Method for enzymatic modification of liquified oats for enabling heat stability & frothing properties

Abstract

Described herein are methods for producing oat-based beverage be compositions and the compositions derived therefrom. The process involves hydrolyzing an oat base using alpha-amylase and glucoamylase while maintaining a stable pH. The method preserves beta-glucans in the resulting oat milk. Additionally, a protein is incorporated to stabilize air bubbles, enhancing foaming and frothing properties, even when the beverage is exposed to high temperatures.

Description

[0001] Method for Enzymatic Modification of Liquified Oats for Enabling Heat Stability & Frothing Properties

[0002] CLAIM OF PRIORITY

[0003] The present application includes subject matter disclosed in and claims priority to U.S. provisional patent application Serial No. 63 / 645,770, filed May 10, 2024, entitled “Method For Enzymatic Modification Of Liquified Oats For Enabling Heat Stability & Frothing Properties”, incorporated herein by reference, and which describes an invention made by the present inventor.

[0004] Field of the Invention:

[0005] The present invention relates to food processing, specifically to enzymatic methods for modifying oat base mixtures for enhanced nutritional value and texture.

[0006] Background:

[0007] In recent years, plant-based milk has surged in popularity, carving out a significant share of the global milk industry. Due to health concerns, environmental considerations, and dietary preferences, consumers are increasingly turning to non-dairy beverage alternatives. Classic dairy -free “milks” are typically produced from soy, rice, coconut, cashew, almond, oat, and hemp. However, known methods for producing non-dairy, plant-based milks often yield a product containing chemical additives, preservatives, and high sugar content, diminishing the health benefits those seeking dairy-free milk alternatives are pursuing.

[0008] Additionally, plant-based milks generally do not perform as well as traditional dairy milk, particularly in regard to frothing and foaming. Traditional dairy milk contains proteins, such as casein and whey, which create a stable structure that can effectively trap air bubbles, resulting in smooth and long-lasting foam. In contrast, most plant-based milks lack these proteins, thereby producing a foam that lacks the same stability as dairy milk or do not possess the capability for aeration at all. Furthermore, the fat composition in plant-based milk is often different from the fat composition in dairy milk, as dairy milk’s emulsified fats assist in stabilizing the foam. Plant-based milks, however, do not necessarily contain such emulsified fats that support the formation of a stable microfoam, making it more challenging for plant-based milks to create the frothy foam often desired in many coffee and tea beverages like lattes and cappuccinos.

[0009] Additionally, the cost of plant-based milk exceeds that of cow's milk, primarily due to the higher expense of raw ingredients such as soy, oats, rice, and nuts. Furthermore, the production of plant-based milks involves more intensive processing compared to cow's milk, which is typically limited to pasteurization and homogenization. The additional processing contributes significantly to the elevated costs of plant-based alternatives.

[0010] There is a great need for minimally processed plant-based milks that mimic the foaming and frothing properties of cow milk. Additionally, given the high cost of plant-based milk, there is a need for plant-based milk beverages with an extended shelf life, preferably without the use of preservatives that may diminish the health and nutritional benefits associated with dairy-free milk alternatives.

[0011] In recent years, there has been a sharp rise in plant and nut-based milk alternatives, including soy, rice, coconut, cashew, and almond milk. However, the nutritional value of these milk alternatives is compromised due to their lack of protein, high added sugar and chemical additive content, along with the environmental impact of their manufacturing methods. There remains a need for improved milk alternatives, such as cereal grain-based compositions, and particularly oat-based compositions.

[0012] Oat-based dairy alternatives are particularly advantageous due to their neutral flavor and the beta-glucans present in oats. Beta-glucans may provide health benefits while also adding a creamy consistency to oat milk, mimicking the creaminess of cow milk. Unfortunately, current methods for producing oat-based dairy alternatives do not maintain the preservation of beta-glucans, a cholesterol-lowering soluble fiber, while maintaining desirable sensory and textural qualities, nor do they simplify the production process by avoiding pH regulators or other additives.

[0013] Oat-based dairy alternatives are also free of common allergens. Being a dairy alternative makes them suitable for those allergic to dairy as well as those who cannot tolerate lactose. Additionally, oat-based dairy alternatives are suitable for those with nut and soy allergies.

[0014] Conventional enzymatic methods for producing oat milk utilize beta-amylase to hydrolyze oat starch into simpler sugars. However, beta-amylase is not an optimal enzyme for producing a smooth, frothable oat beverage, as beta-amylase cleaves the a- 1,4 glycosidic bonds from the non-reducing end of the amylopectin polysaccharide chain and is, therefore, less efficient at cleaving starch bonds than alpha amylase, which randomly cleaves a- 1,4 glycosidic bonds.

[0015] Conventionally produced oat-based beverages produced using beta-amylase require the addition of emulsifiers, oils, and other stabilizers to achieve foaming characteristics similar to those of whole cow’s milk.

[0016] Alternative methods of producing oat milk may rely on fungal glucoamylase and bacterial-derived alpha amylase, such that the glucoamylase may produce a product with a thicker, less sweet base that is over-thinned by bacterial alpha-amylase. Such products have hindered foaming capabilities and are not comparable to cow milk. Additionally, products produced with fungal glucoamylase do not maintain beta-glucans, thereby removing the health benefits and textural advantages provided by beta-glucans.

[0017] Some methods currently known in the art rely on a temperature of approximately seventy-one degrees Celsius during a first enzymic hydrolysis. While such relatively “lower” temperatures may produce a beverage having a thicker and creamier mouthfeel, such low temperatures may also hinder efficient starch breakdown and produce a less smooth product. Alternative methods for producing a creamy product while efficiently breaking down starches are needed for producing plant-based milks that wholly mimic cow milk's creaminess, smoothness, and frothing properties.

[0018] While some oat-based dairy alternatives are currently available, there remains a need for improved processes to produce cereal grain-based compositions that mimic the frothing ability of cow’s milk, eliminate the use of chemical additives, and maintain an extended shelf life.

[0019] There is a continuing interest in alternatives to animal milk (e.g., dairy or goat) and associated products (cheese, yogurt, etc.), with a sharp rise in recent years in plant- and nutbased “milk,” including soy, rice, coconut, cashew, and almond milk. However, the nutritional value of these milk alternatives has come under scrutiny for their high added sugar and chemical additive content, along with the environmental impact of their manufacturing methods. There remains a need for improved milk alternatives, such as cereal grain-based compositions. Further, there remains a need for improved processes to produce cereal grainbased compositions. Described herein is a plant-based milk alternative, as beverage or other consumable mode, primarily made from oats, which preserves the nutritional richness of oats and / or mimics the nutritional benefits of cow's milk. Additionally, the plant-based oat beverage described herein may be produced using an aseptic, extended shelf-life process, resulting in a product that can remain shelf-stable and fresh for over a year. In other embodiments, wherein the aseptic process is not used, the product may remain fresh for 60 to 90 days under refrigerated conditions before opening. Furthermore, the oat-based composition is unique in that it offers a creamy smooth product with healthful beta-glucans that provide barista-grade foaming properties without requiring the addition of chemical additives, emulsifiers, and stabilizers.

[0020] Detailed Description:

[0021] Provided herein are enzymic-based compositions and methods for producing a plantbased beverage that may function as a milk alternative, such that the plant-based beverage is nutritionally dense, has an extended shelf life, and mimics the foaming and frothing properties of cow’s milk without requiring chemical additives, emulsifiers, or foaming agents. The methods herein described may provide a consumable product in liquid, solid, gel, or other form.

[0022] The herein-described method may involve a sequential enzymatic treatment of an oatbase, such that the oat-base is sequentially treated with preferably bacterial amylase (preferably bacteria derived glucoamylase) and preferably fungi derived alpha amylase, having preferably a more efficient bacterial amylase step, wherein bacterial amylase is added at a relatively high temperature, and a less efficient alpha-amylase step, wherein fungal alpha-amylase may be added at a lower temperature. In some alternative embodiments, the enzymic sequence may be switched, such that the fungi-derived alpha-amylase may be added before the bacteria-derived glucoamylase.

[0023] It is preferable that the first enzyme be an enzyme that effectively cleaves 1,4 glycosidic bonds while maintaining branched 1,6 glycosidic bonds, such that the enzyme may be, but is not limited to, bacteria-derived glucoamylase. Additionally, it is preferable that the second hydrolysis be performed with an enzyme, such as alpha-amylase, that maintains the branched 1,6 glycosidic bonds as well. It is preferable that at least a majority of the 1,6- glycosidic bonds remain intact in the final product as retaining the branched 1,6-glycosidic molecules may yield a non-gelling, yet viscous beverage. In a preferred embodiment, the 1,6 glycosidic molecules may produce a product that is thick enough to create microfoam but thin enough to steam and pour well. The presence of 1,6 glycosidic molecules is additionally preferable because such molecules resist rapid collapse and help trap air bubbles when frothed, achieving a uniform foam without requiring added emulsifiers or thickeners. Additionally, retaining branched dextrin preserves soluble fibers like |3-glucans, which may be beneficial for digestion, cholesterol management, and blood sugar control.

[0024] In some embodiments, the alpha-amylase may be derived from fungi, while the glucoamylase is derived from bacteria, such that the fungus derived alpha amylase gently cleaves starch molecules to produce short polysaccharides that enhance beverage viscosity, but the bacteria derived glucoamylase effectively breaks 1,4 glycosidic starch bonds, to avoid excess starches that inhibit air retention during foaming.

[0025] In a preferred embodiment, the enzymatic treatment may be optimized to function within the oat base's natural pH range, eliminating the need for pH adjustments. In some embodiments, the method may preferably be performed in a solution with a pH ranging from six and a half to seven and a half, the natural pH of the herein described oat-base, thereby simplifying the manufacturing process and reducing production costs. In some embodiments, the oat beverage may include a pH adjuster, such as, but not limited to, citric acid, such that the final oat beverage has an optimal acidity for use in coffee, but the pH adjustment is not necessary for the enzymic treatment.

[0026] In a preferred embodiment, the process may optimize the final product’s capacity to maintain viscosity and to produce a stable foam, even at high temperatures, such that the product may be suitable for culinary applications requiring frothing or foaming.

[0027] In preferred embodiments, the herein described enzymatic treatment, preferably including alpha-amylase and glucoamylase, may prevent the produced oat beverage from gelatinization, thickening, or gelling when heated, thus maintaining a consistent viscosity and facilitating the production of a stable foam, even when the oat beverage is subjected to boiling temperatures.

[0028] Oat Starches

[0029] As further described below, oats primarily consist of two starch types: approximately twenty-five percent amylose and seventy-five percent amylopectin. Amylose, as seen in Fig. 1, has a linear, helical structure, such that the molecular arrangement is such that repeating, linear units, formed from a- 1,4 glycosidic bonds, coil into a spiral, “helical” shape, as seen in Fig. 2, due to intramolecular interactions. Amylose is configured as a straight chain without any branching. Because amylose is composed of glucose units linked by a- 1,4 glycosidic bonds, when amylose is heated in water and then cooled, it may form strong, stable gels, as the linear structure allows amylose to align and form hydrogen bonds with adjacent chains, creating a gel-like network.

[0030] As it is formed from glucose units, amylose forms strong, stable gels. Amylose's gelforming properties can be beneficial for making oat beverages, as when amylose is hydrolyzed, the produced gel structure may increase the viscosity of the beverage. Additionally, because amylose forms a gel-like network, it may contribute a creamy, smooth texture to oat beverages.

[0031] Additionally, the gel -like structure of hydrolyzed amylose may contribute to the foaming and frothing properties of oat milk, as the gel formation helps trap air during the frothing process, allowing oat milk to develop a stable foam, as is produced by dairy milk due to dairy milk’s emulsified fats.

[0032] While amylose’s gel -forming capacity is beneficial when producing oat beverages, over-hydrolyzed amylose may contribute excessive gelation, making the oat milk too thick or gelatinous, therefore, the herein described enzyme-based lysis process may produce an appropriate, consistent, and stable oat beverage texture.

[0033] Beta-amylase, an enzyme used in conventional oat milk production, cleaves amylose, breaking down the a- 1,4 glycosidic bonds and producing maltose. Beta-amylase is an exoacting amylolytic enzyme that may catalyze the hydrolysis of a-l,4-glycosidic bonds in starch, glycogen, and related polysaccharides, including, but not limited to, amylose.

[0034] Beta-amylase, an enzyme used in oat-milk production methods currently known in the art, acts on amylose by cleaving its a-l,4-glycosidic bonds from the non-reducing end, releasing maltose (a disaccharide of glucose) in a stepwise fashion. The enzyme progresses along the amylose chain, sequentially liberating maltose units until it reaches the final two glucose residues, which are left as a limit dextrin. Beta-amylase exclusively acts from the non-reducing ends of amylose and does not generate oligosaccharides of variable length.

