Modified milk proteins and methods for their production

Abstract

The present disclosure includes a denatured whey protein composition comprising, on a dry weight basis, 60% or more by weight protein, less than 8% by weight unmodified glycomacropeptide (GMP), greater than 2% by weight enzymatically hydrolyzed GMP based on total weight of protein, a proteolytic index of 8% or more by weight, and greater than 50% by weight denatured whey protein based on total weight of protein.

Description

[Technical field]

[0001] The present technology relates to denatured whey protein compositions comprising denatured whey protein having low levels of native glycomacropeptide. [Background technology]

[0002] Milk-derived powder products, such as milk proteins, aldobion products, and galactooligosaccharides, are the primary source of ingredients in a wide variety of foods and beverages. For example, milk-derived proteins are the primary source of protein fortification in nutritional bars, sports drinks, and yogurt products. One source of milk protein is whey protein, which is produced as a by-product of cheese manufacturing. During cheese manufacturing, the casein proteins in milk become cheese curds, while liquid whey is drained from the curds and diverted for further processing. In most cheese manufacturing processes, the liquid whey is a mixture of whey proteins with significant amounts of lactose and minerals, and this mixture undergoes further purification to separate the whey proteins from the lactose and minerals.

[0003] Whey protein derived from cheese production also contains additional by-products such as cheese-making enzymes and protein hydrolysates produced by cheese-making enzymes. Unmodified glycomacropeptide (GMP) is considered a poor source of protein for muscle recovery because it has few branched-chain amino acids (especially leucine), which stimulate muscle protein synthesis and are the main building blocks in muscle tissue after periods of intense exercise and resistance training. Furthermore, high unmodified GMP content in whey protein compositions can result in undesirable flavors and poor process incorporation, reducing the total amount of protein that can be enriched into products. These and other challenges are addressed by the present technology. [Brief description of the drawings]

[0004] [Figure 1]1A-1D illustrate selected operations in a forming method according to some embodiments of the present technique. [Figure 2A] FIG. 2 shows particle size distribution of a non-denatured whey protein composition (WPC) having 80% protein on a dry basis. [Figure 2B] FIG. 2 shows the particle size distribution of a denatured whey protein composition according to an embodiment of the present disclosure. [Figure 2C] FIG. 2C is a diagram comparing the particle size distributions of FIG. 2A and FIG. 2B. [Figure 3A] FIG. 2 shows the capillary electrophoresis profile of a non-denatured whey protein composition (WPC) having 80% protein on a dry basis. [Figure 3B] FIG. 2 shows a capillary electrophoresis profile of a denatured whey protein composition according to an embodiment of the present disclosure. [Figure 4A] FIG. 2 shows particle size distribution of a non-denatured high fat whey protein composition. [Figure 4B] FIG. 2 shows the particle size distribution of a denatured high-fat whey protein composition according to an embodiment of the present disclosure. [Figure 4C] FIG. 4C is a diagram comparing the particle size distributions of FIG. 4A and FIG. 4B. [Diagram 5] FIG. 3 shows a sample according to Example 3. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS

[0005] In general, embodiments of the present disclosure include a denatured whey protein composition comprising, on a dry weight basis, 60% or more by weight of protein, less than 8% by weight of undenatured glycomacropeptide (GMP) and more than 2% by weight of enzymatically hydrolyzed GMP based on the total weight of the protein, a proteolytic index of 8% or more by weight, and more than 50% by weight of denatured whey protein based on the total weight of the protein.

[0006] In some embodiments, the denatured whey protein can comprise enzymatically hydrolyzed denatured cheese whey protein. In additional or alternative embodiments, the undenatured GMP is about 7% by weight or less based on the total weight of the protein. In further embodiments, the denatured whey protein is characterized by a D50 particle size distribution value of about 4.5 μm or less. In yet further embodiments, the denatured whey protein is further characterized by a D10 particle size distribution value of about 2.5 μm or less. In additional embodiments, the denatured whey protein is further characterized by a D90 particle size distribution value of about 8 μm or less. In further embodiments, the denatured whey protein composition can further comprise 7.0% by weight or less fat on a dry weight basis. In embodiments, the denatured whey protein composition can comprise 2% or more fat.

[0007] The embodiment of the present technology also includes a method for producing a denatured whey protein composition, comprising filtering cheese whey from enzymatically coagulated milk, producing a retentate and a permeate, combining the cheese whey retentate with one or more enzymes that selectively hydrolyze GMP in the cheese whey retentate to form a GMP-reduced cheese whey retentate composition, and heating the GMP-reduced cheese whey retentate composition to form the denatured whey protein composition. The denatured whey protein composition may be characterized by containing 60% or more whey protein by weight on a dry weight basis, less than 8% GMP and more than 2% enzymatically hydrolyzed GMP by weight based on the total weight of the protein, a proteolytic index of 8.0% or more by weight, and more than 50% denatured whey protein by weight based on the total weight of the protein.

