Comparison of Thermal and High-Pressure Gelation of Potato Protein Isolates

Understanding aggregation in food protein systems is essential to control processes ranging from the stabilization of colloidal dispersions to the formation of macroscopic gels. Patatin rich potato protein isolates (PPI) have promising techno-functionality as alternatives to established proteins from egg white or milk. In this work, the influence of pH and temperature on the kinetics of PPI denaturation and aggregation was investigated as an option for targeted functionalization. At a slightly acidic pH, rates of denaturation and aggregation of the globular patatin in PPI were fast. These aggregates were shown to possess a low amount of disulfide bonds and a high amount of exposed hydrophobic amino acids (S0). Gradually increasing the pH slowed down the rate of denaturation and aggregation and alkaline pH levels led to an increased formation of disulfide bonds within these aggregates, whereas S0 was reduced. Aggregation below denaturation temperature (Td) favored aggregation driven by disulfide bridge formation. Aggregation above Td led to fast unfolding, and initial aggregation was less determined by disulfide bridge formation. Inter-molecular disulfide formation occurred during extended heating times. Blocking different protein interactions revealed that the formation of disulfide bond linked aggregation is preceded by the formation of non-covalent bonds. Overall, the results help to control the kinetics, morphology, and interactions of potato protein aggregation for potential applications in food systems.

Section: Methodssupporting

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins

Andlinger

Röscheisen

Hengst

et al. 2021

“…It consists of the majority from patatin and has a low thermal denaturation temperature (55–75 °C) at which it forms a gel network [ 154 ]. Thermally formed gels from potato protein isolates were obtained at pH 3 and pH 7 with minimal gelation temperatures around 45–50 °C [ 155 ], which can be beneficial for applications where a low temperature is required. However, similar to the rest of the proteins, potato protein properties can change with the use of different protein isolation methods [ 156 ] or post-treatment modification using enzymes [ 157 ].…”

Section: Plant-based Ingredients For Meat Analoguesmentioning

confidence: 99%

Functionality of Ingredients and Additives in Plant-Based Meat Analogues

Kyriakopoulou

Keppler

Goot

2021

318

211

Meat analogue research and development focuses on the production of sustainable products that recreate conventional meat in its physical sensations (texture, appearance, taste, etc.) and nutritional aspects. Minced products, like burger patties and nuggets, muscle-type products, like chicken or steak-like cuts, and emulsion products, like Frankfurter and Mortadella type sausages, are the major categories of meat analogues. In this review, we discuss key ingredients for the production of these novel products, with special focus on protein sources, and underline the importance of ingredient functionality. Our observation is that structuring processes are optimized based on ingredients that were not originally designed for meat analogues applications. Therefore, mixing and blending different plant materials to obtain superior functionality is for now the common practice. We observed though that an alternative approach towards the use of ingredients such as flours, is gaining more interest. The emphasis, in this case, is on functionality towards use in meat analogues, rather than classical functionality such as purity and solubility. Another trend is the exploration of novel protein sources such as seaweed, algae and proteins produced via fermentation (cellular agriculture).

“…The low denaturation temperature of patatin, one of the main potato protein fractions, may be partially responsible for this. The denaturation temperature is roughly 20 °C lower compared to common food proteins as ovalbumin (egg) or soy glycinin [ 33 , 34 ]. Figure 1 reveals no significant difference between G ’76°C,suspension of the egg white protein and G’ 76°C,suspension of soy concentrate, indicating good gelation characteristics of the latter.…”

Section: Resultsmentioning

confidence: 99%

Phosphate Elimination in Emulsified Meat Products: Impact of Protein-Based Ingredients on Quality Characteristics

Goemaere

Glorieux

Govaert

et al. 2021

The addition of phosphates to meat products improves the emulsifying and gelling properties of meat proteins, in turn enhancing overall product quality. The current market trend towards additive-free products and the health issues related to phosphate challenge the industry to develop phosphate-free meat products. The aim of this study was to evaluate the potential of seven protein-based ingredients (pea, blood plasma, gelatin, soy, whey, egg, and potato) to remediate quality losses of emulsified meat products (cooked sausages) upon phosphate elimination. First, the intrinsic gelling and emulsifying characteristics of the proteins were assessed. Next, the proteins were added to phosphate-free sausages, of which quality characteristics during production (viscoelastic behavior and emulsion stability) and of the final products (texture, cooking loss, and pH) were screened. Blood plasma and soy were superior in phosphate-free cooked sausages, as no significant differences in hardness, cooking yield, or stability were found compared to phosphate-containing sausages. Egg and pea also improved the previously mentioned quality characteristics of phosphate-free sausages, although to a lesser extent. These insights could not entirely be explained based on the intrinsic gelling and emulsifying capacity of the respective proteins. This indicated the importance of a well-defined standardized meat matrix to determine the potential of alternative proteins in meat products.