[0035] However, beta-amylase is not an optimal enzyme for producing a smooth, frothable oat beverage, as beta-amylase cleaves the a-1,4 glycosidic bonds from the non-reducing end of the amylopectin polysaccharide chain. In some embodiments, the amylopectin remains only partially hydrolyzed, leaving residual starch that impairs the foaming properties of the final oat beverage. Consequently, conventionally produced oat-based beverages produced using beta-amylase require the addition of emulsifiers, oils, and other stabilizers to achieve foaming characteristics similar to those of whole cow’s milk.

[0036] Alpha-amylase

[0037] In contrast, Alpha-amylase is an endo-amylase that randomly hydrolyzes internal a- 1,4-glycosidic bonds to yield oligosaccharides. Alpha-amylase catalyzes the hydrolysis of a- 1,4-glycosidic bonds in polysaccharides like amylose and amylopectin but does not cleave a- 1,6 linkages (which are present in amylopectin but are not present in amylose). Unlike betaamylase, which works progressively from the non-reducing end, alpha-amylase acts randomly along the polysaccharide chain, generating a mixture of shorter oligosaccharides, maltose, and maltotriose.

[0038] Alpha-amylase may be preferred over beta-amylase for oat starch liquification, as alpha-amylase breaks starch randomly and rapidly, breaking down the starch more quickly than beta-amylase, which works in a slower, sequential manner from the ends of the polysaccharide. Alpha amylase may be derived from both bacterial and fungal sources, with bacterial alpha amylase being more aggressive at starch breakdown than fungal alpha amylase. Fungi-derived alpha-amylases may break down starches relatively gently, thereby producing a product with short polysaccharides that enhance a beverage's viscosity and body.

[0039] Additionally, unlike Beta-amylase, which cannot completely liquify amylose, alphaamylase is highly effective at liquefying amylose, converting it into a mixture of maltose, maltotriose, and dextrin.

[0040] The active site of alpha-amylase contains a substrate-binding cleft, which accommodates five to seven glucose residues of an amylose chain. Hydrogen bonds and van der Waals interactions may stabilize the bond between the enzyme and hydroxyl groups of the glucose residue, stabilizing the bond between alpha-amylase and amylose. As seen in Fig. 3, during enzymic hydrolysis, alpha-amylase follows the double-displacement mechanism. First, a nucleophile in alpha-amylase’s active site, typically an aspartate 1 la 1 lb or glutamate 12 residue, attacks the anomeric carbon of the glycosidic bond, leading to bond cleavage. The bond cleavage forms a covalent glycosyl-enzyme intermediate, releasing the leaving group and a shorter oligosaccharide or maltose.

[0041] The second displacement occurs when a water molecule, activated by a nearby general acid / base residue, often another aspartate or glutamate, attacks the covalent glycosyl- enzyme complex, resulting in hydrolysis and releasing a new reducing end and regenerating the enzyme for another catalytic cycle. This double-displacement mechanism retains the a- configuration of the glucose units after cleavage, allowing the products to remain in the a- anomeric form.

[0042] Structural Features of Alpha- Amylase The following description is a general description of alpha-amylase structure and function and is not meant to limit the structure and function of the particular glucoamylase described in the method herein. As seen in Fig. 3, alpha-amylase may include “domain A” 5, “domain B” 6, and “domain C” 7, with each domain contributing to the enzyme's structure and function. Domain A5 is the primary catalytic domain of alpha-amylase and is usually the most prominent in terms of structural and functional significance. It often adopts a (p / a)8- barrel fold, a structural motif in enzymes. This domain is responsible for the enzyme's ability to catalyze the hydrolysis of glycosidic bonds in starch and glycogen. The active site of alpha-amylase, where the cleavage of polysaccharides occurs, is located within Domain A. The catalytic residues in this domain, typically a pair of aspartic acid residues 11 and a glutamic acid residue 12, play a central role in breaking down the starch substrate by facilitating the hydrolysis reaction.

[0043] Domain B6 typically adopts an a / p-fold and is often less conserved than Domain A. It is found in many types of amylases, particularly in bacterial or fungal alpha-amylases. Domain B6 generally stabilizes the enzyme structure and may participate in substrate recognition and binding. In some embodiments, domain B 6 contains the calcium-binding site, such that when Ca2+ions bind to domain B 6, the enzyme’s structure is stabilized. Domain B6 does not typically contain the catalytic residues but is important for the overall stability of the enzyme. Domain B 6 may also facilitate interactions with other molecules, such as regulatory proteins, and sometimes aids in the enzyme's specificity for a particular substrate.

[0044] Domain C7 is typically a more variable region in terms of sequence and structure when compared to Domain A, and its fold can differ between species. It often contains several loops and helical regions that help form the substrate's binding site. Domain C7 is primarily involved in substrate binding and positioning the starch or glycogen molecule for proper interaction with the active site in Domain A5. It plays a role in determining the enzyme's specificity for particular types of polysaccharides. Domain 6 interacts with the substrate through various non-covalent interactions (such as hydrogen bonding or van der Waals forces), helping to stabilize the substrate in the enzyme's active site during catalysis.

[0045] As seen in Fig 3, most alpha-amylases contain a catalytic triad of two aspartate residues 11 and one glutamate 12, which facilitate proton donation and nucleophilic attack. In some embodiments, alpha-amylase may require Ca2+ions for structural stability. The calcium-binding site, labeled “domain B” in Fig. 3, helps maintain the enzyme's conformation, preventing denaturation.

[0046] As seen in Fig. 3, the a-amylase mechanism involves several key steps within its three domains, domain A 5, domain b 6, and domain c 7, such that the mechanism may produce starch hydrolysis. Step 1, as seen in Fig. 3 illustration 21, involves the enzyme, a-amylase, binding to the substrate, namely the starch amylose. In preferred embodiments, starch may bind to the active site of a-amylase, facilitated by enzymic residues including preferably Asp340 11b, Glu278 12, and Asp248 I la.

[0047] As seen in Fig. 3, illustration 22, after the enzyme binds to the substrate, the enzyme, a-amylase, enters transition state I, wherein water is introduced, initiating the hydrolysis of the glycosidic bond in starch. Illustration 23 depicts the substrate undergoing further transformation as it enters transition state II, wherein the amylose’s glycosidic bonds move towards cleavage. As seen in Fig. 3 illustration 24, transition state III occurs when the glycosidic bond is cleaved. In some embodiments, proton transfer involving Glu278 12 may facilitate the glycosidic bond cleavage. As seen in Fig. 3 illustration 25, the mechanism is complete when a mixture of maltose, maltotriose, and limited dextrin is produced.

[0048] In a preferred embodiment, fungal-derived alpha-amylase is preferable over bacteria- derived alpha-amylase for production of the herein described oat beverage. The structure of fungal alpha-amylase may differ from that of bacterial alpha-amylase, as described below, making fungal-derived alpha-amylase a “milder” enzyme, such that when hydrolyzing an oat composition with fungal alpha amylase, the hydrolysis may be less aggressive than that of bacteria-derived alpha-amylase. Oat hydrolysis with fungal-derived alpha-amylase may produce a product with enhanced viscosity and body. Alternatively, when bacteria-derived alpha-amylase is used for oat composition enzymic hydrolysis, the final product may be watery and less viscous.

[0049] Fungal alpha-amylase and bacterial alpha-amylase may differ in amino acid composition, glycosylation, stability, and domain organization; such structural differences may contribute to alpha-amylase's mild hydrolysis properties. In some embodiments, fungal alpha-amylases may have a more compact structure, such that disulfide bonds contribute to fungal alpha-amylase’s thermal stability and enzymatic activity at moderate temperatures. Whereas, bacterial alpha-amylases may exhibit an open or flexible structure, allowing for (more) activity across a broader temperature and pH range. Additionally, fungal alpha-amylases may be glycosylated, such that fungal-derived alpha-amylase may include attached carbohydrate chains that contribute to enhanced stability and controlled enzymatic activity. This glycosylation modulates enzyme function, resulting in a milder and more controlled starch hydrolysis process compared to bacterial alpha-amylases. In contrast, bacterial alpha-amylases are typically non-glycosylated and, therefore, less stable, relying instead on intramolecular interactions and structural flexibility for stability. As a result, bacterial alpha-amylases often exhibit higher catalytic activity across broader temperature and pH ranges but may also demonstrate more aggressive enzymatic action, making them less suitable for applications requiring precise or gentle starch breakdown, such as oat beverage production.

[0050] Additionally, differences in domain structure may contribute to fungal alphaamylase’ s mild hydrolysis properties. While both fungal and bacterial alpha-amylase may have a catalytic TIM barrel domain and a calcium-binding site for stability, their loop regions and additional domains may vary. In some embodiments, bacterial alpha-amylases have extra-carbohydrate-binding modules (CDMs) that improve substrate binding and processing, such CDMs are less common in fungal amylases. The absence or reduced presence of CBMs in fungal alpha-amylases may suggest that fungal -derived alpha-amylase enzymes may have weaker substrate binding and less aggressive hydrolysis, leading to a more controlled and gradual breakdown of starch, as discussed herein.

[0051] In a preferred embodiment, fungal-derived alpha-amylase is preferable over bacteria- derived alpha-amylase for production of the herein described oat beverage. The structure of fungal alpha-amylase may differ from that of bacterial alpha-amylase, as described below, making fungal-derived alpha-amylase a “milder” enzyme, such that when hydrolyzing an oat composition with fungal alpha amylase, the hydrolysis may be less aggressive than that of bacteria-derived alpha-amylase. Oat hydrolysis with fungal-derived alpha-amylase may produce a product with enhanced viscosity and body. Alternatively, when bacteria-derived alpha-amylase is used for oat composition enzymic hydrolysis, the final product may be watery and less viscous.

[0052] Hydrolysis with Glucoamylase

[0053] Glucoamylase is an exo-acting enzyme that may hydrolyze both a- 1,4 and a- 1,6 glycosidic bonds, breaking down starches completely to produce glucose. In some embodiments, fungal-derived glucoamylases may effectively break both a- 1,4 and a- 1,6 glycosidic bonds, while bacteria-derived glucoamylases, as herein described, are limited in their capacity to break down a-1,6 glycosidic bonds. Bacteria-derived glucoamylases, as described herein, may use an inverting mechanism to produce glucose from intact starch, such that the glucose product is in the P-anomeric form.

[0054] It is preferable that to produce the herein disclosed beverage, glucoamylase be bacterial derived, such that at least a majority of the 1,6-glycosidic bonds remain intact in the final product as retaining the branched 1,6-glycosidic molecules may yield a non-gelling, yet viscous beverage. In a preferred embodiment, the 1,6 glycosidic molecules may produce a product that is thick enough to create micro-foam but thin enough to steam and pour well. The presence of 1,6 glycosidic molecules is additionally preferable because such molecules resist rapid collapse and help trap air bubbles when frothed, achieving a uniform foam without requiring added emulsifiers or thickeners. Additionally, retaining branched dextrin preserves soluble fibers like P-glucans, which may be beneficial for digestion, cholesterol management, and blood sugar control.

[0055] While glucoamylase effectively produces glucose from non-reducing ends of starch molecules, it is slow at hydrolyzing intact starch, including but not limited to intact oats, where there are few exposed non-reducing ends without prior liquefaction. Therefore, it is preferable that oats first be hydrolyzed and liquified, with methods such as but not limited to manual liquefaction, including but not limited to via blending. In other alternative embodiments, oats may be first hydrolyzed with enzymes such as, but not limited to, alphaamylase and beta-amylase, after which the oat liquid may be further treated with glucoamylase to produce a sweet, glucose-containing beverage.

[0056] In alternative embodiments, wherein an enzyme is used to liquify intact oats, alpha amylase may be a preferred enzyme over beta-amylase, as alpha-amylase works optimally at a neutral pH. While beta-amylase has a lower, more acidic optimal pH. Therefore, in embodiments where an oat beverage is being produced in an environment having a neutral pH, without pH stabilizers, alpha-amylase may be a preferred enzyme. Additionally, as alphaamylase is an endoenzyme that randomly cleaves starch bonds, alpha-amylase produces a faster and more complete hydrolysis when compared to beta-amylase, an exoenzyme that slowly hydrolyzes starch from the non-reducing end of a starch molecule. In a preferred embodiment, as herein described, oats may be first mechanically liquified, after which the oat slurry may be treated with preferably bacteria- derived glucoamylase, at a higher temperature, such that the glucoamylase step is maximized, breaking down excess starch bonds that may interfere with air retention and foaming. After the glucoamylase step is completed, as discussed below, a second enzymic treatment may be performed. In a preferred embodiment, the enzyme administered to the slurry in the second treatment may be performed at a lower temperature, as discussed below, with fungal derived alpha-amylase, such that any starches remaining after the first enzymic treatment with glucoamylase may be broken down gently, such that the remaining starches break down to shorter polysaccharides that enhance beverage viscosity and body.

