The compact protein revolution

The demand for high-quality protein in ready-to-drink formats keeps accelerating. In recent years, protein waters have grown rapidly as refreshing, convenient protein sources post-exercise. And with new trends - including GLP 1-mediated weight management - the market increasingly looks for concentrated protein delivery in compact formats. High protein shots meet that demand: delivering 20–25 grams of protein and over 3 grams of leucine in just 100 mL (3.4 fl. oz).

However, not every protein is suited for such concentrated applications. At these concentrations, many proteins increase viscosity, precipitate, sediment, or cause an unpleasant mouthfeel. To succeed, and in addition to excellent nutritional quality, a protein needs to offer minimal viscosity and full solubility even at extremely high loads.

This is where β-lactoglobulin (BLG) - the primary whey protein - excels. With advances in precision fermentation, fermentation-derived BLG offers even more advantages for beverage developers: purity, lactose-free, predictable functionality, and animal-free production - with superior nutritional quality to milk-derived whey protein isolate. These ingredient characteristics can be optimally leveraged in BLG shots.  

Formulating high-protein shots: solubility at the core

The formulation process begins with hydrating and solubilizing pre-acidified BLG. Thanks to its excellent solubility, concentrations up to 25% protein can be achieved without the viscosity typically seen in other protein sources (Fig. 1). This allows the creation of protein shots 25g with a smooth, drinkable mouthfeel — learn more about strategies for achieving high protein concentrations in beverages. After hydration, the pH is fine-tuned — typically between 3.2 and 3.8 — balancing microbial stability with a refreshing tartness that suits fruit flavors.  The formulation is then completed with natural, clean label sweeteners, colors, and flavors which are a key consideration for U.S. consumers seeking natural, simple and recognizable ingredients.

At these protein loads, two properties make BLG shots unique:

• Low viscosity: Even at 20–25% protein, BLG remains drinkable.

• Low turbidity: BLG stays fully solubilized at low pH, avoiding sedimentation during shelf life.

Compare this to plant proteins or less purified whey proteins, which often struggle with grittiness, cloudiness or solubility issues at such levels.
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Figure 1 Viscosity comparison between Vivitein™ BLG, pea protein isolate (PPI) and faba bean protein isolate (FBPI) at 10 wt. % protein, showing the minimal viscosity contribution of β-lactoglobulin in water

‍Preserving shelf life without heat

Once formulated, microbiological safety and shelf life become critical. Despite Vivitein™ BLG having superior heat stability compared to other milk derived whey proteins, thermal pasteurization is generally not suitable: heating such high protein concentrations leads to denaturation and gelation (McSwiney et al., 1994; Pan et al., 2025).

Two non-thermal preservation routes dominate in BLG shots: ‍

Cold-fill with preservatives

• The shots can be cold-filled under sanitary – preferably aseptic – conditions, then preserved with additives such as potassium sorbate or sodium benzoate ​(Battey et al., 2002)​, or natural preservatives (e.g., mushroom extract). At the appropriate pH, sorbate effectively inhibits yeast and mold growth, extending shelf life. This method is cost-effective, scalable, and easily implemented for smaller operations.
• The trade-off: preservatives appear on labels, may subtly affect taste, and do not fully eliminate microbial risk if filling hygiene is not excellent. However, with proper control of pH and hygiene, cold-fill with preservatives remains a highly viable commercial approach for high-protein BLG shots.   

High pressures processing (HPP)

HPP applies extreme pressures (400 – 600 MPa) to sealed bottles, substantially reducing microbial load without heat. While part of the protein unfolds as a result of HPP ​(Dumay et al., 1994)​, the treatment does preserves both solubility and a fresh flavor and color (no cooking effect). For acidified BLG shots (pH ~3.5), HPP synergizes well: low pH suppresses spores while HPP handles vegetative cells ​(Nema et al., 2022)​.  

