Enzymatic Modification of Oat Proteins for Barista Oat Drinks : Linking Structure to Foaming and Coffee Stability
(2026) KLTM02 20261Food Technology and Nutrition (M.Sc.)
- Abstract
- The rapid expansion of the plant-based beverage sector has increased the demand for high-performance, barista-grade oat drinks that are capable of withstanding the thermal and acidic stresses of coffee applications. This master’s thesis, conducted in collaboration with Cerealiq AB, evaluates the efficacy of six specific enzymatic treatments in modifying the structural and physical properties of oat protein to establish a rational structure-function relationship for enzyme selection. Using a multi-analytical approach, the study identified proteolytic control as the primary determinant of interfacial performance. Although Sample 1 (Protease 1) showed maximum protein solubility, its high molecular polydispersity hindered the formation of a... (More)
- The rapid expansion of the plant-based beverage sector has increased the demand for high-performance, barista-grade oat drinks that are capable of withstanding the thermal and acidic stresses of coffee applications. This master’s thesis, conducted in collaboration with Cerealiq AB, evaluates the efficacy of six specific enzymatic treatments in modifying the structural and physical properties of oat protein to establish a rational structure-function relationship for enzyme selection. Using a multi-analytical approach, the study identified proteolytic control as the primary determinant of interfacial performance. Although Sample 1 (Protease 1) showed maximum protein solubility, its high molecular polydispersity hindered the formation of a cohesive interfacial film resulting in lower foam stability. In contrast, through limited proteolysis, Sample 5 and 6 (Protease 4) maintained molecular dispersity, facilitating an ordered molecular assembly at the air-water interface resulting in superior Foam Stability Index (FSI). Furthermore, the study confirmed that the maintenance of an appropriate particle size and apparent viscosity is essential for suppressing coalescence kinetics. Ultimately, this research provides a predictable framework for the enzymatic development of high-performance oat beverages for barista application by showing that superior foaming and colloidal stability depend on balancing protein solubility with molecular fragments which are less polydisperse and refined particle size. (Less)
- Popular Abstract
- Enzymatic Craftsmanship: Reshaping Oat Proteins for the Perfect Coffee
Oat drink is sustainable, but in coffee applications it often fails due to the nature of its proteins. This project studies different enzyme treatments that reshape oat proteins to create a stable coffee with robust foam.
In recent times, global food systems have undergone a significant transition towards sustainability, with consumers increasingly choosing plant-based diets to reduce their environ-mental footprint. Among the coffee enthusiasts who are seeking a creamy, dairy-free alter-native, oat drink has gained popularity. However, oat drink in a coffee cup presents a significant “Barista Challenge”. Unlike cow’s milk, proteins in oat drink have a rigid, tightly... (More) - Enzymatic Craftsmanship: Reshaping Oat Proteins for the Perfect Coffee
Oat drink is sustainable, but in coffee applications it often fails due to the nature of its proteins. This project studies different enzyme treatments that reshape oat proteins to create a stable coffee with robust foam.
In recent times, global food systems have undergone a significant transition towards sustainability, with consumers increasingly choosing plant-based diets to reduce their environ-mental footprint. Among the coffee enthusiasts who are seeking a creamy, dairy-free alter-native, oat drink has gained popularity. However, oat drink in a coffee cup presents a significant “Barista Challenge”. Unlike cow’s milk, proteins in oat drink have a rigid, tightly coiled structure. When introduced to the hot, acidic environment of a brewed coffee, these proteins react unfavourably causing them to clump together and curdle, while the foam collapses quickly.
The ability of a beverage to maintain a creamy, stable foam depends on the behaviour of proteins at the interfacial film which is the thin boundary between air and liquid. To function effectively, proteins must unfold and wrap around the air bubbles like a protective shield. However, the primary storage proteins in oat, known as 12S globulins, are too rigid to do this efficiently. To solve this issue, the food industry uses enzymes as molecular scissors to unfold the protein structure. This master’s thesis, conducted in collaboration with Cerealiq AB, sought to determine how different enzymatic treatments modify oat proteins to achieve barista-grade stability.
The study utilized a multi-analytical approach to look deeper into the molecular structure of the modified oat proteins. A key finding was that the precision of the enzymatic cut is as important as how much protein was cut and got dissolved. One treatment was highly efficient at extracting protein into the drink but created a polydisperse mixture. This system was much like trying to build a stable wall with bricks of random shape. The mismatched fragments could not pack together tightly, leading to a weak interfacial film that reduced the foam stability. In contrast, another specific treatment performed a limited proteolysis resulting in a more uniform less polydisperse population of protein fragments. These fragments arranged orderly and tightly around the bubbles to create a robust, viscoelastic film that kept the foam stable for more time.
Thus, the research shows that pairing a suitable protein modification enzyme technique with specific starch breaking enzymes, it is possible to develop a naturally creamy, stable oat drink suitable for coffee applications. These findings provide a scientific framework for engineering a sustainable, high-performance oat beverage. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/student-papers/record/9230784
- author
- Theresa George, Amala LU
- supervisor
-
- Anna Fureby LU
- organization
- course
- KLTM02 20261
- year
- 2026
- type
- H2 - Master's Degree (Two Years)
- subject
- keywords
- oat protein, limited proteolysis, foam stability, colloidal stability, barista-grade, food engineering nutrition and food chemistry
- language
- English
- id
- 9230784
- date added to LUP
- 2026-06-10 14:40:44
- date last changed
- 2026-06-10 14:40:44
@misc{9230784,
abstract = {{The rapid expansion of the plant-based beverage sector has increased the demand for high-performance, barista-grade oat drinks that are capable of withstanding the thermal and acidic stresses of coffee applications. This master’s thesis, conducted in collaboration with Cerealiq AB, evaluates the efficacy of six specific enzymatic treatments in modifying the structural and physical properties of oat protein to establish a rational structure-function relationship for enzyme selection. Using a multi-analytical approach, the study identified proteolytic control as the primary determinant of interfacial performance. Although Sample 1 (Protease 1) showed maximum protein solubility, its high molecular polydispersity hindered the formation of a cohesive interfacial film resulting in lower foam stability. In contrast, through limited proteolysis, Sample 5 and 6 (Protease 4) maintained molecular dispersity, facilitating an ordered molecular assembly at the air-water interface resulting in superior Foam Stability Index (FSI). Furthermore, the study confirmed that the maintenance of an appropriate particle size and apparent viscosity is essential for suppressing coalescence kinetics. Ultimately, this research provides a predictable framework for the enzymatic development of high-performance oat beverages for barista application by showing that superior foaming and colloidal stability depend on balancing protein solubility with molecular fragments which are less polydisperse and refined particle size.}},
author = {{Theresa George, Amala}},
language = {{eng}},
note = {{Student Paper}},
title = {{Enzymatic Modification of Oat Proteins for Barista Oat Drinks : Linking Structure to Foaming and Coffee Stability}},
year = {{2026}},
}