[0057] Glucoamylase Structure and Function

[0058] As seen in Fig 4, glucoamylase is an exoenzyme that may hydrolyze starch and starch byproducts, including but not limited to maltose, dextrin, and limit dextrin into glucose by breaking a- 1,4 and fungal embodiments, a- 1,6 glycosidic bonds from the non-reducing end of starch molecules. In bacterial embodiments, glucoamylases have active sites specialized exclusively for a-1,4 linkages, making them less effective at accommodating a-1,6 linkages. While some auxiliary regions within the enzyme may allow occasional a-1,6 hydrolysis, the process is slow and inefficient.

[0059] The following description is a general description of glucoamylase structure and function and is not meant to limit the structure and function of the particular glucoamylase described in the method herein. As seen in Fig. 4, the catalytic domain 30, wherein a starch or other such polysaccharide is hydrolyzed into glucose, folds as a twisted (alpha / alpha)(6)- barrel with a central funnel-shaped active site 32, while the starch-binding domain 31 folds as an antiparallel beta-barrel and has two binding sites for starch or beta-cyclodextrin. Starch- binding domain 31 folds as an antiparallel P-barrel having two independent substrate binding sites.

[0060] Catalytic domain 30 houses the active site residues responsible for catalysis. The active site contains a conserved pair of aspartic acid residues, functioning as a nucleophile and an acid / base catalyst, crucial for hydrolysis. Starch-binding domain 31 includes a C- terminal domain that facilitates substrate affinity and enzymatic efficiency by increasing local starch concentration near the catalytic site. In some embodiments, glucoamylase may be present as a monomer; in other embodiments, glucoamylase may be glycosylated. Monomeric Glucoamylase is composed of a single polypeptide chain without post-translational glycosylation. While monomeric glucoamylase functions efficiently, it may have lower thermostability and reduced resistance to proteolysis. In some embodiments, monomeric glucoamylase may be prone to aggregation and denaturation under industrial conditions.

[0061] In other embodiments, particularly in fungal embodiments, glucoamylase may be present in the glycosylated form, such that the enzyme contains covalently attached glycan chains, typically in the form of N-linked and O-linked glycosylations. Glycosylated glycoamylase may have improved protein stability over monomeric glucoamylase, as the covalently attached glycan chain may prevent aggregation and proteolytic degradation. Additionally, glycosylated glycoamylase may have enhanced solubility, making the enzyme more effective in industrial applications. Glycosylated glycoamylase may modulate catalytic activity as glycosylation influences substrate affinity and enzyme conformation.

[0062] Glucoamylase may operate via an acid-base catalysis mechanism, following a retaining or inverting hydrolytic process depending on specific active site configurations. When glycoamylase binds to a substrate, including but not limited to dextrin and maltose, the active site cleft accommodates linear a-l,4-linked glucans, with additional specificity for a- 1,6 branch points in amylopectin. Aromatic and polar residues within the active site may engage in hydrogen bonding and hydrophobic stacking to stabilize substrate positioning.

[0063] After binding, catalysis may begin via acid-base hydrolysis. In some embodiments, a first Asp residue, a nucleophile, attacks the anomeric carbon of the terminal glucose unit, forming a glycosyl -enzyme intermediate. Subsequently, the second Asp residue facilitates protonation and departure of the leaving group, glucose, followed by water-mediated hydrolysis of the intermediate, thereby resulting in successive release of P-D-glucose units. In some embodiments, calcium ions may enhance enzymic structural stability.

[0064] When hydrolyzing oats, the starches amylose and amylopectin must both be hydrolyzed. The hydrolysis of amylopectin will be further described in detail below. To hydrolyze amylase, the oats may first be liquified with the enzyme alpha-amylase such that the amylase breaks a-l,4-glycosidic bonds within the starch molecule, randomly cleaving long amylose chains into smaller oligosaccharides and dextrin. After treatment, the amylose is liquified, such that the starch viscosity is reduced, and short-chain polysaccharides are produced. To further hydrolyze the short-chain polysaccharides, the produce may be treated with glucoamylase, such that saccharification occurs. The glucoamylase may hydrolyze the a- 1,4 linkages from the non-reducing ends of oligosaccharides, releasing glucose as the final product, thereby converting dextrin and maltose into free glucose and hydrolyzing the amylose.

[0065] Bacterial and Fungal Glucoamylase Embodiments

[0066] In a preferred embodiment, for the production of the herein described oat beverage, bacteria derived glucoamylase may be preferable over fungal -derived glucoamylase The structure of bacterial glucoamylase may differ from that of fungal glucoamylase, as described below, making bacterial derived glucoamylase a more active enzyme, particularly at higher temperatures as described below, such that when hydrolyzing an oat composition with bacterial glucoamylase, the hydrolysis may be more aggressive, than that of fungal-derived glucoamylase. Oat hydrolysis with bacterial-derived glucoamylase may produce a product with fewer remaining starch bonds, such that the beverage composition does not include starch bonds that may interfere with beverage frothing and foaming. Oat beverages known in the art that are produced with fungal -derived glucoamylase may have inferior foaming properties due to remaining starch bonds, particularly 1,4 glycosidic bonds that interfere with air retention.

[0067] In some embodiments, the activity differences between fungal and bacterial glucoamylases arise from their structural variations, including but not limited to variations in glycosylation, domain organization, and intramolecular interactions.

[0068] In some embodiments, glycosylation may provide enhanced glucoamylase stability, as glycosylation shields enzymes from proteolytic degradation, enhances thermal stability, and increases solubility. While fungal glucoamylases are heavily glycosylated, bacterial glucoamylases are either non-glycosylated or minimally glycosylated and are, therefore, less stable and more active, particularly in extreme temperatures, as discussed below.

[0069] Bacteria-derived and fungus-derived glucoamylase may also differ in domain organization. While rigid and compact fungal glucoamylase may include a single catalytic domain, bacterial glucoamylase may have multiple domains. Bacteria-derived glucoamylase domains include a carbohydrate-binding molecule and flexible linker regions, such that bacterial glucoamylase may adapt to diverse conditions, whereby such bacterial-derived glucoamylase models may be more active at high temperatures than fungal -derived glucoamylase.

[0070] Glucoamylase molecules derived from fungus, having covalent bonds, may have advanced molecular stability when compared to glucoamylase molecules that rely on non- covalent intermolecular interactions (such as those derived from bacterial sources). But, at higher heat temperatures, such as temperatures between fifty and eighty degrees Celsius, glucoamylases with weaker intramolecular interaction, including but not limited to hydrophobic interactions and hydrogen bonding, may be more flexible and, therefore, more adept at adapting and functioning at such high temperatures. In contrast, rigid, fungal -derived glucoamylases may be more stable at moderate heat conditions but are not able to adapt to perform at higher heat conditions, as described above. Hydrolysis of Amylopectin

[0071] To produce an oat beverage, it is preferable that oat starches amylase and amylopectin be hydrolyzed. A detailed description of the mechanism for amylose hydrolysis is described above. Amylopectin, as seen in Fig. 5, often makes up approximately seventy-five to eighty percent of oat starch. The remaining twenty to twenty-five percent of oat starch may be made up of amylose, which may preferably be hydrolyzed by glucoamylase and alpha-amylase as described above.

[0072] Glucoamylase, an exo-acting enzyme, hydrolyzes a- 1,4 and, in some fungal-derived glucoamylase embodiments, a- 1,6 glycosidic bonds by cleaving glucose units from the nonreducing ends of the oligosaccharides. In some embodiments, glucoamylase may hydrolyze a- 1,4 glycosidic bonds by binding to the non-reducing end of an oligosaccharide. Once bound, the active site of glucoamylase, which may be an Asp or Glu residue, as seen in Fig. 4, protonates the glycosidic oxygen of the bond, destabilizing the linkage, leading to the cleavage of the glycosidic bond, forming an oxocarbenium ion-like transition state. Then, a nucleophilic water molecule, positioned by the enzyme, attacks the Cl carbon of the glucose unit, releasing P-D-glucose, which rapidly mutarotates to a-D-glucose in solution. Once glucose is released, the enzyme then resets, such that the enzyme may continue onto the next non-reducing end of an oligosaccharide to continue breaking down the glycosidic bonds to release glucose molecules, one at a time. While the mechanism of action for a-1,4 and a-1,6 glycosidic bond cleavage is the same, the mechanism occurs at a slower rate for a-1,6 glycosidic bond cleavage due to steric hindrance. In some embodiments, such as when glucoamylase is of bacterial origin, a-1,6 glycosidic bond cleavage is limited, and the enzyme predominantly cleaves a-1,4 glycosidic bonds. Such a-1,6 glycosidic bond retention is preferable for beverages as described herein /

[0073] In some embodiments, after amylopectin is treated with glucoamylase, a second enzymic treatment with alpha-amylase may be performed such that remaining starches having a-1,4 glycosidic bonds may be hydrolyzed. It is preferable to perform the second treatment with fungal-derived a-amylase due to its gentle reaction nature, ensuring that the final product does not become over-liquified.

[0074] When treating the mixture with a second enzyme, preferably fungal-derived alpha amylase, the remaining starch enzyme may be broken down into small polysaccharides, such that the small polysaccharides may enhance beverage viscosity and body. The remaining polysaccharides may include maltose, maltotriose, and limit dextrin. To hydrolyze starch with fungal -derived alpha-amylase into small polysaccharides, fungal alpha amylase may undergo a double-displacement reaction, such that the alpha-configuration of the anomeric carbon is retained in the final product.

[0075] In some embodiments, when performing, preferably a second, hydrolysis with alphaamylase, the catalytic residues may include two acidic amino acids, a nucleophile and an acid / base catalyst (typically Aspartate (Asp) and Glutamate (Glu)). The aforementioned catalytic residues may facilitate hydrolysis by forming a covalent intermediate such that the nucleophile, such as Asp, attacks the anomeric carbon, forming a covalent enzyme-substrate intermediate. Simultaneously, an acid catalyst, such as Glu, may donate a proton to the departing glucose unit, breaking the a-1,4 bond and forming an intermediate. To release the polysaccharide, a water molecule may be activated by the deprotonated acid catalyst, such that the deprotonated acid catalyst may function as a base catalyst to activate the water molecule, such that the water molecule attacks the aforementioned intermediate, releasing the cleaved oligosaccharide while regenerating the enzyme for another cycle.

[0076] Because bacterial glucoamylase is limited in its ability to cleave a-1,6 linkages, and fungal alpha-amylase does not cleave a-1,6 linkages, the final product may contain highly branched residual starch fragments, such that the remaining starch fragments may contribute to the thickness, viscosity, and mouthfeel of a beverage, as herein described. Oat Milk Production Process

[0077] The present invention is broadly concerned with oat-based liquid suspensions intended for consumption, which may be characterized herein as oat-based beverages, oat milk, oat drink, and the like. The present invention is also concerned with starch hydrolysis processes for producing such oat-based liquid suspensions. The herein described hydrolysis processes are preferable, as they produce “frothable”, foaming beverages that mimic cow milk's texture and foaming properties.

[0078] In the herein described process, oats, preferably oat flour in an aqueous suspension, are hydrolyzed with selected enzymes, such that a preferable concentration of polysaccharides remains in the beverage to maximize the texture, thickness, viscosity, and mouthfeel of the beverage. In some embodiments, the beverage may be mixed with one or more optional flavoring agents to yield an oat-based beverage. Oat-based beverages according to embodiments of the invention may include hydrolyzed oat flour suspended in an aqueous solution. Additional ingredients include amylase enzymes (preferably bacterial glucoamylase and fungal alpha-amylase), an acid source, such as preferably citric acid, a protein source, preferably a sunflower-based protein source, and one or more additives, including but not limited to flavoring agents, adaptogens, and vitamins.

[0079] Flavoring agents may preferably include vanilla extract and / or cocoa powder / chocolate flavor. In some embodiments, flavoring agents may additionally, or alternatively include one or more of vanilla extract, salt, cacao powder, cocoa powder, caramel, spices such as cinnamon, turmeric, chai, and natural or artificial flavor extracts including vanilla, strawberry, raspberry, blueberry, banana, coffee, pumpkin, toffee, licorice, chocolate, mocha, other seasonal flavors, and the like. Adaptogens may include, but are not limited to, ginseng extract, preferably organic, ashwagandha, preferably organic, and 1- theanine. When referring to ginseng extract and ashwagandha, the term ‘organic’ may refer to substances derived from biological sources or produced following organic certification standards, free from synthetic additives, pesticides, or genetically modified organisms.

[0080] In some alternative embodiments, one or more sweeteners or sweetening agents may be included in the oat-based beverage; however, the oat-based beverage will have intrinsic sweetness from hydrolysis of the oat flour and, therefore, in preferred embodiments, may not require added sugars to achieve a sweet taste. Thus, no-added sugar embodiments of the oatbased beverage composition are contemplated herein and preferred. However, if desired, exemplary sweetening agents that may be incorporated to the oat beverage may include but are not limited to cane sugar, stevia, maple syrup, corn syrup, molasses, agave nectar, monk fruit, as well as artificial sweeteners such as saccharin, sucralose, sugar alcohols, acesulfame potassium, aspartame, and the like.

