利用大豆蛋白纤维聚集体(soy protein isolate fibril,SPIF)制备Pickering乳液,并研究其对β-胡萝卜素的包埋稳定性。结果表明,大豆分离蛋白(soy protein isolated,SPI)经酸热处理可以生成含大量β-折叠结构的SPIF,其乳化活性可达到14.3...利用大豆蛋白纤维聚集体(soy protein isolate fibril,SPIF)制备Pickering乳液,并研究其对β-胡萝卜素的包埋稳定性。结果表明,大豆分离蛋白(soy protein isolated,SPI)经酸热处理可以生成含大量β-折叠结构的SPIF,其乳化活性可达到14.38 m~2/g,乳化稳定性可达到88.72%,均显著高于SPI。利用SPIF剪切乳化制备Pickering乳液,发现NaCl浓度未超过600 mmol/L时,随着其浓度的增加,SPIF乳液界面蛋白吸附率增加,从而使Pickering乳液稳定性提高。同时,SPIF乳液对β-胡萝卜素的包埋率可达到98.79%。当NaCl浓度为600 mmol/L时,SPIF形成的Pickering乳液中β-胡萝卜素在贮藏第7天的保留率达到最大值81.46%,相比SPI乳液提高了13.24%。展开更多
A thorough understanding of how proteins induce nanoparticle （NP） aggregation is crucial when designing in vitro and in vivo assays and interpreting experimental results. This knowledge is also crucial when developi...A thorough understanding of how proteins induce nanoparticle （NP） aggregation is crucial when designing in vitro and in vivo assays and interpreting experimental results. This knowledge is also crucial when developing nano-applications and formulation for drug delivery systems. In this study, we found that extraction of immunoglobulin G （IgG） from cow serum results in lower polystyrene NPs aggregation. Moreover, addition of isolated IgG or fibrinogen to fetal cow serum enhanced this aggregation, thus demonstrating that these factors are major drivers of NP aggregation in serum. Counter-intuitively, NP aggregation was inversely dependent on protein concentration; i.e., low protein concentrations induced large aggregates, whereas high protein concentrations induced small aggregates. Protein-induced NP aggregation and aggregate size were monitored by absorbance at 400 nm and dynamic light scattering, respectively. Here, we propose a mechanism behind the protein concentration dependent aggregation; this mechanism involves the effects of multiple protein interactions on the NP surface, surface area limitations, aggregation kinetics, and the influence of other serum proteins.展开更多
文摘利用大豆蛋白纤维聚集体(soy protein isolate fibril,SPIF)制备Pickering乳液,并研究其对β-胡萝卜素的包埋稳定性。结果表明,大豆分离蛋白(soy protein isolated,SPI)经酸热处理可以生成含大量β-折叠结构的SPIF,其乳化活性可达到14.38 m~2/g,乳化稳定性可达到88.72%,均显著高于SPI。利用SPIF剪切乳化制备Pickering乳液,发现NaCl浓度未超过600 mmol/L时,随着其浓度的增加,SPIF乳液界面蛋白吸附率增加,从而使Pickering乳液稳定性提高。同时,SPIF乳液对β-胡萝卜素的包埋率可达到98.79%。当NaCl浓度为600 mmol/L时,SPIF形成的Pickering乳液中β-胡萝卜素在贮藏第7天的保留率达到最大值81.46%,相比SPI乳液提高了13.24%。
文摘A thorough understanding of how proteins induce nanoparticle （NP） aggregation is crucial when designing in vitro and in vivo assays and interpreting experimental results. This knowledge is also crucial when developing nano-applications and formulation for drug delivery systems. In this study, we found that extraction of immunoglobulin G （IgG） from cow serum results in lower polystyrene NPs aggregation. Moreover, addition of isolated IgG or fibrinogen to fetal cow serum enhanced this aggregation, thus demonstrating that these factors are major drivers of NP aggregation in serum. Counter-intuitively, NP aggregation was inversely dependent on protein concentration; i.e., low protein concentrations induced large aggregates, whereas high protein concentrations induced small aggregates. Protein-induced NP aggregation and aggregate size were monitored by absorbance at 400 nm and dynamic light scattering, respectively. Here, we propose a mechanism behind the protein concentration dependent aggregation; this mechanism involves the effects of multiple protein interactions on the NP surface, surface area limitations, aggregation kinetics, and the influence of other serum proteins.
