Browsing by Subject "Pea protein"

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Comparison of binding properties of a laccase-treated pea protein-sugar beet pectin mixture with methylcellulose in a bacon-type meat analogue
(2022) Moll, Pascal; Salminen, Hanna; Stadtmueller, Lucie; Schmitt, Christophe; Weiss, Jochen
A bacon-type meat analogue consists of different structural layers, such as textured protein and a fat mimetic. To obtain a coherent and appealing product, a suitable binder must glue those elements together. A mixture based on pea protein and sugar beet pectin (r = 2:1, 25% w/w solids, pH 6) with and without laccase addition and a methylcellulose hydrogel (6% w/w) serving as benchmark were applied as binder between textured protein and a fat mimetic. A tensile strength test, during which the layers were torn apart, was performed to measure the binding ability. The pea protein–sugar beet pectin mixture without laccase was viscoelastic and had medium and low binding strength at 25 °C (F ≤ 3.5 N) and 70 °C (F ≈ 1.0 N), respectively. The addition of laccase solidified the mixture and increased binding strength at 25 °C (F ≥ 4.0 N) and 70 °C (F ≈ 2.0 N), due to covalent bonds within the binder and between the binder and the textured protein or the fat mimetic layers. Generally, the binding strength was higher when two textured protein layers were glued together. The binding properties of methylcellulose hydrogel was low (F ≤ 2.0 N), except when two fat mimetic layers were bound due to hydrophobic interactions becoming dominant. The investigated mixed pectin–pea protein system is able serve as a clean-label binder in bacon-type meat analogues, and the application in other products seems promising.
Solidification of concentrated pea protein–pectin mixtures as potential binder
(2023) Moll, Pascal; Salminen, Hanna; Stadtmüller, Lucie; Schmitt, Christophe; Weiss, Jochen
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 solidi- ﬁed 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.
Upscaling of alkaline pea protein extraction from dry milled and pre-treated peas from laboratory to pilot scale: Optimization of process parameters for higher protein yields
(2022) Schmidt, Florian; Blankart, Max; Wanger, Janina; Scharfe, Markus; Scheuerer, Theresa; Hinrichs, Jörg
The upscaling of pea protein extraction from laboratory scale with a centrifuge to pilot scale with a decanter centrifuge was investigated, and the pea protein extraction efficiency from dry milled and pre-treated peas was compared. Upscaling from laboratory to pilot scale is possible since starch was under the limit of detection (< 0.5%). The protein banding pattern of a sodium-dodecyl-sulfate polyacrylamide gel electrophoresis confirmed that albumins and globulins were extracted by alkali extraction. Protein yield increased from 59.5% to 67.1% for dry milled peas due to constant and quick discharge of dry matter in the decanter centrifuge. For pre-treated peas, the protein yield increased from 60.3% to 94.3%, which is explained by an improved cutting and improved separation in pilot scale compared to laboratory scale. The impact of acceleration, mass flow, differential speed and their respective interactions in the decanting process was determined with a design of experiments. For dry milled peas, only the mass flow exceeded the significance level. However, a mass flow of 5 kg h −1 , an acceleration of 1000 g ×and a differential speed of 50 min −1 led to the highest protein yield of 75.6%. The obtained protein yields for the pre-treated peas were in the range of 83 to 96% and therefore did not show significant differences in protein yield.