[0081] In some embodiments, a preferred oat-milk beverage may be produced by combining water, oat flour, citric acid, bacterial amylase, and fungal amylase. In a preferred embodiment, the oat flour may be whole colloidal fine oat flour. It is preferable that the oat flour be organically grown and processed, such that the oat flour is grown and produced following “organic” certification standards, such that the oat flour may be free from synthetic additives, pesticides that do not qualify as “organic”, or genetically modified organisms (GMOs).

[0082] Enzymic Embodiments

[0083] An enzymic process for producing oat milk is herein described. The following enzymes are exemplary in nature and are not intended to limit the scope of the present disclosure. The process preferably involves the use of alpha-amylase and glucoamylase. In some embodiments, a combination of alpha amylase derived from fungal origin and glucoamylase derived from bacterial origin may be used.

[0084] Alternative, subpar, enzyme-based oat beverages known in the art rely on fungal glucoamylase and bacterial alpha-amylase. In such embodiments, the fungal glucoamylase may produce a product with a thicker, less sweet base, after which the product is over-thinned with bacterial alpha-amylase, hindering foaming capabilities. Therefore, it is preferable, as herein disclosed, that an alpha-amylase of fungal origin be used to hydrolyze an oat slurry, such that the starches are broken down gently, resulting in shorter polysaccharides and enhanced viscosity and beverage “body”. Additionally, bacterial glucoamylase may be preferable over fungal-derived glucoamylase, as bacterial glucoamylase is more efficient at breaking starch bonds at higher temperatures, as disclosed herein, therefore, the higher temperature glucoamylase step may be more efficient at removing excess starch to enhance air retention, producing a beverage with superior foaming capabilities.

[0085] Different amylase origins may be preferred based on production conditions. For example, fungal amylase functions optimally at moderate temperatures, preferably between forty-five and sixty-degrees Fahrenheit. In contrast, bacterial amylases may be more thermotolerant, with a preferable optimal operating temperature ranging from fifty to ninety degrees Celsius.

[0086] In some embodiments, a preferred oat milk beverage may be produced by combining water, oat flour, citric acid, bacterial amylase, and fungal amylase. In a preferred embodiment, the oat flour may be whole colloidal fine oat flour. It is preferable that the oat flour be organically grown and processed, such that the oat flour is grown and produced following “organic” certification standards, such that the oat flour may be free from synthetic additives, pesticides that do not qualify as “organic”, or genetically modified organisms (GMOs).

[0087] In a preferred embodiment, the bacterial amylase may be bacteria bacteria-derived glucoamylase, such that the glucoamylase is particularly thermostable. Bacterial glucoamylases may include, but are not limited to, Bacillus licheniformis glucoamylase, Bacillus amyloliquefaciens glucoamylase, Bacillus subtilis glucoamylase, Clostridium thermocellum glucoamylase, and Geobacillus stearothermophilus glucoamylase.

[0088] In a preferred embodiment, the fungal amylase may be alpha-amylase of fungal origin, such that the alpha-amylase is relatively mild at lower temperatures, as discussed below. Fungal derived alpha amylases useful for the described processes may include, but are not limited to, aspergillus oryzae a-amylase, aspergillus niger a-amylase, and rhizopus oryzae a-Amylase, penicillium spp. a-Amylase. Such fungal derived alpha-amylase enzymes may be more active at high temperatures, therefore in a preferred embodiment, the fungal derived alpha amylase may be added to the herein described oat beverage for a second hydrolysis at a lower temperature, such that further starch breakdown is limited, preventing an excessive increase in simple sugars in the final product. At higher temperatures, fungal amylase activity may be more aggressive, thereby leading to over-hydrolysis and a thinner beverage consistency, compromising foaming stability.

[0089] Oat Beverage Recipe Embodiments

[0090] In some embodiments, a preferred oat-milk beverage may be produced by combining water, oat flour, a protein source, citric acid, bacterial amylase, and fungal amylase. In a preferred embodiment, the oat flour may be whole colloidal fine oat flour. It is preferable that the oat flour be organically grown and processed, such that the oat flour is grown and produced following “organic” certification standards, such that the oat flour may be free from synthetic additives, pesticides that do not qualify as “organic”, or genetically modified organisms (GMOs).

[0091] In some embodiments, a preferred oat-milk beverage may include a protein source. A preferred protein source may be, but is not limited to, sunflower protein, preferably sunflower protein powder. In some, alternative embodiments, the protein source include, but is not limited to pumpkin seed protein, watermelon seed protein, chia seed protein, pea protein, lentil protein, fava bean protein, oat protein, quinoa protein, rice protein, almond protein, cashew protein, fungi -based protein, algae based protein, animal protein, or lab grown proteins.

[0092] In preferred embodiments, the protein source may be a plant-based protein derived from sunflower seeds. In some embodiments, sunflower based protein (or any protein source or combination thereof) may be present in the herein described oat beverage, making up approximately between one and five percent of the final oat beverage composition, with a preference of between 2.8% to 4.5%. In some preferred embodiment, an oat beverage may contain approximately three-point thirty percent sunflower protein, or other such protein sources. In other preferred embodiments, an oat beverage may contain approximately four percent sunflower protein, or other such protein.

[0093] As discussed above, in alternative embodiments, alternative protein sources may be used to replace sunflower protein. In some embodiments, alternative protein sources may be incorporated into the herein described oat beverage, in the same proportions as described above for sunflower protein. In alternative embodiments, alternative protein sources may be incorporated into the herein described oat beverage in proportions that differ from those described herein for sunflower protein.

[0094] In some preferred embodiments, a protein source may be included in the composition of the herein-disclosed beverage. In a preferred embodiment, the protein source may provide optimal beverage texture, such that the proteins may stabilize air bubbles, thereby producing a beverage that may mimic the foaming and frothing properties of cow milk.

[0095] In a preferred embodiment, when the protein-fortified oat beverage, as described herein, is frothed, the added proteins form a flexible film around the air bubbles, effectively surrounding and stabilizing the trapped air. This protein film may function to prevent the bubbles from collapsing, thereby maintaining the structure of the beverage, even when poured over hot coffee, iced drinks, or other such liquids of various temperatures. Additionally, the protein film may enhance the beverage’s viscosity, as the protein film may bind with the water in the oat beverage to produce a relatively dense, cohesive liquid with a creamy texture.

[0096] In some embodiments, sunflower protein may function as a preferred protein source due to its balanced amino acid profile. A balanced amino acid profile is herein defined as an amino acid profile that provides all essential amino acids in the requisite proportions necessary for efficient protein synthesis. A balanced amino acid profile may provide optimal solubility and emulsification properties, such that sunflower protein may be thoroughly dissolved and emulsified into an oat beverage. And therefore, unlike other plant proteins, including but not limited to pea or soy protein, sunflower protein has a lower tendency to create sediment, thereby producing a smooth oat beverage that is free of sediment and other such particles that may disrupt foam structure.

[0097] Therefore, in a preferred embodiment, as described herein, an oat beverage fortified with sunflower protein may generate a stable, long-lasting foam that does not separate and or settle. Furthermore, sunflower protein offers a neutral sensory profile, which enhances its compatibility with added flavors and extracts.

[0098] In a preferred embodiment, a protein source may be sunflower seed based. Production methods for producing sunflower-based protein may include, but are not limited to, preferably dehulling the sunflower seeds before processing and preferably texturizing the seeds to yield a product having a protein content ranging from forty to sixty percent protein, with a preferable protein concentration of approximately sixty percent.

[0099] In preferred embodiments, the addition of protein may significantly contribute to the texture of the herein described oat beverage. The proteins may stabilize air bubbles, such that the beverage may be “foamable” and “frothable”. When oat milk is frothed, proteins surround the air bubbles, forming a flexible, supportive film around the air bubbles. The aforementioned film may help trap and stabilize the air. The protein film, or “shell”, may prevent air bubbles from collapsing, such that a frothed and / or foamed oat beverage, as herein described may maintain its foamy structure even when poured over hot coffee.

[0100] In preferred embodiments, the protein additive may function to improve beverage viscosity. In preferred embodiments, the protein may bind with the water, as described above, creating a dense, thick liquid with a creamy texture. In some, preferred embodiments, wherein an oat beverage is composed of exclusively water, colloidal fine oat flour, citric acid, bacterial amylase (preferable glucoamylase), fungal amylase (preferably alpha-amylase), and a sunflower based protein source, an oat beverage may have the herein described proportions. A preferred oat beverage may be between eighty and ninety percent water, being preferably eighty-eight point four seven percent water. In some embodiments, a preferred oat beverage may be between eighty -five and ninety percent water. In alternative embodiments, an oat beverage, as disclosed herein, may be between sixty and ninety-five percent water.

[0101] Additionally, an oat beverage may also be composed of oat flour, preferably fine colloidal oat flour, such that the oat beverage contains approximately between five and twenty percent oat flour. In a preferred embodiment, an oat beverage may be eight percent colloidal oat flour. In other, preferred embodiments, an oat beverage may be composed of approximately ten percent oat flour. In some embodiments, the oat flour may be free of genetically modified components and free of particular synthetic pesticides, such that the oat flour follows the requirements for products considered “organic” as defined herein.

[0102] In preferred embodiments, an oat beverage, as herein described, may be further composed of approximately between zero point one percent and one percent bacterial amylase. In a preferred embodiment, the bacterial amylase may be a glucoamylase. In some embodiments, the oat beverage may contain zero point fourteen percent bacterial amylase.

[0103] The following is an example of an enzymic embodiment of a preferred bacterial glucoamylase and is not intended to limit the scope of the present disclosure. In some embodiments, the glucoamylase may be derived from Bacillus sp, such that the enzyme is present in an aqueous liquid having an approximate density of around one point two. In some embodiments, the enzyme may optimally perform at a temperature range between approximately seventy degrees Celsius to ninety degrees Celsius, and at an optimal pH ranging from approximately four point five to seven point zero. The enzyme may be inactivated when the substrate is heated to a temperature range of approximately ninety-five degrees Celsius to one hundred degrees Celsius from approximately between ten and twenty minutes. In some embodiments, in addition to the bacterial glucoamylase enzyme, the enzymic embodiment may include one or all the following ingredients; water, glycerol, sorbitol, and salt. In some embodiments, the enzyme containing aqueous liquid, as described above, may function to liquify starch for the subsequent production of dextrose, or enzyme- enzyme syrups. In some embodiments, the enzyme containing aqueous liquid may be used where simple viscosity reduction of starch solution is required, or to produce dextrins or modified starches. The enzymic embodiment, as herein exemplified, may have an activity of 22,500 SKB / g, and a pH ranging from approximately five to seven.

[0104] In alternative embodiments, alternative enzyme sources may be substituted for the aforementioned bacterial amylase. In some embodiments, when substituting alternative embodiments of glucoamylase, preferably bacteria-derived glucoamylase, the enzyme concentration may be consistent with the aforementioned percentages. In alternative embodiments, the concentration of glucoamylase or other bacterial amylase may differ from the aforementioned percentages when substituting alternative embodiments of amylase.

[0105] Alternative bacterial amylases may be used in place of glucoamylase and fall within the scope of this disclosure. Preferably, the enzyme used for the first hydrolysis is of bacterial origin, as bacterial amylases more effectively cleave starches at high temperatures. This results in smaller starch fragments, enhancing mouthfeel and improving the ability to trap air during foaming. The reduction in starch particle size increases the aeration potential of oat milk, enabling the formation of stable, microfoam-like bubbles essential for barista-style beverages and lattes. Although the hydrolyzed beverage may exhibit a more watery consistency compared to oat milks produced by conventional hydrolysis methods, the added protein in this formulation enhances viscosity and thickening properties without relying on excess starch. In traditional oat beverages, excess starch may inhibit foaming and frothing.

[0106] In preferred embodiments, an oat beverage, as herein described, may undergo a second hydrolysis with a fungal amylase, and preferably a fungal alpha-amylase. The second hydrolysis may occur at a lower temperature, such that the bacterial amylase from the first hydrolysis is not active at the low temperature, thereby preventing over hydrolysis. It is preferable that the second hydrolysis be mild and, therefore be performed with a fungal amylase at lower temperatures, thereby preserving some starch integrity to support air bubble retention during frothing and additionally to prevent an excess of simple sugars in the final product.

[0107] In a preferred embodiment, the fungal amylase may be a fungal-derived derived alpha-amylase, preferably at a proportion of approximately between zero point one and one percent (0.1% to 1%) of the final oat beverage composition. In some embodiments, the oat beverage may contain approximately zero-point eight percent (0.8%) fungal -derived alphaamylase.

