High moisture extrusion cooking of meat analogs: A review of mechanisms of protein texturization.

High-moisture extrusion cooking (HMEC) is an efficient method for converting proteins and polysaccharides into fibrous structure that is used in the industrial production of meat analogs. The purpose of this review is to systematically evaluate current knowledge regarding the modification of protein structure including denaturation and reassembly upon extrusion processing and to correlate this understanding to the structure of the final products. Although there is no consensus on the relative importance of a certain type of bond on extrudates' structure, literature suggests that, regardless of moisture level, these linkages and interactions give rise to distinctive hierarchical order. Both noncovalent and disulfide bonds contribute to the extrudates' fibrous structure. At high water levels, hydrogen and disulfide bonds play a dominant role in extrudates' texture. The process parameters including cooking temperature, screw speed, and moisture content have significant albeit different levels of impact on the texturization process. Their correlation with the ingredients' physiochemical properties provides a greater insight into the process-structure-function relationship of meat analogs. The tendency of protein and polysaccharide blends to phase separate rather than produce a homogeneous mix is a particularly important aspect that leads to the formation of fibrous layers when extruded. This review shows that systematic studies are required to measure and explain synergistic and competitive interactions between proteins and other ingredients such as carbohydrates with a focus on their incompatibility. The wide range of plant protein source can be utilized in the HMEC process to produce texturized products, including meat analogs.

Influence of Spacer Design and Module Geometry on the Filtration Performance during Skim Milk Microfiltration with Flat Sheet and Spiral-Wound Membranes.

Spacer design in spiral-wound membranes (SWMs) significantly affects the axial pressuredrop in the flow channel but also the deposit layer removal. However, the effects of the spacerdesign and feed flow distribution in the module on the filtration performance have not yet beeninvestigated during the highly fouling-susceptible fractionation of proteins from skim milk bySWMs. Therefore, a parallel spacer with no turbulence promotion and a less homogeneous feedflow distribution in the SWM was compared to a diamond spacer with regard to its impact ondeposit formation and filtration performance. The experiments were conducted in a flat sheet testcell and in SWMs. The parallel spacer induced a more homogeneous deposit layer formation.However, no difference in filtration performance could be observed in the experiments with the testcell. Even though deposit layer formation dominates the microfiltration, its amount and spatialdistribution could not be directly linked to the filtration performance. Furthermore, both spacerswere assessed in SWM. Despite the higher crossflow velocity applicable in the more open channelsof the parallel spacer, the performance of the parallel spacer was inferior to the diamond spacer.This was independent of the viscosity of the feed. Due to the high curvature of the membrane sheetsclose to the permeate collection tube, the cross-section of the flow channels in the SWM equippedwith the parallel spacer was reduced. This resulted in a distinctly lower deposit layer control andperformance, which could not be compensated by the resulting higher crossflow velocity far fromthe permeate collection tube.

Semi-quantitative, spatially resolved analysis of protein deposit layers on membrane surfaces.

Fouling distinctly reduces the filtration performance of membranes. A characterization of the fouling in membranes, however, is difficult due to its spatial distribution. Currently applied methods for deposit layer analysis are rather complex or do not offer a spatial resolution. Knowledge of the spatial distribution, however, could be used to improve the design of membranes, modules, and spacers. Staining with Coomassie Brilliant Blue, related to the staining of PAGE gels, is a simple method to visualize and analyze the deposited proteins semi-quantitatively. We improved an existing staining technique for protein deposits on membranes by adding a calibration for the semi-quantitative analysis and optimizing the sample handling. The method provides a spatially resolved analysis of deposited proteins up to a concentration of 10 g m-2. Apart from staining, data processing is described in order to generate false colors or topographic images of deposits. Thus, the paper describes a simple method to assess and visualize the influence of module characteristics such as spacer design on the spatially resolved protein fouling of polymeric and ceramic membranes. Therefore, the method can contribute to the improvement of the module design and processing conditions with regard to the filtration performance. •Visualization of proteinaceous deposits on membranes•Spatially resolved quantification of proteinaceous deposits.