@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}},
}