[0108] The following is an example of an enzymic embodiment of a preferred bacterial glucoamylase and is not intended to limit the scope of the present disclosure. In some embodiments, the alpha-amylase may be a concentrated food grade fungal alpha amylase enzyme produced from Aspergillus oryzae, with very low proteolytic activity. The enzyme may be stored in the form of a low viscosity liquid, that may be easily mixed with a substrate, having a specific gravity of approximately one point twenty-six. In some embodiments, the enzyme may have a high saccharifying activity in an environment having an approximate pH range of four to six point four, with an optimum environmental pH of five point two to five point eight. Over long incubation times, the enzymic product may be stable at a temperature range of fifty to fifty -five degrees Celsius. Over shorter incubation times, the enzymic product may be stable at a temperature ranging from fifty -five degrees Celsius to fifty-seven degrees Celsius. The enzymic product does not require activators and is sensitive to heavy metals. Metals such as Fe+, Hg+, Ag+ and Sn4+ may inhibit enzymic activity. The action of the enzyme on gelatinized starch results in a breakdown of starch to dextrins and maltose. The enzymic product may function for rapid starch degradation. In some embodiments, in addition to the fungal alpha-amylase enzyme, the enzymic product may include one or all the following ingredients; water, sorbitol, sodium chloride, and potassium sorbate. The enzymic embodiment, as herein exemplified, may have an activity of 31,500-38,500 SKB / g, and a pH ranging from approximately five point five to seven.

[0109] In some embodiments, alternative sources of fungal amylase, preferably fungal alphaamylase, may be substituted for the aforementioned fungal amylase. In some embodiments, when substituting alternative embodiments of amylase, the concentration of amylase may be consistent with the aforementioned percentages. In alternative embodiments, the enzyme concentration may differ from the aforementioned percentages. In some alternative embodiments, fungal alpha amylase sources may include, but are not limited to, enzymes supplied by American Biosystems, Ultreze Enzymes, Lallemand Brewing, Noor Enzymes Group, Autozyme Biotech, and Creative Enzymes. Alternative sources of fungal amylase are also satisfactory and fall within the scope of the present disclosure. In some embodiments, alpha-amylose may be substituted by alternative fungal -amylases. In some preferred embodiments, citric acid may be added to the oat beverage composition such that, in some embodiments, the citric acid may function as a pH stabilizer. In a preferred embodiment, the citric acid may function to lower the beverage pH to an approximate pH of six. A low-pH oat beverage may be preferable for admixture with coffee, as coffee’s natural acidity may, in some embodiments, interact poorly with higher-pH oat milks, leading to curdling or separation. With a lower pH, the herein described oat beverage may have preferred stability in coffee, preserving a smooth texture and creamy appearance devoid of clumping. The pH adjustment, which may in some embodiments be performed with citric acid, may optimize the herein described oat beverages' “barista-grade” appeal, with the term “barista grade” being known to those familiar with the art of oat beverage production.

[0110] Additionally, in some embodiments, citric acid may additionally function as a mechanism for preventing enzymic oxidation and browning, a mechanism for preventing spoilage and bacterial growth, and a method for chelating metal ions. In preferred embodiments, citric acid may function to optimize enzyme activity, prevent discoloration, enhance flavor, and improve shelf stability. In preferred embodiments, the herein described oat beverage may include approximately between five-thousandths percent (0.005%) citric acid and five-hundredths percent (0.05%) citric acid, with a preferable citric acid concentration of approximately one-hundredth percent (0.01%).

[0111] In some embodiments, alternative pH stabilizers and preservatives may be used in place of citric acid. A single agent can serve as a direct substitute, or multiple agents may work synergistically to replicate its functions. For example, lactic acid, malic acid, or tartaric acid can stabilize pH, while acetic acid may offer antioxidant and anti -browning properties. Additionally, sodium citrate or phosphoric acid can replace citric acid’s chelating function. In some embodiments, alternatives to citric acid may be added in the same proportion as citric acid, as described above. In other embodiments, alternatives to citric acid may make up a different percentage of the final oat beverage composition.

[0112] Oat beverage production methods currently known in the art often conduct a first hydrolysis at an approximate temperature of seventy-one degrees Celsius. Such relatively low temperatures may produce a beverage with a thick and creamy mouthfeel, hindering efficient starch breakdown, thereby producing a less smooth product. The herein described oat beverage may be produced at a higher temperature, with a first hydrolysis occurring at a preferable temperature of approximately seventy-seven to eighty-two degrees Celsius, such that starch is effectively hydrolyzed and thoroughly cleaved. To provide a thick, creamy mouthfeel, the herein described oat beverage may be fortified with protein, such that the added protein produces a similar thick and creamy mouthfeel without compromising the smoothness of the beverage.

[0113] In some embodiments, the oat beverage described herein may include some or all of the aforementioned ingredients, including, but not limited to, water, oat flour, citric acid (or other suitable agents), bacterial amylase, fungal amylase (or other enzymes as discussed above), and a protein source. Additionally, in certain embodiments, the oat beverage may contain at least one additive, such as an adaptogen.

[0114] In preferred embodiments, adaptogens may include, but are not limited to, L-theanine, ginseng extract, and ashwagandha. When additives are incorporated, the oat beverage composition may be adjusted accordingly. In a preferred embodiment, the percentage of water may be reduced to accommodate the additives. However, while the water content decreases, the proportions of oat flour, citric acid, amylases, and protein preferably remain as described above.

[0115] In a preferred oat beverage, containing adaptogens, the oat beverage’s proportion of water may decrease slightly, such that, in a preferred embodiment, the beverage’s water content may decrease to approximately eighty-point twenty two percent water, such that at least one adaptogen or adaptogenic extract may replace a proportion of the water. In a preferred embodiment, the adjusted water content may be partially compensated for by L- theanine, such that the proportion of L-theanine in the final oat beverage composition may, preferably, be approximately between one-hundredth and nine-hundredth, with a preferred proportion of five-hundredth percent (0.05%), of the total oat beverage composition.

[0116] Additionally, in a preferred “adaptogenic” embodiment of the herein described oat beverage, as described above, an oat beverage may also contain ginseng extract. In some embodiments, it may be preferable that the ginseng extract be organic in origin, such that the ginseng is grown without and the extract of free of synthetic chemicals, genetically modified organisms, or ingredients that are prohibited to be used in “organic” products, as defined by the United States Department of Agriculture.

[0117] In a preferred embodiment, the adjusted water content may be further partially compensated for by ginseng extract, such that the proportion of ginseng extract in the final oat beverage composition may, preferably, be approximately between a one hundredth and one percent, with a preferred proportion of approximately one tenth percent of the total oat beverage composition.

[0118] Furthermore, in a preferred “adaptogenic” embodiment of the herein described oat beverage, as described above, an oat beverage may also contain ashwagandha. In some embodiments, it may be preferable that the ashwagandha be organic in origin, such that the ashwagandha is grown without and is free of synthetic chemicals, genetically modified organisms, or ingredients that are prohibited to be used in “organic” products, as defined by the United States Department of Agriculture.

[0119] In a preferred embodiment, the adjusted water content may be further partially compensated for by ashwagandha, such that the proportion of ashwagandha in the final oat beverage composition may, preferably, be approximately between a one hundredth and one percent (0.01% to 1%), with a preferred proportion of approximately one tenth percent (0.1%) of the total oat beverage composition.

[0120] In some alternative embodiments, the final oat beverage composition may include a single adaptogen. In other embodiments, a combination of two of the aforementioned adaptogens may be incorporated. Additionally, adaptogens not specifically listed herein may be included, either in place of or in addition to those described.

[0121] Adaptogens may be added in any proportion; however, it is preferable that their total composition ranges between point one percent (0.1%) and one percent of the final oat beverage. A particularly preferred proportion is approximately a quarter of a percent (0.25%) of the total composition, such that the proportion of suggested serving size is comparable to recommended daily dosage range of each particular adaptogen and / or adheres to concentration limitations by the FDA or other regulatory bodies.

[0122] In other, alternative preferred embodiments, an oat beverage, as described herein, may be flavored, such that a flavoring agent may be added to the ingredients described herein. In a preferred embodiment, a flavored oat beverage may include some or all of the aforementioned ingredients, including, but not limited to, water, oat flour, citric acid (or other suitable agents), bacterial amylase, fungal amylase, and a protein source. Additionally, in certain embodiments, the flavored oat beverage may contain at least one flavoring additive, such as, but not limited to, vanilla extract, coco powder, or other such flavoring agents.

[0123] In a preferred vanilla-flavored oat beverage, the oat beverage’s proportion of water may be slightly adjusted, such that a flavoring agent may replace a proportion of the water. In a preferred embodiment, the adjusted water content may be compensated for by vanilla extract, such that the proportion of vanilla extract in the final oat beverage composition may, preferably, be approximately between point sixty-eight percent (0.68%) and three percent, depending on the strength of the vanilla extract.

[0124] For example, in a preferred embodiment, double-strength vanilla extract may be used. In such embodiments, the proportion of water in the oat beverage may decrease to approximately eighty-seven point seventy-nine percent, while the percentage of double strength vanilla extract may be point sixty-eight percent. Alternatively, if single-strength vanilla extract is used, the proportion of water in the oat beverage may decrease to approximately eighty-seven point eleven percent, while the percentage of double-strength vanilla extract may be one point thirty-six percent of the total oat beverage composition.

[0125] In some preferred embodiments, chocolate flavor may be added to an oat beverage. In a preferred embodiment, the chocolate flavor may be, but is not necessarily limited to, coco powder. In such embodiments, chocolate flavored oat milk may be, but is not necessarily composed of some or all of the following ingredients: water, oat flour, citric acid (or other suitable agents), bacterial amylase, fungal amylase (or other enzymes as discussed above), a protein source, cocoa powder, and chocolate flavor, natural flavors, or other such flavoring agents.

[0126] In a preferred chocolate-flavored oat beverage, the oat beverage’s proportion of water may be slightly adjusted, such that a flavoring agent or plurality of flavoring agents may replace a proportion of the water. In some chocolate-flavored embodiments, water content may be adjusted, such that the final oat beverage composition is between eighty-five and eighty-seven percent water, with a preferable water content of approximately eighty-six point seventy -two.

[0127] In a preferred embodiment, the adjusted water content may be compensated for by cocoa powder and flavor agents (preferably chocolate flavor with other natural flavors), such that the proportion of cocoa powder in the final oat beverage may be preferably between zero point five and one percent of the total oat beverage composition. In a preferred embodiment, an oat beverage as herein disclosed may have a final cocoa powder content of preferably zero point seventy-five percent. A preferred chocolate-flavored oat beverage may also have natural or artificial flavors, such that flavoring agents may be between point five and three percent of the final oat beverage composition. It is preferable that flavoring agents make up approximately one percent of the final oat beverage.

[0128] Exemplary Embodiments of Oat Beverage Processing Methods

[0129] As described in detail herein above, in some embodiments, an oat milk base may, but does not necessarily include, water, oat flour, citric acid (or other such agent(s)), bacterial amylase (preferably bacterial amylase), fungal amylase (preferably fungal alpha-amylase), and a protein source.

[0130] In an exemplary embodiment, it is preferable that all equipment be sanitized or sterile before oat milk production begins. Equipment may include but is not limited to, at least one kettle, a plurality of food storage containers which may include, but are not limited to a round Cambro, a stirring mechanism, including but not limited to a stirring spoon or a stirring rod, an appropriately sized ice bath, as discussed below, a whisk, a pH test mechanism (such as, but not limited to pH test strips), blending mechanism, preferably an immersion blender, and bottles with a closing mechanism, such as but not limited to lids.

[0131] All measurements in the following exemplary processes may follow the proportions discussed above; in alternative embodiments, the proportions may be adjusted. In an exemplary embodiment, oat beverage production may include first heating water, preferably in a kettle, to approximately sixty degrees Celsius.

[0132] After the water is heated, it is preferable that the water be mixed with the oat flour. In some embodiments, water may first be transferred from the heat source to a food storage container, such that the food storage container is large enough to accommodate the water and oat flour. Once the water is combined with the oat flour, the water and oat flour may be blended. In embodiments where water and oat flour are combined in a food storage container, an immersion blender may be used to properly blend the water and oat flour. It is preferable that, if using an immersion blender, the oat flour and water be mixed with an immersion blender for between two and four minutes, and approximately three minutes, such that the slurry is fully solubilized. In alternative embodiments, water and oat flour may be combined in a traditional or stand blender. In such embodiments, the blend time may be adjusted as needed to fully solubilize the slurry. In some embodiments, to properly blend the slurry, the oat and water mixture may first be added to a stand blender, such as but not limited to a Ninja stand blender, after which the mixture may be further blended with an immersion blender, such that the oats and water are fully mixed. Once the slurry is solubilized, citric acid may be added, such that the slurry reaches a pH of preferably between five point four and five point nine. After reaching the target pH, the slurry may be heated again; in some embodiments, the slurry may be reheated in a kettle. Alternatively, the slurry may be transferred to or already set in a heat-resistant container such that the slurry may be heated on a heating element, such as but not limited to a stove. It is preferable that the slurry be heated to a temperature of seventy-five to eighty-five degrees Celsius, with a preferable temperature of seventy-seven to eighty-two degrees Celsius. The aforementioned temperature range is preferable for the first enzymic hydrolysis, as discussed below, such that the rate of starch breakdown, particularly alpha 1-4 linkages, is rapid and thorough. In other embodiments, known to those in the art, first enzymatic hydrolysis might occur at a slightly lower temperature. The herein disclosed temperature increase is preferable as the increased temperature provides the thermal energy necessary for the enzyme access and cleaves the alpha 1,4 glycosidic bonds more thoroughly.

