Solidification of concentrated pea protein-pectin mixtures as potential binder.

BACKGROUND: Binders in plant-based meat analogues allow different components, such as extrudate and fat particles, to stick together. Typically, binders then are solidified to transform the mass into a non-sticky, solid product. As an option for a clean-label binder possessing such properties, the solidification behavior of pea protein-pectin mixtures (250 g kg-1 , r = 2:1, pH 6) was investigated upon heating, and upon addition of calcium, transglutaminase, and laccase, or by combinations thereof. RESULTS: Mixtures of (homogenized) pea protein and apple pectin had higher elastic moduli and consistency coefficients and lower frequency dependencies upon calcium addition. This indicated that calcium physically cross-linked pectin chains that formed the continuous phase in the biopolymer matrix. The highest degree of solidification was obtained with a mixture of pea protein and sugar beet pectin upon addition of laccase that covalently cross-linked both biopolymers involved. All solidified mixtures lost their stickiness. A mixture of soluble pea protein and apple pectin solidified only slightly through calcium and transglutaminase, probably due to differences in the microstructural arrangement of the biopolymers. CONCLUSION: The chemical makeup of the biopolymers and their spatial distribution determines solidification behavior in concentrated biopolymer mixtures. In general, pea protein-pectin mixtures can solidify and therefore have the potential to act as binders in meat analogues. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

Comparison of the functional properties of RuBisCO protein isolate extracted from sugar beet leaves with commercial whey protein and soy protein isolates.

BACKGROUND: RuBisCO was extracted from sugar beet leaves using soft and food-compatible technologies. Proximate composition, solubility, emulsifying, foaming and gelling properties of the protein isolate were determined. All these properties were systematically benchmarked against commercial whey and soy protein isolates used in food applications. RESULTS: RuBisCO protein isolate (RPI) contained 930 g kg-1 of crude protein. Protein solubility was higher than 80% at pH values lower than 4.0 or higher than 5.5. Foaming capacity of RPI was better at pH 4.0 than at pH 7.0. Interestingly, 10 g kg-1 protein foams were more stable (pH 7.0 and 4.0) than foams obtained with whey or soy protein. Moreover, 10 g kg-1 RPI emulsions at pH 4.0 or 7.0 exhibited good stability, being similar to whey protein isolate. Remarkable gelling properties were observed at pH 7.0, where 50 g kg-1 protein solutions of RPI formed self-supporting gels while more concentrated solutions were needed for whey or soy protein. CONCLUSION: RuBisCO showed comparable or superior functional properties to those of currently used whey and soy protein isolates. These results highlight the high potential of sugar beet leaf protein isolate as a nutritious and functional food ingredient to face global food security and protein supply. © 2018 Society of Chemical Industry.