Unknown

Dataset Information

0

Data on the characterization of native soy globulin by SDS-Page, light scattering and titration.


ABSTRACT: The data presented in this article are related to the research article entitled Structure of Self-assembled Native Soy Globulin in Aqueous Solution as a Function of the Concentration and the pH by N. Chen, M. Zhao C. Chassenieux, T. Nicolai (2016) [1]. Please refer to this article for interpretation of the data. The protein composition of soy protein isolate (SPI) was characterized by SDS-Page. The molar mass of native soy globulin aggregates formed at different protein concentrations was determined by light scattering as a function of the waiting time. The dependence of the pH on the net charge density of native soy globulins was determined for solutions containing 5 g/L or 2 g/L SPI.

SUBMITTER: Chen N 

PROVIDER: S-EPMC5096597 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Data on the characterization of native soy globulin by SDS-Page, light scattering and titration.

Chen Nannan N   Zhao Mouming M   Chassenieux Christophe C   Nicolai Taco T  

Data in brief 20161025


The data presented in this article are related to the research article entitled <i>Structure of Self-assembled Native Soy Globulin in Aqueous Solution as a Function of the Concentration and the pH</i> by N. Chen, M. Zhao C. Chassenieux, T. Nicolai (2016) [1]. Please refer to this article for interpretation of the data. The protein composition of soy protein isolate (SPI) was characterized by SDS-Page. The molar mass of native soy globulin aggregates formed at different protein concentrations was  ...[more]

Similar Datasets

| S-EPMC10712055 | biostudies-literature
| S-EPMC7717971 | biostudies-literature
| S-EPMC6988229 | biostudies-literature
| S-EPMC10969193 | biostudies-literature
| S-EPMC2644111 | biostudies-literature
| S-EPMC6992818 | biostudies-literature
2011-04-15 | PRD000092 | Pride
| S-EPMC2077256 | biostudies-literature
| S-EPMC6218646 | biostudies-literature
| S-EPMC10639126 | biostudies-literature