Reformulating protein beverages: Thermal stability and amino acid profiles drive next-generation functional sodas
The protein beverage market is undergoing a significant reformulation, with manufacturers seeking ingredients that can deliver high protein content without compromising clarity, taste, or processing efficiency. Arla Foods Ingredients’ Lacprodan® BLG-100, a pure beta-lactoglobulin ingredient, addresses key technical challenges in protein soda development through its heat-stable formulation and enhanced amino acid profile. Callan Emery speaks to Sebastian Braad Poulsen, Application Scientist, Arla Foods Ingredients, about the molecular characteristics that enable water-like viscosity in clear protein beverages, the manufacturing advantages of thermal stability across various processing methods, and how the ingredient’s leucine content supports the growing sports nutrition segment.
Food Engineering & Ingredients: Protein Soda: Your data shows nearly 20% of consumers have reduced traditional carbonated beverage intake in the past year. How is Arla Foods Ingredients’ Lacprodan BLG-100 positioned to capture this emerging “functional soda” market segment, and what manufacturing advantages does your heat-stable formulation offer processors looking to pivot their production lines?
Sebastian Braad Poulsen: Arla Foods Ingredients’ protein soda concept aligns with the “better for you” soft drinks trend. It provides 10g of high-quality, complete protein per serving from Lacprodan® BLG-100, our pure beta-lactoglobulin ingredient. This offers a refreshing, water-like quality, clarity and clean taste, with zero sugar and no lactose, enabling brands to set a new quality standard for protein-enriched functional sodas. Lacprodan® BLG-100 beverages can be processed using various heating methods, including pasteurization, high-temperature-short time (HTST pasteurization), retort, and tunnel pasteurization. This wide range of processing options enables manufacturers not currently working with proteins to diversify and expand their portfolio into a broad, fast-growing market without additional investments in heat-treatment equipment.
FEI: Clear Protein: The challenge of maintaining protein clarity in beverages has historically plagued formulators. Can you explain the specific molecular characteristics of Lacprodan BLG-100 that enable water-like viscosity while delivering 10g of protein per serving, and how this compares to standard whey protein performance metrics?
SBP: Lacprodan® BLG-100 is a highly specialized whey-derived ingredient, produced using a patented technology. Unlike standard whey proteins, which contain a mix of all major whey fractions, Lacprodan® BLG-100 is composed of pure beta-lactoglobulin – one distinct whey protein. This delivers unique advantages, offering higher levels of leucine, EAAs, and BCAAs for enhanced nutritional value, while also enabling an extremely clean taste, low turbidity and low viscosity across applications.
FEI: Amino Acids: You highlight enhanced essential and branched-chain amino acid content in BLG-100 compared to standard whey. What specific amino acid concentrations are we talking about, and how do these translate into measurable performance benefits for consumers in sports nutrition applications?
SBP: Beta-lactoglobulin is the key component that makes whey protein such a powerful protein source for promoting muscle growth and maintenance. It is already on its way to widespread recognition among sportspeople who take their nutrition seriously, with premium whey protein blends often listing it.
Our Lacprodan® BLG-100 is a pure ingredient, enabling the development of entirely new and more effective protein supplement products. It boasts an unbeatable nutritional profile compared to currently available whey protein, with a higher essential amino acid content – including branched-chain amino acids – compared to standard whey. It is naturally high in leucine, which is scientifically substantiated to support muscle maintenance and growth. Leucine plays a critical role in stimulating muscle protein synthesis (MPS), primarily through its activation of the mTORC1 pathway, the master regulator responsible for driving muscle growth and protein assembly.
FEI: Processing: With protein sodas requiring both hot and cold processing compatibility, how does Lacprodan BLG-100’s thermal stability translate into real-world manufacturing efficiency gains? What processing specifications can manufacturers expect when integrating this ingredient into existing beverage lines?
SBP: Lacprodan® BLG-100 is suitable for both hot and cold processing in the production of protein sodas. It can be processed using a variety of heating methods, including pasteurization, HTST pasteurization, retort, and tunnel pasteurization. This versatility makes it an attractive option for manufacturers looking to enter the functional soda market without the need for additional heat treatment equipment. Moreover, cold processing lines require lower initial capital and operational expenditures (OPEX) compared to hot processing, making it easier to expand existing production or launch new ventures.
While Lacprodan® BLG-100 is generally easy to work with and compatible with most existing equipment, high-shear mixing is recommended, and precise pH control is essential to ensure clarity and stability.
Sebastian Braad Poulsen, Application Scientist,
Arla Foods Ingredients
References
1. Gorissen et al. Protein content and amino acid composition of commercially available plant-based protein isolates. Amino Acids, 2018;50:1685-1695. https://doi.org/10.1007/s00726-018-2640-5
2. Katsanos et al. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. American Journal of Physiology-Endocrinology and Metabolism, 2006;291(2):E381-7. doi: https://doi.org/10.1152/ajpendo.00488.2005
3. Atherton et al. Enriching a protein drink with leucine augments muscle protein synthesis after resistance exercise in young and older men. Clinical Nutrition, 2017;36(3):888-895. doi: https://doi.org/10.1016/j.clnu.2016.04.025
