

References 28 publications

Influence of Convective and Vacuum-Type Drying on Quality, Microstructural, Antioxidant and Thermal Properties of Pretreated Boletus edulis Mushrooms

Influence of Convective and Vacuum-Type Drying on Quality, Microstructural, Antioxidant and Thermal Properties of Pretreated Boletus edulis Mushrooms

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

An insight into the structural analysis of α-crystallin of habitat-specific fish: a computational approach

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