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 , r = 2:1, pH 6) was investigated upon heating, and upon addition of calcium, transglutaminase, and laccase, or by combinations thereof.

Comparison of Binding Properties of a Laccase-Treated Pea Protein-Sugar Beet Pectin Mixture with Methylcellulose in a Bacon-Type Meat Analogue.

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% / solids, pH 6) with and without laccase addition and a methylcellulose hydrogel (6% /) serving as benchmark were applied as binder between textured protein and a fat mimetic.

Homogenization improves foaming properties of insoluble pea proteins.

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.

Use of molecular interactions and mesoscopic scale transitions to modulate protein-polysaccharide structures.

Mixed protein-polysaccharide structures have found widespread applications in various fields, such as in foods, pharmaceuticals or personal care products. A better understanding and a more precise control over the molecular interactions between the two types of macromolecules leading to an engineering of nanoscale and colloidal building blocks have fueled the design of novel structures with improved functional properties. However, these building blocks often do not constitute the final matrix.

Primary resistance mechanism of the canine distemper virus fusion protein against a small-molecule membrane fusion inhibitor.

Morbilliviruses (e.g. measles virus [MeV] or canine distemper virus [CDV]) employ the attachment (H) and fusion (F) envelope glycoproteins for cell entry.