Gelation of faba bean concentrate processed by dry fractionation

ANTONIO, GUERRERO; JESSICA, PEREZ; ISMAEL, SANTANA; SCIAMMARO, LEONARDO P.; CARLOS, BENGOECHEA RUIZ; PUPPO, MARÍA CECILIA

Lisbon

Congreso; IBERHEO 2024, The Iberian Meeting on Rheology; 2024

Instituto Superior de Agronomia

Dry fractionation of faba bean meal involves air classification, or densification to separatetheir components, where the light fraction provides a protein concentrate. It is a sustainableprocess that avoids the use of solvents and minimizes functional and chemical changes ofthe protein [1]. Fava bean concentrate contains globulins, being the main storage proteins,and albumins, rich in essential amino acids. Understanding the gelling behavior of theseproteins is key to exploiting their functional properties in food formulation and productdevelopment, allowing for the creation of a wide range of textures and nutritional profiles.Unfortunately, despite the abundance of plant proteins globally, their gelling properties areless explored compared to animal proteins [2].The objective of this study was to evaluate rheological, textural and hydration propertiesof gels formulated at different protein contents and pH. A faba bean concentrate (FBC) of60% protein produced by a dry fractionation method, was used (HerbaPRO FB65,Seville, Spain). FBC was dispersed in distilled water at different protein contents (10, 12,14%) and pHs (2, 3, 5, 6, 8). Gelation of dispersions was analyzed in situ in the linearregion (using a Discovery Hybrid Rheometer DHR-3, geometry: 40 mm parallel plate) bytemperature ramps (25 to 95 ºC) and frequency sweeps before and after thermal treatment.Texture (TPA) and water holding capacity of gels prepared in a water bath (95ºC-30 min),cooled and stored (4ºC-24 h) were characterized. Heating increased viscoelastic properties,mainly at high protein contents, and cooling reinforced gel structures. An acid-inducedgelation before heating was detected at pH 2 (low E”/E’) but the 14%-pH 5 gel presentedthe highest reinforced structure. Soft cohesive gels (TPA) at 14%-pH 8 were obtained. Thepotential use of these proteins in human plant-based foods was highlighted.