[0133] It is preferable that the first enzymatic hydrolysis be performed using an enzyme that does not efficiently cleave a-1,6 glycosidic bonds, such as, but not limited to, bacterial glucoamylase. These a-1,6 glycosidic bonds are highly branched and do not form a gel when mixed with water. Consequently, when retained in an oat beverage, as disclosed herein, they contribute to a non-gelling viscosity, resulting in a texture that is thick enough to create microfoam yet fluid enough to steam and pour effectively.

[0134] Additionally, retaining a-1,6 glycosidic bonds in the final oat beverage is advantageous because the branched chains resist rapid collapse, thereby helping to trap air bubbles during frothing, facilitating the formation of a uniform, stable foam without the need for emulsifiers or thickeners. Furthermore, preserving a-1,6 glycosidic bonds ensure the retention of soluble fibers such as P-glucans. P-glucans may offer digestive benefits, support cholesterol management, and help moderate the beverage’s impact on the consumer’s glycemic index, thereby enhancing the beverage's nutritional value.

[0135] To effectively and completely hydrolyze the 1,4 glycosidic bonds while retaining the 1,6 glycosidic bonds, it is preferable that a bacterial amylase, preferably bacterial glucoamylase, as described above, be added to the aforementioned slurry once the slurry reaches the preferred, aforementioned temperature range. Alternatively, in alternative embodiments, other enzymes may be substituted for glucoamylase. In a preferred embodiment, the amylase may be stirred into the oat flour and water slurry, thereby forming what is herein referred to as the mixture. To ensure optimal enzymatic activity, as described above, the mixture should be maintained at a temperature between seventy-seven and eighty- two degrees Celsius for approximately seventy-five minutes. In a preferred embodiment, the mixture may be stirred at regular intervals, preferably approximately every five to ten minutes, throughout the seventy-five-minute period. In some alternative embodiments, the mixture may be stirred at alternative intervals, including, but not limited to, every four to eleven minutes.

[0136] After the completion of the seventy-five-minute period, it is preferable that the mixture be transferred to an ice bath, such that the mixture may cool, preferably to a temperature ranging between fifty and fifty-five degrees Celsius. In a preferred embodiment, the mixture may be transferred out of the kettle into a container such that the container may be placed in the ice bath. Subsequently, while the mixture is cooling in the ice bath, it is preferable that, in some embodiments, the kettle be turned off and rinsed out with cool water.

[0137] Once the mixture, as described above, cools, preferably to a temperature of between approximately every fifty and fifty-five degrees Celsius, the mixture may be transferred back to the kettle. Alternatively, the mixture may be transferred to an alternative kettle. In some embodiments, the mixture may be placed on or in a different heat source, including but not limited to a gas, electric, or induction stovetop. It is preferable that fungal amylase, preferably fungal alpha-amylase, then be added to the mixture. In some embodiments, an alternative enzyme may be added additionally or alternatively. In some embodiments, the enzyme may be stirred or otherwise distributed through the mixture.

[0138] Preferably, after the addition of fungal amylase, the mixture may be maintained at a temperature between fifty degrees Celsius and fifty -five degrees Celsius for approximately thirty minutes. In some embodiments, a kettle or other heat source may be used to ensure that the mixture remains within this preferred temperature range. Alternatively, in certain embodiments, the mixture may be maintained within the desired temperature range using a sots vis or a similar device designed to regulate temperature. In some embodiments, the kettle may have a dial, such that the dial may be adjusted for temperature regulation.

[0139] In embodiments where the mixture temperature is maintained in a kettle, it is preferable that the kettle temperature be continuously monitored, such that the kettle may be raised or lowered to ensure that the mixture remains in the preferable temperature range. In some embodiments, the kettle settings may need to be adjusted between “one” and “three” such that the kettle temperature is raised and lowered as necessary to maintain a constant temperature range of fifty to fifty-five degrees.

[0140] The temperature range of fifty to fifty-five degrees is preferable to avoid over hydrolysis as the enzyme from the aforementioned first hydrolysis is not properly active at a tempter of fifty to fifty-five degrees. Additionally, keeping the temperature relatively low may keep the fungal amylase activity mild, thereby preventing an excessive increase in simple sugars in the final product. At higher temperatures, fungal amylase activity may be more aggressive, thereby leading to over-hydrolysis and thinner consistency beverage, which compromises foaming stability. In contrast, maintaining the optimal low temperature preserves some starch integrity, further supporting air bubble retention during frothing.

[0141] After a timespan of approximately thirty minutes (plus or minus five minutes), a protein source, such as, but not limited to sunflower protein powder may be whisked into the mixture, after which the mixture may be strained / filtered and heated to a temperature of preferably ninety-one degrees Celsius (plus or minus 5 degrees Celsius). In some embodiments, the mixture may be heated in a kettle, including but not limited to the same kettle used in the aforementioned steps. In some embodiments, the kettle may be rinsed; in other embodiments, the kettle may not be rinsed between the aforementioned glucoamylase heating step and the herein described protein heating step. In other embodiments, the mixture may be heated in a container set on a heating element. In other embodiments, the mixture may be heated in a container set with a sois vis or other such device designed to regulate the temperature of a liquid.

[0142] Once the mixture is heated to a temperature of approximately ninety-one degrees Celsius, the mixture may be placed in an ice bath, such that the mixture may cool to a preferable temperature of approximately between seventy and eighty degrees Celsius. In some embodiments, the mixture may be transferred out of the kettle and into a separate container, such that the container may be placed in an ice bath. In alternative embodiments, the mixture may be removed from a heat source and set in the ice bath, such that the mixture cools to a preferred temperature range of approximately seventy to eighty degrees Celsius (plus or minus five degrees Celsius).

[0143] Once the mixture reaches the preferred temperature range, it may be blended, preferably with an immersion blender, such that a smooth, homogeneous consistency is reached. The texture may be adjusted as needed to meet the desired consistency. Alternatively, a stand blender or another such suitable blending tool may be used. Once a desired consistency is reached, the mixture may be refrigerated, such that the beverage reaches refrigeration temperatures. In a preferred embodiment, the beverage may be packaged in appropriately sized, sanitized containers, including but not limited to bottles, jars, canisters, or other such storage containers.

[0144] In some preferred embodiments, at least one adaptogen, as described above, may be added to the beverage. In a preferred embodiment, the adaptogenic beverage may be produced by first heating water, preferably in a kettle, to approximately sixty degrees Celsius.

[0145] After the water is heated, it is preferable that the water be mixed with the oat flour. In some embodiments, water may first be transferred from the heat source to a food storage container, such that the food storage container is large enough to accommodate the water and oat flour. Once the water is combined with the oat flour, the water and oat flour may be blended. In embodiments where water and oat flour are combined in a food storage container, an immersion blender may be used to properly blend the water and oat flour. It is preferable that, if using an immersion blender, the oat flour and water be mixed with an immersion blender for between two and four minutes, and approximately three minutes, such that the slurry is fully solubilized. In alternative embodiments, water and oat flour may be combined in a traditional or stand blender. In such embodiments, the blend time may be adjusted as needed to fully solubilize the slurry.

[0146] Once the slurry is solubilized, citric acid may be added, such that the slurry reaches a pH of preferably between five point four and five point nine. After reaching the target pH, the slurry may be heated again; in some embodiments, the slurry may be reheated in a kettle. Alternatively, the slurry may be transferred to or alternatively already set in a heat-resistant container such that the slurry may be heated on a heating element, such as but not limited to a stove. It is preferable that the slurry be heated to a temperature of seventy -five to eighty-five degrees Celsius, with a preferable temperature of seventy-seven to eighty-two degrees Celsius.

[0147] Once the slurry reaches the preferred temperature range, it is preferable that bacterial amylase, preferably bacterial glucoamylase. Alternatively, in alternative embodiments, other enzymes may be substituted for glucoamylase. In a preferred embodiment, the amylase may be stirred into the oat flour and water slurry, thereby forming what is herein referred to as the mixture. To ensure optimal enzymatic activity, the mixture should be maintained at a temperature between seventy-seven and eighty-two degrees Celsius for approximately seventy -five minutes. In a preferred embodiment, the mixture may be stirred at regular intervals, preferably approximately every five to ten minutes, throughout the seventy-five- minute period. In some alternative embodiments, the mixture may be stirred at alternative intervals, including, but not limited to, every four to eleven minutes.

[0148] It is preferable that the first enzymatic hydrolysis be performed using an enzyme that does not efficiently cleave a-1,6 glycosidic bonds, such as, but not limited to, bacterial glucoamylase. These a-1,6 glycosidic bonds are highly branched and do not form a gel when mixed with water. Consequently, when retained in an oat beverage, as disclosed herein, they contribute to a non-gelling viscosity, resulting in a texture that is thick enough to create microfoam yet fluid enough to steam and pour effectively.

[0149] Additionally, retaining a-1,6 glycosidic bonds in the final oat beverage is advantageous because the branched chains resist rapid collapse, thereby helping to trap air bubbles during frothing, facilitating the formation of a uniform, stable foam without the need for emulsifiers or thickeners. Furthermore, preserving a-1,6 glycosidic bonds ensures the retention of soluble fibers such as P-glucans. P-glucans may offer digestive benefits, support cholesterol management, and help moderate the beverage’s impact on the consumer’s glycemic index, thereby enhancing the beverage's nutritional value.

[0150] To effectively and completely hydrolyze the 1,4 glycosidic bonds while retaining the 1,6 glycosidic bonds, it is preferable that a bacterial amylase, preferably bacterial glucoamylase, as described above, be added to the aforementioned slurry once the slurry reaches the preferred, aforementioned temperature range. Alternatively, in alternative embodiments, other enzymes may be substituted for glucoamylase. In a preferred embodiment, the amylase may be stirred into the oat flour and water slurry, thereby forming what is herein referred to as the mixture. To ensure optimal enzymatic activity, as described above, the mixture should be maintained at a temperature between seventy-seven and eighty- two degrees Celsius for approximately seventy-five minutes. In a preferred embodiment, the mixture may be stirred at regular intervals, preferably approximately every five to ten minutes, throughout the seventy-five-minute period. In some alternative embodiments, the mixture may be stirred at alternative intervals, including, but not limited to, every four to eleven minutes. After the completion of the seventy-five minutes, it is preferable that the mixture be transferred to an ice bath, such that the mixture may cool, preferably to a temperature ranging between fifty and fifty-five degrees Celsius. In a preferred embodiment, the mixture may be transferred out of the kettle into a container such that the container may be placed in the ice bath. Subsequently, while the mixture is cooling in the ice bath, it is preferable that, in some embodiments, the kettle be turned off and rinsed out with cool water.

[0151] Once the mixture, as described above, cools, preferably to a temperature of between approximately every fifty and fifty-five degrees Celsius, the mixture may be transferred back to the kettle. Alternatively, the mixture may be transferred to an alternative kettle. In some embodiments, the mixture may be placed on or in a different heat source, including but not limited to a gas, electric, or induction stovetop. It is preferable that a fungal amylase, preferably fungal alpha-amylase, then be added to the mixture. In some embodiments, an alternative enzyme may be added additionally or alternatively. In some embodiments, the enzyme may be stirred or otherwise distributed through the mixture.

[0152] The temperature range of fifty to fifty-five degrees is preferable to avoid over hydrolysis as the enzyme from the aforementioned first hydrolysis is not properly active at a tempter of fifty to fifty-five degrees. Additionally, keeping the temperature relatively low may keep the fungal amylase activity mild, thereby preventing an excessive increase in simple sugars in the final product. At higher temperatures, fungal amylase activity may be more aggressive, thereby leading to over-hydrolysis and thinner consistency beverage, which compromises foaming stability. In contrast, maintaining the optimal low temperature preserves some starch integrity, further supporting air bubble retention during frothing.

[0153] Preferably, after the addition of the fungal amylase, the mixture may be maintained at a temperature between fifty degrees Celsius and fifty-five degrees Celsius for approximately thirty minutes. In some embodiments, a kettle or other heat source may be used to ensure that the mixture remains within this preferred temperature range. Alternatively, in certain embodiments, the mixture may be maintained within the desired temperature range using a sots vis or a similar device designed to regulate temperature. In some embodiments, the kettle may have a dial, such that the dial may be adjusted for temperature regulation.

[0154] In embodiments where the mixture temperature is maintained in a kettle, it is preferable that the kettle temperature be continuously monitored, such that the kettle may be raised or lowered to ensure that the mixture remains in the preferable temperature range. In some embodiments, the kettle settings may need to be adjusted between “one” and “three” such that the kettle temperature is raised and lowered as necessary to maintain a constant temperature range of fifty to fifty-five degrees.

