Evaluation of pH, NaCl and CaCl2 salts on Solubility, Zeta Potential and air - water interfacial properties of the protein isolate from lupin seeds

IF 5.6 3区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY

Food Structure-Netherlands Pub Date : 2023-10-01 DOI:10.1016/j.foostr.2023.100350

Richard Marins da Silva, Márcia Cristina Teixeira Ribeiro Vidigal, Valéria Paula Rodrigues Minim, Luis Antonio Minim

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Abstract

Lupin is a legume seed rich in proteins and presents high nutritional and health benefits but is little used in the human diet. In this work, lupin proteins were extracted using an alkaline-saline solution followed by dialysis. Then, globulins were separated by isoelectric precipitation to give lupin globulin isolate (LGI). The solubility, zeta potential and interfacial properties of LGI were evaluated at pH of 3.4 and 6.8 in the presence of NaCl or CaCl₂. The solubility of LGI was dependent on the pH and type of salt, with lower solubility in the isoelectric region (pH ∼ 5), with lower solubility in the presence of NaCl (42.81 ± 1.23 %). The lowest value of interfacial tension was at pH 3.4 and absence of salts (41.79 ± 0.63 mN m⁻¹). Indicating the type of salt changes the electrostatic shielding of the LGI electrical double layer, which leads to a decrease in electrostatic potential at the surface of LGI. The rate of diffusion is highest at pH 6.8 under conditions without salts or in the presence of NaCl (0.57 ± 0.01 and 0.55 ± 0.05 mN m⁻¹ s^−0.5 respectively). When the salt was changed to CaCl₂ diffusion was decreased, probably due to protein-protein interactions. On the other hand, the protein adsorption rate is lower at pH 6.8 under all conditions studied. Apparently, it is influenced by the type of surface electrical charge of the proteins and the rate of rearrangement is greater than the rate of adsorption. The results obtained demonstrate that the lupin protein isolate can be used in multiphase food systems, such as foams, due to its interfacial properties.

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pH、NaCl和CaCl2盐对罗苹种子分离蛋白溶解度、Zeta电位和空气-水界面性质的影响

羽扇豆素是一种富含蛋白质的豆类种子，具有很高的营养和健康益处，但在人类饮食中很少使用。在这项工作中，羽扇豆蛋白是使用碱性盐水溶液提取的，然后进行透析。然后，通过等电沉淀分离球蛋白，得到羽扇豆球蛋白分离物（LGI）。在NaCl或CaCl2存在下，在pH为3.4和6.8时评估LGI的溶解度、ζ电位和界面性质。LGI的溶解度取决于pH值和盐的类型，在等电区（pH～5）的溶解度较低，在NaCl存在下的溶解度较小（42.81±1.23%）。界面张力的最低值是在pH 3.4和不存在盐的情况下（41.79±0.63 mN m−1）。表明盐的类型改变了LGI双电层的静电屏蔽，这导致LGI表面的静电电势降低。在无盐或NaCl存在的条件下，pH 6.8时的扩散速率最高（分别为0.57±0.01和0.55±0.05 mN m−1 s−0.5）。当盐变为CaCl2时，扩散减少，可能是由于蛋白质-蛋白质相互作用。另一方面，在所研究的所有条件下，在pH 6.8时蛋白质吸附率较低。显然，它受到蛋白质表面电荷类型的影响，重排速率大于吸附速率。所获得的结果表明，羽扇豆蛋白分离物由于其界面性质，可用于多相食品系统，如泡沫。

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来源期刊

Food Structure-Netherlands Chemical Engineering-Bioengineering

CiteScore

7.20

自引率

0.00%

发文量

期刊介绍： Food Structure is the premier international forum devoted to the publication of high-quality original research on food structure. The focus of this journal is on food structure in the context of its relationship with molecular composition, processing and macroscopic properties (e.g., shelf stability, sensory properties, etc.). Manuscripts that only report qualitative findings and micrographs and that lack sound hypothesis-driven, quantitative structure-function research are not accepted. Significance of the research findings for the food science community and/or industry must also be highlighted.