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1.
Food Res Int ; 157: 111049, 2022 07.
Artigo em Inglês | MEDLINE | ID: mdl-35761514

RESUMO

Properties of powders produced from drying solute-containing droplets arise from the dynamic redistribution of solute during drying. While insights on the dynamic redistribution are instrumental for the rational design of powders and for the optimized operation of equipment such as spray dryers, experimental techniques that allow measuring the spatio-temporal concentration of solute in drying droplets are scarce. In this work, we explore and demonstrate the use of optical coherence tomography (OCT) to measure the spatio-temporal concentration of solute in drying droplets and the development of a solidifying shell at the liquid-air interface, using aqueous droplets of maltodextrin as a model system. This work provides a solid foundation for the use of OCT to quantify the dynamic redistribution of solute and link it to the development of the morphology of the produced particles and agglomerates.


Assuntos
Dessecação , Tomografia de Coerência Óptica , Dessecação/métodos , Tamanho da Partícula , Polissacarídeos , Pós , Soluções
2.
Food Res Int ; 120: 449-455, 2019 06.
Artigo em Inglês | MEDLINE | ID: mdl-31000261

RESUMO

During gastric digestion, hydrolysis of proteins by pepsin contributes largely to the breakdown of protein-rich food. We hypothesized that the effect of pepsin is limited by its diffusivity, which is co-determined by the food structure and the local pH in the food during digestion. To investigate the principle mechanism of enzyme diffusion in food matrices, we used enhanced green fluorescent protein (EGFP) as probe to study the diffusivity of proteins in whey protein isolate gels, using fluorescence correlation spectroscopy (FCS). Gels made with different ionic strength showed distinctive elastic moduli but did not show differences in diffusivity of EGFP. Some models for diffusion in hydrogels yield good description of the obtained data, and can approximate the enzyme diffusion in diverse food matrices. However, the enzyme pepsin is more complicated than the probe EGFP, to yield more accurate predictions, electrostatic and enzyme-substrate interaction also need to be considered.


Assuntos
Proteínas de Fluorescência Verde , Hidrogéis/química , Modelos Químicos , Proteínas do Soro do Leite , Difusão , Digestão , Proteínas de Fluorescência Verde/análise , Proteínas de Fluorescência Verde/química , Proteínas de Fluorescência Verde/metabolismo , Pepsina A , Espectrometria de Fluorescência , Proteínas do Soro do Leite/análise , Proteínas do Soro do Leite/química , Proteínas do Soro do Leite/metabolismo
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