Dados do Trabalho

Título

PROTEIN GELS CROSSLINKED WITH TRANSGLUTAMINASE FOR FOOD PROPOSALS

Introdução

Global population growth, which is expected to reach 10 billion people by 2050, and the increase in non-meat eaters are driving food industries to develop products rich in alternative proteins. Protein gels are structures that can be used to develop a wide range of food products. This study aimed to evaluate the effects of processing on the texture and microstructure of pea protein gels crosslinked with transglutaminase.

Material e Métodos

In treatment 1 (T1), 15% of pea protein and transglutaminase (0.5, 0.75, 1 or 1.25% TG) were mixed and heated at 50°C, placed in cylindrical molds and incubated for 30 min for crosslinking. Then, the temperature was raised to 80°C for an additional 30 min. In treatment 2 (T2), pea protein was heated at 80°C for 30 min. In the next step, the temperature was decreased to 50°C and transglutaminase was added. The solutions were placed in the molds and incubated for another 30 min. Samples were cooled overnight at 4°C for uniaxial compression analysis. Rheological measurements and confocal microscopy analysis were also performed.

Resultados e Discussão

Confocal microscopy confirmed that the enzyme promoted protein interactions in both treatments. However, in T1 these interactions were not enough to form a strong network, and no fracture stress could be observed during uniaxial compression analysis. In T2, more protein solubilization with network improvement was observed. The increase in transglutaminase concentration to 1% and 1.25% led to the formation of large protein agglomerates. Transglutaminase increased fracture stress in T2, which raised from 23.24 kPa to 27.15 kPa at 0.5% and 1.25% TG, respectively. However, samples became less deformable, decreasing from 0.96 at 0.5% TG to 0.7 at 1.25% TG. Tan δ confirmed that T2 gels had more elastic behavior than T1 gels and cooling the temperature did not modify the viscoelasticity.

Conclusão

Hence, T2 was more suitable for enhancing the texture of the gels, leading to a strong protein network improved with the highest transglutaminase concentration.