[0155] After a timespan of approximately thirty minutes (plus or minus five minutes), a protein source, such as, but not limited to sunflower protein powder and at least one adaptogen, including but not limited to L theanine, ashwagandha, and / or ginseng extract may be whisked into the mixture, after which the mixture may be strained / filtered and heated to a temperature of preferably ninety-one degrees Celsius (plus or minus 5 degrees Celsius). In some embodiments, the mixture may be heated in a kettle, including but not limited to the same kettle used in the aforementioned steps. In some embodiments, the kettle may be rinsed; in other embodiments, the kettle may not be rinsed between the aforementioned glucoamylase heating step and the herein described protein heating step. In other embodiments, the mixture may be heated in a container set on a heating element. In other embodiments, the mixture may be heated in a container set with a sois vis or other such device designed to regulate the temperature of a liquid.

[0156] Once the mixture is heated to a temperature of approximately ninety-one degrees Celsius, the mixture may be placed in an ice bath, such that the mixture may cool to a preferable temperature of approximately between seventy and eighty degrees Celsius. In some embodiments, the mixture may be transferred out of the kettle and into a separate container, such that the container may be placed in an ice bath. In alternative embodiments, the mixture may be removed from a heat source and set in the ice bath, such that the mixture cools to a preferred temperature range of approximately seventy to eighty degrees Celsius (plus or minus five degrees Celsius).

[0157] Once the mixture reaches the preferred temperature range, it may be blended, preferably with an immersion blender, such that a smooth, homogeneous consistency is reached. The texture may be adjusted as needed to meet the desired consistency. Alternatively, a stand blender or another such suitable blending tool may be used. Once a desired consistency is reached, the mixture may be refrigerated, such that the beverage reaches refrigeration temperatures. In a preferred embodiment, the beverage may be packaged in appropriately sized, sanitized containers, including but not limited to bottles, jars, canisters, or other such storage containers. In some preferred embodiments, the beverage may be flavored. An exemplary method for producing a flavored beverage may involve first heating water, preferably in a kettle, to approximately sixty degrees Celsius.

[0158] After the water is heated, it is preferable that the water be mixed with the oat flour. In some embodiments, water may first be transferred from the heat source to a food storage container, such that the food storage container is large enough to accommodate the water and oat flour. Once the water is combined with the oat flour, the water and oat flour may be blended. In embodiments where water and oat flour are combined in a food storage container, an immersion blender may be used to properly blend the water and oat flour. It is preferable that, if using an immersion blender, the oat flour and water be mixed with an immersion blender for between two and four minutes, and approximately three minutes, such that the slurry is fully solubilized. In alternative embodiments, water and oat flour may be combined in a traditional or stand blender. In such embodiments, the blend time may be adjusted as needed to fully solubilize the slurry.

[0159] Once the slurry is solubilized, citric acid may be added, such that the slurry reaches a pH of preferably between five point four and five point nine. After reaching the target pH, the slurry may be heated again; in some embodiments, the slurry may be reheated in a kettle. Alternatively, the slurry may be transferred to or alternatively already set in a heat-resistant container such that the slurry may be heated on a heating element, such as but not limited to a stove. It is preferable that the slurry be heated to a temperature of seventy -five to eighty-five degrees Celsius, with a preferable temperature of seventy-seven to eighty-two degrees Celsius.

[0160] Once the slurry reaches the preferred temperature range, it is preferable that bacterial amylase, preferably bacterial glucoamylase, be added to the slurry. Alternatively, in alternative embodiments, other enzymes may be substituted for glucoamylase. In a preferred embodiment, the amylase may be stirred into the oat flour and water slurry, thereby forming what is herein referred to as the mixture. To ensure optimal enzymatic activity, the mixture should be maintained at a temperature between seventy-seven and eighty-two degrees Celsius for approximately seventy-five minutes. In a preferred embodiment, the mixture may be stirred at regular intervals, preferably approximately every five to ten minutes, throughout the seventy -five-minute period. In some alternative embodiments, the mixture may be stirred at alternative intervals, including, but not limited to, every four to eleven minutes. It is preferable that the first enzymatic hydrolysis be performed using an enzyme that does not efficiently cleave a- 1,6 glycosidic bonds, such as, but not limited to, bacterial glucoamylase. These a-1,6 glycosidic bonds are highly branched and do not form a gel when mixed with water. Consequently, when retained in an oat beverage, as disclosed herein, they contribute to a non-gelling viscosity, resulting in a texture that is thick enough to create microfoam yet fluid enough to steam and pour effectively.

[0161] Additionally, retaining a-1,6 glycosidic bonds in the final oat beverage is advantageous because the branched chains resist rapid collapse, helping to trap air bubbles during frothing, facilitating the formation of a uniform, stable foam without the need for emulsifiers or thickeners. Furthermore, preserving a-1,6 glycosidic bonds ensures the retention of soluble fibers such as P-glucans. P-glucans may offer digestive benefits, support cholesterol management, and help moderate the beverage’s impact on the consumer’s glycemic index, thereby enhancing the beverage's nutritional value.

[0162] To effectively and completely hydrolyze the 1,4 glycosidic bonds while retaining the 1,6 glycosidic bonds, it is preferable that a bacterial amylase, preferably bacterial glucoamylase, as described above, be added to the aforementioned slurry once the slurry reaches the preferred, aforementioned temperature range. Alternatively, in alternative embodiments, other enzymes may be substituted for glucoamylase. In a preferred embodiment, the amylase may be stirred into the oat flour and water slurry, thereby forming what is herein referred to as the mixture. To ensure optimal enzymatic activity, as described above, the mixture should be maintained at a temperature between seventy-seven and eighty- two degrees Celsius for approximately seventy-five minutes. In a preferred embodiment, the mixture may be stirred at regular intervals, preferably approximately every five to ten minutes, throughout the seventy-five-minute period. In some alternative embodiments, the mixture may be stirred at alternative intervals, including, but not limited to, every four to eleven minutes.

[0163] After the completion of the seventy-five-minute period, it is preferable that the mixture be transferred to an ice bath, such that the mixture may cool, preferably to a temperature ranging between fifty and fifty-five degrees Celsius. In a preferred embodiment, the mixture may be transferred out of the kettle into a container such that the container may be placed in the ice bath. Subsequently, while the mixture is cooling in the ice bath, it is preferable that, in some embodiments, the kettle be turned off and rinsed out with cool water. Once the mixture, as described above, cools, preferably to a temperature of between approximately every fifty and fifty-five degrees Celsius, the mixture may be transferred back to the kettle. Alternatively, the mixture may be transferred to an alternative kettle. In some embodiments, the mixture may be placed on or in a different heat source, including but not limited to a gas, electric, or induction stovetop. It is preferable that fungal amylase, preferably of fungal alpha-amylase, then be added to the mixture. In some embodiments, an alternative enzyme may be added additionally or alternatively. In some embodiments, the enzyme may be stirred or otherwise distributed through the mixture.

[0164] Preferably, after the addition of fungal amylase, the mixture may be maintained at a temperature between fifty degrees Celsius and fifty -five degrees Celsius for approximately thirty minutes. In some embodiments, a kettle or other heat source may be used to ensure that the mixture remains within this preferred temperature range. Alternatively, in certain embodiments, the mixture may be maintained within the desired temperature range using a sots vis or a similar device designed to regulate temperature. In some embodiments, the kettle may have a dial, such that the dial may be adjusted for temperature regulation.

[0165] The temperature range of fifty to fifty-five degrees is preferable to avoid over hydrolysis as the enzyme from the aforementioned first hydrolysis is not properly active at a tempter of fifty to fifty-five degrees. Additionally, keeping the temperature relatively low may keep the fungal amylase activity mild, thereby preventing an excessive increase in simple sugars in the final product. At higher temperatures, fungal amylase activity may be more aggressive, thereby leading to over-hydrolysis and thinner consistency beverage, which compromises foaming stability. In contrast, maintaining the optimal low temperature preserves some starch integrity, further supporting air bubble retention during frothing.

[0166] In embodiments where the mixture temperature is maintained in a kettle, it is preferable that the kettle temperature be continuously monitored, such that the kettle may be raised or lowered to ensure that the mixture remains in the preferable temperature range. In some embodiments, the kettle settings may need to be adjusted between “one” and “three” such that the kettle temperature is raised and lowered as necessary to maintain a constant temperature range of fifty to fifty-five degrees.

[0167] After a timespan of approximately thirty minutes (plus or minus five minutes), a protein source, such as, but not limited to sunflower protein powder, and a flavoring agent, including but not limited to vanilla extract, cocoa powder, chocolate flavor, natural flavors, and / or artificial flavors may be whisked into the mixture, additionally, after which the mixture may be strained, filtered, and heated to a temperature of preferably ninety-one degrees Celsius (plus or minus 5 degrees Celsius). In some embodiments, the mixture may be heated in a kettle, including but not limited to the same kettle used in the aforementioned steps. In some embodiments, the kettle may be rinsed; in other embodiments, the kettle may not be rinsed between the aforementioned glucoamylase heating step and the described protein heating step. In other embodiments, the mixture may be heated in a container set on a heating element. In other embodiments, the mixture may be heated in a container set with a sois vis or other such device designed to regulate the temperature of a liquid.

[0168] Once the mixture is heated to a temperature of approximately ninety-one degrees Celsius, the mixture may be placed in an ice bath, such that the mixture may cool to a preferable temperature of approximately between seventy and eighty degrees Celsius. In some embodiments, the mixture may be transferred out of the kettle and into a separate container, such that the container may be placed in an ice bath. In alternative embodiments, the mixture may be removed from a heat source and set in the ice bath, such that the mixture cools to a preferred temperature range of approximately seventy to eighty degrees Celsius (plus or minus five degrees Celsius).

[0169] Once the mixture reaches the preferred temperature range, it may be blended, preferably with an immersion blender, such that a smooth, homogeneous consistency is reached. The texture may be adjusted as needed to meet the desired consistency. Alternatively, a stand blender or another such suitable blending tool may be used. Once a desired consistency is reached, the mixture may be refrigerated, such that the beverage reaches refrigeration temperatures. In a preferred embodiment, the beverage may be packaged in appropriately sized, sanitized containers, including but not limited to bottles, jars, canisters, or other such storage containers.

[0170] Aseptic Embodiments

[0171] In some embodiments, the herein described oat beverage may be produced using an aseptic process, such that the oat beverage may be shelf stable, and may remain fresh at ambient temperatures, when sealed, in excess of one year. In such embodiments, the oat beverage may be produced using a sequence of controlled unit operations including hydration, enzymatic hydrolysis, separation, thermal treatment, homogenization, and aseptic filling. The aseptic system preferably allows for continuous operation to minimize the risk of microbial and other such contamination. In a preferred embodiment, the system operates as a closed, sterile-flow production line, such that the production line is closed from initial ingredient preparation through final filling. An exemplary production line, production line 40, may be seen in Fig. 6. Such closed, sterile-flow production lines may prevent microbial ingress, thereby ensuring product safety and enabling extended production runs without intermediate sterilization shutdowns.

[0172] In some embodiments, when producing a shelf stable, aseptic oat beverage, the water used for oat hydrolysis may first be treated, such that microbes and other contaminants including heavy metals, chemicals, and other such impurities may be removed from the water. In some embodiments water may be purified via at least one of the methods listed herein. Methods for purifying water may include, but are not limited to, sand filtration, activated carbon filtration, reverse osmosis, and UV sterilization to remove particulates, organics, microbial contaminants, and dissolved solids. To produce a shelf stable, ascetic, oat beverage it is preferable that the treated water have a total dissolved solids (TDS) content below 50 ppm, in addition to being free of microbial colonies.

[0173] In a preferred embodiment, a “Hydronomic Water Treatment System”, such as one of the Hydronomic water treatment system developed by Krones AG as seen in Fig. 6 may be used to sterilize water, as described above. As seen in Fig. 6, “Hydronomic Water Treatment System” 41 may be incorporated into a closed loop oat beverage production system 40. In some embodiments, the “Hydronomic Water Treatment System” may be a “Hydronomic MF / GAC” media filtration system, such that the system filters and adsorbs any unwanted and undissolved water content including but not limited to; suspended solids, odorants, organics, chlorine, iron, manganese, etc. Using a combination of silica sand, manganese oxide, basalt and activated carbon. In some embodiments the “Hydronomic Water Treatment System” may be a “Hydronomic UF” ultra filtration system, such that water is filtered through membrane technology with hollow fibers, having an approximate preferable pore size of 0.02 pm, such that the water undergoes an ultrafiltration process. In some embodiments, the “Hydronomic Water Treatment System” may be a “Hydronomic RO” reverse osmosis system, such that water is desalinated with membrane technology in a reverse osmosis technology where the wound membrane module is flushed tangentially.

[0174] In a preferred embodiment, as seen in Fig. 7, “Hydronomic Water Treatment System” 41 will include Hydronomic MF system 42, Hydronomic UF system 43, and Hydronomic RO system 44, such that water is directed in a sequential flow path, first through the MF system 42, thereafter through the UF system 43, and subsequently through the RO system 44, such that each successive module receives the effluent of the preceding module, thereby ensuring progressive purification and preparation of process water suitable for aseptic beverage production.