Importantly, BLG remains uniquely stable under HPP, even at high protein concentrations. In contrast, conventional whey protein isolates (which contain other whey proteins such as α-lactalbumin and immunoglobulins) were found much more prone to aggregation and gelation upon HPP treatment. This makes Vivitein™ BLG particularly suited for high-protein HPP-stabilized BLG shots – combining microbial safety with excellent physical stability and clarity (NTU < 5).

HPP does require dedicated equipment and batch processing, but offers clean-label, additive-free preservation – highly attractive for premium, label conscious brands.

Physical stability and sensory performance

Perhaps the most striking advantage of BLG in protein shots is its physical stability and sensory contribution at extreme concentrations. At high protein loads (up to 25%), it stands out for its superior functionality and drinkability:

Minimal viscosity  

Even at 25% protein, viscosity remains water-like, with less than 10 mPa∙s in cold-fill applications, enabling protein shots that are easy to drink, pour, and bottle, without the thick mouthfeel typical of high-protein formats.

No sedimentation 

BLG stays fully solubilized throughout shelf life, maintaining a consistent appearance and mouthfeel.

Clean sourness profile  

Acidified BLG allows for a right level of sourness even at low pH values, ideal for fruity flavor formulations such as citrus, berry and tropical.

Clear appearance

BLG allows for clear beverages – a sharp contrast to traditional milky or cloudy protein drinks.

In comparison with conventional whey protein isolates, where additional proteins often contribute to more turbidity and heavier flavors, BLG offers a cleaner and clearer profile

Driving innovation in high-density protein nutrition

Vivitein™ BLG combines the proven nutritional strengths of BLG with next-generation ingredient technology: sustainable production, high purity and consistent functionality. The market for small-format, high-dose protein shots is rapidly expanding, driven by both performance and health-oriented consumers.

By leveraging innovative processing – either HPP or cold fill with the right preservatives – beverage developers can deliver safe, clean-label, highly-concentrated protein shots a with a shelf life of 1-2 years.

As the market evolves, ingredients like Vivitein™ BLG are helping developers meet rising demand for compact, refreshing, and high-protein formats — beyond the thick, milky shakes that have long dominated the protein category.

Ready to formulate your next-generation BLG shot? Contact us for samples or formulation support here.

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References

​​Battey, A. S., Duffy, S., & Schaffner, D. W. (2002). Modeling Yeast Spoilage in Cold-Filled Ready-To-Drink Beverages with Saccharomyces cerevisiae, Zygosaccharomyces bailii, and Candida lipolytica. Applied and Environmental Microbiology, 68(4), 1901–1906. https://doi.org/10.1128/AEM.68.4.1901-1906.2002

​Dumay, E. M., Kalichevsky, M. T., & Cheftel, J. C. (1994). High-Pressure unfolding and aggregation of beta-lactoglobulin and the baroprotective effects of sucrose. Journal of Agricultural and Food Chemistry, 42(9), 1861–1868. https://doi.org/10.1021/jf00045a006

​McSwiney, M., Singh, H., & Campanella, O. H. (1994). Thermal aggregation and gelation of bovine β-lactoglobulin. Food Hydrocolloids, 8(5), 441–453. https://doi.org/10.1016/S0268-005X(09)80087-8

​Nema, P. K., Sehrawat, R., Ravichandran, C., Kaur, B. P., Kumar, A., & Tarafdar, A. (2022). Inactivating Food Microbes by High-Pressure Processing and Combined Nonthermal and Thermal Treatment: A Review. Journal of Food Quality, 2022, 1–27. https://doi.org/10.1155/2022/5797843

​Pan, Z., Kornet, R., Hewitt, S., Welman, A., Hill, J. P., Wubbolts, M., Mitchell, S., McNabb, W. C., Ye, A., Acevedo-Fani, A., & Anema, S. G. (2025). Heat-set gelation of milk- and fermentation-derived β-lactoglobulin variants. Food Hydrocolloids, 165, 111192. https://doi.org/10.1016/j.foodhyd.2025.111192