Comparison of Colorimetric Methods for Measuring the Solubility of Legume Proteins.

Increasing the use of plant proteins in foods requires improving their physical and chemical properties, such as emulsification, gelation capacity, and thermal stability. These properties determine the acceptability and functionality of food products. Higher protein solubility significantly impacts these properties by affecting denaturation and the stability of emulsifiers or gels.

Enzymatic hydrolysis of soy and chickpea protein with Alcalase and Flavourzyme and formation of hydrogen bond mediated insoluble aggregates.

Food applications involving plant proteins require modification of their functionality to mimic the unique properties of animal proteins. Enzymatic hydrolysis is commonly used to alter the functionality of plant proteins, particularly to improve their solubility near the isoelectric point. Current methodological approaches mostly indicate improved solubility upon hydrolysis.

Pulse protein processing: The effect of processing choices and enzymatic hydrolysis on ingredient functionality.

Plant-based protein ingredients are an emerging solution to the environmental and health issues associated with animal-based proteins. Pulses have become a promising source of these plant-based ingredients. In order to produce functional proteins from pulse grains, extensive processing must be conducted to extract their proteins.

Transcriptional Dynamics of Cultured Human Villous Cytotrophoblasts.

During human pregnancy, cytotrophoblasts (CTBs) play key roles in uterine invasion, vascular remodeling, and anchoring of the feto-placental unit. Due to the challenges associated with studying human placentation in utero, cultured primary villous CTBs are used as a model of the differentiation pathway that leads to invasion of the uterine wall. In vitro, CTBs emulate in vivo cell behaviors, such as migration, aggregation, and substrate penetration.