Development of non-animal chicken fat using faba bean protein-based emulsion gels

Le résumé fourni par la source

Increasing awareness of the risks associated with overconsumption of saturated fats has focused attention on healthier fat replacers that can be incorporated into alternative protein foods as non-animal fat. A key technological challenge is in developing non-animal fats that are: (1) relatively high in melting point, (2) low in saturated fat, and (3) able to combine with proteins in a food matrix. In our study, protein-based emulsion gels (PEGs) consisting of faba bean protein concentrate, olive oil and water at different protein (7–10% w/w) and oil (40–60% w/w) concentrations, were created using high-pressure processing (HPP) technology. The PEGs were characterized and compared to chicken fatty deposits based on their appearance, color, oil-holding capacities, freeze-thaw stability, and rheological properties. We found that PEGs with lower protein concentrations, particularly 7% protein, 40% oil (7%P,40%O) exhibited the closest rheological properties and gel strength G’ (4465.07 ± 76.12 Pa) to chicken fatty deposits (2933.60 ± 763.21 Pa). PEGs with 10% protein had better long-term oil-holding capacities after the second freeze-thaw (for 10%P,60%O: 42.062 ± 0.530%), in comparison to chicken fat (45.362 ± 5.928%). Freeze-thaw treatments disrupted the stability of the PEG, signifying the importance of temperature control during gel storage and transportation. These results provide valuable insight into the effect of protein and oil concentrations on measured attributes in the PEGs. This will enable us to utilize PEGs to create and mimic animal fats such as chicken fat. • Plant protein-based emulsion gels (PEGs) with low saturated fat content were developed using high-pressure processing. • The PEGs could mimic chicken fat, providing higher melting points (>75 °C) and comparable rheological properties. • The PEGs had good oil-holding capacities but suffered structural instability after freeze-thaw storage conditions. • Modifications in PEG formulations and further processing of proteins may improve freeze-thaw stability.

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