[0175] As seen in Fig. 6, after water is properly filtered, the purified water may flow from Hydronomic Water Treatment System 41 into a high shear mixing tank, such as but not limited to “pre-masher” 45, wherein the purified water may be mixed with oats, oat flakes, or oat flour to produce an oat-water slurry, as discussed above.

[0176] As seen in Fig. 8, pre-masher 45 may include top feed 46 and side feed 47 such that, in some embodiments, oats or oat products such as oat flakes and / or oat flour may enter pre- masher 45 via top feed 46, while purified water may enter pre-masher 45 via side feed 47. In some embodiments, a pocket (not shown) may be set with pre-masher 45, such that the water is fed into the pocket, horizontally, such that the oat / oat product and water combine with one another in the pocket (not shown).

[0177] In a preferred embodiment, the pre-masher unit is configured to maximize contact and mixture between the oat particles and water. Therefore, in a preferred embodiment, swirl vanes (not shown) may be set at the nozzle outlet (not shown) of the ingredient feed pocket (not shown), such that the swirl vanes may induce increased turbulence within the mixing zone (not shown). Additionally, downstream of the pocket, the flow path of the oat / water mixture may have a reduced diameter, thereby increasing the flow velocity of the mixture, and causing the oats / oat flakes / oat flour to expand rapidly. This controlled hydrodynamic expansion promotes thorough intermixing by dispersing the solid particles uniformly throughout the liquid phase. The swirl vanes, and decreased diameter may, in combination, facilitate intimate contact between the fine solid particles and the water, thereby optimizing hydration and enhancing downstream enzymatic accessibility. In some embodiments citric acid may be added to the slurry in the pre-masher unit as well, such that the slurry will have a preferred pH range of five point four to five point nine.

[0178] After the oats and water, or in some embodiments, oats, water and citric acid, are combined in pre-masher 45, the slurry may flow, via an aseptic closed line system, to thermally controlled mashing tank 48. In some alternative embodiments, the citric acid may be added to mashing tank 48, rather than to pre-masher 45, such that the slurry reaches the preferred pH range within mashing tank 48, rather than within pre-masher 45.

[0179] In some embodiments, mashing tank 48 may be integrating with an agitation mechanism, and be additionally equipped with pillow plates, for heating. It is preferable that the mixture be heated to a preferred temperature range of approximately eighty to ninety degrees Celsius, such that the oat starch granules become gelatinized. After which the mixture may preferably cool to and be maintained at a preferred approximate temperature range of seventy-seven to eighty to degrees Celsius for a first enzymic hydrolysis with a bacterial amylase, as described above. It is preferable that once the bacterial amylase is added, the mixture is held, within mashing tank 48 at a temperature ranging from seventyseven to eighty degrees Celsius for approximately seventy-five minutes, during which that mixture is stirred or otherwise agitated with the agitating mechanism.

[0180] Fig. 9 represents a multi-step or multi-stage process of oat and other ingredients for production. In some embodiments, as seen in Fig. 10. mashing tank 48 may include pillow plates 51, such that pillow plates 51 encourage micro-turbulent flow of the suspension. Pillow plates 51 may be specialized heat exchanger surfaces that are used in the heating jackets of mashing tank 48. In some embodiments, pillow plates may be two thin stainless-steel sheets welded in a preferably corrugated, or alternatively webbed, meshed, or other pattern, and then attached to one another to form a “pillow-shaped” structure. In some embodiments, the pillow plates may be set within mashing tank 48, such that one side of pillow plates 51 is set along the interior wall of mashing tank 48, and a second side of pillow plates 51 is exposed to the interior space 53 of mashing tank 48. In a preferred embodiment, pillow plates may function as a heating element to heat the mixture. In some embodiments, the mixture may circulate between the walls of pillow plates 51, such that heat transfers from the pillow plates 51 to the mixture.

[0181] In a preferred embodiment, pillow plates 51 may maintain temperature control during the oat beverage hydrolysis process. In a preferred embodiment, pillow plates 51 may optimize heat transfer and the mixture heating rate, promoting even heat absorption during mixing without overheating the outer layer of the mixture. Therefore, offering reduced spoilage and improved beverage quality.

[0182] As seen in Fig. 10 mashing tank 48 may additionally be set with vibration unit 52, such that vibration units may be optionally activated during hydrolysis to agitate the mixture, preferably at approximately five-minute intervals, as described above. In some embodiments, vibration unit 52 may provide vibrations within a defined frequency range to generate a resonance vibration in the suspension. Resonance vibrations may intensify the physiochemical degradation processes, as well as expel gas inclusions from solid particle.

[0183] In preferred embodiments, mashing tank 48 may be configurable, such that users may change the configuration depending on the required result: For example, pillow plate 51 temperature may be raised and lowered, vessel diameter may be adjusted, and vibration frequency may be altered.

[0184] After the approximately seventy -five-minute time period is complete, the mixture may cool to a temperature of preferably approximately fifty to fifty-five degrees Celsius. In some embodiments, the mixture may cool within mashing tank 48, in other embodiments, the mixture may flow, within a closed loop system, to enzymic tank 49. After the mixture cools to an approximate temperature of fifty to fifty -five degrees Celsius, the mixture may be treated with a fungal amylase, as described above. In embodiments wherein the mixture flows to enzymic tank 29, enzymic tank 49 may include pillow plates 51 and vibration unit 52 as described above.

[0185] As herein described, in a preferred embodiment, oat fiber and beta-glucans remain present in the final oat beverage, but in some alternative embodiments, the slurry may be decanted, such that insoluble fibers are removed from the final oat beverage. In such, alternative embodiments, as seen in Fig. 6, following the two enzymatic treatments, the mixture may flow in a closed loop system to decanter centrifuge 55 operating at preferably 3,000 to 5,000 G-forces. Devanter centrifuge 55 may separate the oat base (liquid extract) from insoluble oat fiber. The insoluble fraction can be collected and dried for by-products, while the oat base may flow out for further processing.

[0186] In preferred embodiments, after the two enzymic treatments, as described above, the oat base may flow, in a closed loop system to formulation tank 56, which may include a decanter centrifuge 55 as described above, wherein a protein additive may be added to the beverage. In flavored and adaptogenic embodiments, as described above, flavorings, vitamins (e.g., B12, D2), and adaptogens may be added as well. It is preferable that formulation tank 56 may be set with high-shear mixers, such that the protein source, and other added ingredients may be fully dispersion and emulsified into the beverage. After additives are fully mixed into the beverage, the beverage may flow to product treatment tank 57, such that the beverage may be heat treated and homogenized. It is preferable that product treatment tank 57 be set with a tubular heat exchanger, plate heat exchanger, or a direct steam injection unit, such that the beverage may undergo ultra-high- temperature (UHT) sterilization. In a preferred embodiment, the beverage may be heated to a temperature between one hundred thirty five and one hundred forty five degrees for a dwell time of two to five seconds to achieve commercial sterility.

[0187] After thermal treatment, the product is passed through a sterile homogenizer, also set within product treatment tank 57, under pressures of preferably between one hundred fifty and two hundred fifty bar. The homogenizer is preferably positioned downstream of the UHT unit within the sterile boundary to prevent recontamination. Homogenization may reduce fat globule size and ensures long-term stability of the emulsion.

[0188] As seen in Fig. 6, the sterilized and homogenized product may be stored in a sterile buffer tank 58. This tank allows continuous operation by decoupling the sterilization and filling units. From sterile buffer tank, the oat beverage may flow into pre-sterilized containers (e.g., PET bottles, cartons) using an aseptic filling machine.

[0189] As used herein, the term “approximately” should be understood as plus or minus ten percent of the goal quantity.

Claims

I CLAIM:

1. A hydrolysis method for producing an oat-based beverage the method comprising the steps of:(a) liquifying oat flour with water in a blender to create an oat slurry;(b) treating the oat slurry with a bacteria derived amylase enzyme for a first hydrolysis time to initially hydrolyze the oat flour and yield an initial hydrolyzed oat mixture;(c) treating the initial hydrolyzed oat mixture produced in step (b) with a fungal derived amylase enzyme for a second hydrolysis time to hydrolyze the oat flour to yield a final hydrolyzed oat slurry; and(d) adding a protein source into the final hydrolyzed oat slurry, until homogenously combined to yield an oat-based beverage composition.

2. The method of claim 1, wherein the oat flour is whole colloidal fine grain oat flour.

3. The method of claim 1, wherein the oat flour is organic.

4. The method of claim 1, wherein the oat flour is organic whole colloidal fine grain out flour.

5. The method of claim 1, further comprising adjusting the pH of the oat slurry to between five and six before the treating (b) with bacterial amylase.

6. The method of claim 1, further comprising adjuring the pH of the oat slurry with citric acid, whereby the pH is adjusted to a pH of between five point one and six.

7. The method of claim 1, whereby the first hydrolysis occurs at a temperature of between seventy-five and eighty-five degrees Celsius.

8. The method of claim 7, whereby the first hydrolysis time lasts for between seventy and eighty minutes.

9. The method of claim 7, whereby during the first hydrolysis, the mixture is stirred at intervals of approximately five to ten minutes.

10. The method of claim 1, whereby after the first hydrolysis is completed, the initially hydrolyzed mixture is cooled to a temperature approximately fifty to fifty -five degrees Celsius.

11. The method of claim 1, whereby after the initially hydrolyzed mixture is cooled to a temperature of approximately fifty to fifty -five degrees Celsius, a fungal derived amylase enzyme is added to the mixture, whereby a second enzymatic hydrolysis is performed.

12. The method of claim 11, whereby the second hydrolysis occurs for approximately thirty minutes at a temperature ranging between approximately fifty and fifty-five degrees Celsius.

13. The method of claim 1, wherein the protein source is sunflower protein powder.

14. The method of claim 1, whereby after the protein source is added to the final hydrolyzed oat slurry, the final hydrolyzed slurry is heated to a temperature of approximately between ninety and ninety-five degrees Celsius.

15. The method of claim 14, whereby after the final hydrolyzed oat slurry is heated to a temperature of approximately between ninety and ninety five degrees Celsius, the final hydrolyzed out slurry is cooled to a temperature of approximately between seventy and eighty degrees Celsius, after which the cooled final hydrolyzed oat slurry may be blended and subsequently refrigerated.

16. The method of claim 1, whereby said steps (a)-(d) are carried out as a continuous flow process.

17. The method of claim 1, wherein the oat-based beverage composition is fortified with adaptogens, the method further comprising adding at least one adaptogen to the oat slurry during the protein adding step (d).

18. The method of claim 17 wherein the at least one adaptogen is added after the protein source is added, and before the final hydrolyzed oat slurry is heated to a temperature of between ninety and ninety-five degrees Celsius.

19. The method of claim 1 or claim 17, wherein the oat-based beverage composition is flavored, said method comprising adding at least one flavoring agent to the oat slurry during the protein adding step (d).

20. The method of claim 1, wherein the enzymes used in said method are limited in their ability to break alpha 1,6 glycosidic bonds.

21. The method of claim 1, wherein the enzymes used in said method exclude fungal glucoamylase.

22. The method of claim 1 step b, wherein the bacterial amylase is a bacterial glucoamylase that hydrolyzes terminal (l,4)-alpha-D-glucoside linkages successively from non-reducing ends of the oat starch to release glucose molecules and does not effectively hydrolyze (l,6)-alpha-D-glucoside linkages.

23. The method of claim 22, wherein the liquified oats are partially hydrolyzed into glucose via a first hydrolysis with bacterial glucoamylase, wherein beta glucans are preserved in the final beverage.

24. The method of claim 22, wherein the fungal amylase is a fungal alpha-amylase that hydrolyzes (l,4)-alpha-D-glucoside linkages at specific points to produce maltose, maltotriose, and dextrin.

25. A method for producing an oat-based consumable product, the method comprising the steps of:(a) liquifying oat flour with water to create an oat slurry;(b) treating the oat slurry with a first enzyme for a first hydrolysis time to initially hydrolyze the oat flour and yield an initial hydrolyzed oat mixture;(c) further treating the initial hydrolyzed oat mixture produced in step (b) with a second enzyme for a second hydrolysis time to hydrolyze the oat flour or hydrolyzed mixture to yield a final hydrolyzed oat slurry; and(d) adding a protein source into the final hydrolyzed oat slurry, until homogenously combined to yield the oat-based consumable product.

26. A method for producing an oat-based consumable product, the method comprising the steps of:(a) liquifying oat flour with water to create an oat slurry;(b) sequentially enzymatically treating the oat slurry with a first enzyme for a first hydrolysis time to initially hydrolyze the oat flour, and subsequently enzymatically treating the initial hydrolyzed oat mixture with a second enzyme for a second hydrolysis time to yield a final hydrolyzed oat slurry; and(c) adding a protein source until combined to yield the oat-based consumable product.

27. An oat-based beverage produced from liquefied oat flour and water that is sequentially treated with enzymatic amylases, including alpha- and glucoamylases, and further comprising a protein.

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