Abstract
Abstract In the studied commercial pea protein isolate (PPI) some physicochemical modifications are induced in the protein structure during its processing. That fact would result into a reduction of proteins techno-functional properties. It has been evidenced by Differential Scanning Calorimetry the protein denaturation what gives as a result poor gelling ability. Microbial transglutaminase (MTGase) was added at different concentrations to improve the gelation process at two different settings/thermal treatments to make suitable texture PPI gels as a base for various meat and/or seafood analogues. SDS-PAGE analysis indicated that MTGase activity was focused on the polymerization of vicilins and legumins resulting in the promotion of new intermolecular protein complexes (increase in β-sheet aggregates). Rheological data showed that at 23% PPI with 5 and 7 U/g protein of MTGase the gel strength increased in terms of breaking force and complex modulus. It also improved the conformational stability and flexibility of their gel networks. The results suggest that appropriate gels with 23% PPI could be obtained adding 5 U/g MTGase able to be used as meat and/or seafood analogues.
Highlights
There is increasing consumer demand for convenient and healthy foodstuffs of vegetable origin
The studied pea protein isolate (PPI) had low fat content (0.5%), especially in comparison to other commercial pea isolates (3-11.7%) (Shand et al, 2007; Barac et al, 2015); these differences could be due to lipid-protein binding during protein extraction, causing lipid concentration in the pea isolates (Shand et al, 2007)
These authors reported that PPIs exhibit better gelation capacity at pH values close to neutral as it is in this case
Summary
There is increasing consumer demand for convenient and healthy foodstuffs of vegetable origin. Dried peas and other pulses are good sources of proteins, fibre, starch, vitamins and minerals. There are two main ways of obtaining pea protein isolate (PPI) by salt solubilization of the proteins, and by alkaline solubilization of proteins and further isoelectric precipitation. This last procedure is followed by the industry to obtain high yield of PPIs. This last procedure is followed by the industry to obtain high yield of PPIs This procedure induces some protein denaturation mainly unfolding reducing protein functionality (Shand et al, 2007)
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