By Eben van Tonder, 24 April 2025
Introduction
In the processing of emulsified and restructured meat products, especially in lean and additive-light systems, seemingly small procedural variations can have a major impact on the final product’s performance. One such variation is the resting phase prior to cooking, a step often considered optional or omitted in fast-paced operations. This article examines the impact of resting reformed bacon on structural integrity, slicing performance, and yield, using a phosphate and hydrocolloid-based system, with no added starch.
These systems typically include functional ingredients such as triphosphates (E451) and gelling agents, which promote protein extraction, water binding, and gel formation. Resting allows these components time to interact and stabilise within the meat matrix. The result is a firmer, more cohesive product with improved post-freeze slicing quality and reduced cook loss.
Effect of Resting Before Cooking
| Parameter | Without Resting | With Overnight Rest (12 to 24 hours at 0 to 4°C) |
|---|---|---|
| Protein Binding | Moderate, reliant only on mechanical mixing | Stronger due to extended protein solubilisation and hydration |
| Texture Uniformity | Variability possible, risk of weak junctions | More consistent texture, better particle integration |
| Water Retention / Yield | Slightly lower, risk of purge during cook | Improved yield and water retention as proteins and hydrocolloids hydrate |
| Slicing Stability | May shear or crumble at edges, especially after freezing | Clean slicing with better edge integrity post-freeze |
| Appearance (Cut Face) | Minor voids or pitting possible | Dense, smooth appearance with fewer structural gaps |
| Cook Loss | Slightly higher | Lower cook loss due to a more cohesive protein and gel network |
| Ease of Demoulding | Some fragility after cooking | More solid and stable when removed from casing or mould |
Recommended Resting Practices
| Condition | Recommended Practice |
|---|---|
| Duration | 12 to 24 hours |
| Temperature | 0 to 4°C (never exceed 5°C) |
| Form | Rest in bacon moulds for best structure; alternatively, use firm 120 mm casings |
| Vacuum or Wrapping | Vacuum seal or wrap tightly to avoid oxidation and surface drying |
Discussion
The advantage of resting lies in the biochemical processes that continue after mixing but before heat is applied. Functional phosphates increase the solubility of myofibrillar proteins like myosin, allowing them to unfold and interact. During resting, these interactions deepen, creating a more stable matrix.
Gelling agents begin hydrating during the cold phase. Though they fully set upon heating, prehydration ensures uniform gel formation, reducing structural failure and water loss. Resting also promotes brine equilibration throughout the mass, reducing risk of localised over-saturation or purge.
For low-cook temperature systems where final internal temperature is held around 58°C, these factors become critical. The system relies entirely on gelation and protein interaction, with no added starch or gelatin to serve as backup. Resting effectively enhances these natural binding pathways.
Conclusion
Resting reformed bacon before cooking improves cohesion, slicing performance, and yield. It strengthens the internal protein network, enhances gel performance, and reduces variability between batches. For processors working at low internal cooking temperatures, especially without additional binders, this resting phase is highly beneficial.
Use of a bacon mould is recommended to enhance shaping and compactness, but even in standard casings, a tightly packed and chilled rest will offer noticeable advantages. This simple, cost-free step can elevate quality and consistency in even the most streamlined production systems.
References
Ahmed, J., Al-Salem, D., and Almusallam, A. A. (2012). Rheological properties of selected hydrocolloids as influenced by temperature and concentration. Food Hydrocolloids, 26(2), 365–372.
Food Additives and Contaminants (2005). Regulation and functional roles of carrageenan and Eucheuma-based polysaccharides in meat systems. Food Addit Contam, 22(11), 975–987.
Sárossy, Z., Tenkanen, M., Pitkänen, L., and Nordlund, E. (2018). Physical and chemical interactions between polysaccharides and proteins in meat analogues. Trends in Food Science and Technology, 75, 27–39.
Xiong, Y. L. (1997). Structure-function relationships of muscle proteins. In: Damodaran, S., Paraf, A. (Eds.), Food Proteins and Their Applications. New York: Marcel Dekker, pp. 341–392.