Browsing by Person "Moll, Pascal"

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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.
Homogenization improves foaming properties of insoluble pea proteins
(2022) Moll, Pascal; Salminen, Hanna; Griesshaber, Elena; Schmitt, Christophe; Weiss, Jochen
Foams are essential in many food applications and require surface-active ingredients such as proteins for formation and stabilization. We investigated the influence of high-pressure homogenization on foaming properties of insoluble pea protein dispersions (5% w/w) at pH 3 and 5. Unhomogenized insoluble pea protein dispersions did not foam at either pH 3 or 5, as they consisted of large insoluble pea protein aggregates with limited surface activity. At pH 3, the homogenized pea protein dispersions generated foams due to higher protein solubility and surface activity through disruption of large protein aggregates into smaller particles. The foam stability decreased with increasing homogenization pressure and number of cycles due to a reduction in continuous phase viscosity. At pH 5, the insoluble pea proteins foamed when the homogenization resulted in formation of aggregates made of smaller protein entities, which was the case for homogenization ≥ 100 MPa and three cycles. In general, the foam capacity (amount of formed foam) was higher at pH 3 due to improved protein solubility and surface activity that facilitated incorporation of air, while the foam stability (resistance against foam collapse) was better at pH 5 because of the presence of larger protein aggregates that formed thicker and more viscous films around the air bubbles benefitting retention of gas bubbles. Overall, homogenization improved the foaming properties of insoluble pea proteins at pH 3 and 5.
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.