[0008] The embodiment of the present technology also includes a method for producing a denatured whey protein composition, comprising filtering cheese whey from enzymatically coagulated milk, producing a retentate and a permeate, reducing native glycomacropeptides in the cheese whey retentate to form a GMP-reduced cheese whey retentate composition, and heating the GMP-reduced cheese whey retentate composition to form the denatured whey protein composition. The denatured whey protein composition may be characterized by containing 60% or more protein by weight on a dry weight basis, less than 11% GMP by weight based on the total weight of the protein, more than 2% enzymatically hydrolyzed GMP, a proteolytic index of 8.0% or more by weight, and more than 50% denatured whey protein by weight based on the total weight of the protein.

[0009] In additional embodiments, the one or more enzymes that selectively hydrolyze GMP in the cheese whey retentate comprise one or more alkaline serine protease enzymes and one or more neutral protease enzymes. In embodiments, the step of reducing GMP comprises combining the cheese whey retentate with one or more enzymes that selectively hydrolyze GMP in the cheese whey retentate. In other embodiments, the one or more enzymes that selectively hydrolyze GMP in the cheese whey retentate comprise one or more alkaline serine protease enzymes and one or more neutral protease enzymes. In further embodiments, the heating step further inactivates the one or more enzymes that selectively hydrolyze the GMP in the cheese whey retentate. In yet additional embodiments, the GMP-reduced cheese whey retentate composition is heated to a temperature of about 160°F or greater. In other embodiments, the heating step further comprises subjecting the GMP-reduced cheese whey retentate composition to high shear conditions. In yet further embodiments, the denatured whey protein composition is characterized by a weight ratio of unmodified GMP to total whey protein of about 0.15 or less. Additionally or alternatively, the denatured whey protein composition is characterized by about 11% GMP or less by weight based on the total weight of the protein. In some embodiments, the denatured whey protein composition is characterized by about 7% GMP or less by weight based on the total weight of the protein. In additional embodiments, the denatured whey protein composition is characterized by 7% fat or less by weight on a dry weight basis. In further embodiments, the denatured whey protein in the denatured whey protein composition is characterized by a D50 particle size distribution value of about 5 μm or less.

[0010] Embodiments of the present technology also include denatured whey protein compositions comprising 60% or more by weight of protein on a dry basis, less than 11% by weight of undenatured GMP based on the total weight of the protein, more than 7% by weight of fat on a dry basis, a β-lactoglobulin to α-lactalbumin ratio of greater than 5.00, and more than 50% by weight of denatured whey protein based on the total weight of the protein.

[0011] In some embodiments, the whey protein already comprises 30% or more denatured protein by weight prior to denaturation. In additional embodiments, the whey protein contains 60% or more β-lactoglobulin by weight based on the total weight of protein. Additionally or alternatively, in embodiments, the whey protein contains 12% or less α-lactalbumin by weight based on the total weight of protein. In other embodiments, the whey protein comprises a weight ratio of β-lactoglobulin to α-lactalbumin of about 7 or more. In further embodiments, the denatured whey protein is characterized by a D50 particle size distribution value of about 0.3 μm or less. In yet other embodiments, the denatured whey protein is further characterized by a D10 particle size distribution value of about 0.1 μm or less. In additional embodiments, the denatured whey protein is further characterized by a D90 particle size distribution value of about 1.0 μm or less.

[0012] An embodiment of the present technology includes a protein-enriched food product. An embodiment includes where the food product contains at least 3% by weight of total protein. In an embodiment, the protein comprises a denatured whey protein composition, the denatured whey protein composition containing less than 8% by weight of undenatured glycomacropeptide and more than 2% by weight of enzymatically hydrolyzed glycomacropeptide based on the total weight of the whey protein composition.

[0013] Embodiments of the present technology also include protein-enriched food products, said food products containing 3% or more by weight of total protein, said protein comprising a denatured whey protein composition containing less than 11% by weight of undenatured glycomacropeptide, more than 7% by weight of fat, and a β-lactoglobulin to α-lactalbumin ratio of greater than 5.00, based on the total weight of said whey protein composition.

[0014] A further understanding of the nature and advantages of selected embodiments of the present technology may be realized by reference to the remaining portions of the specification and drawings, in which like reference numerals may be used throughout the several drawings to refer to like components. In some instances, a sub-label is associated with a reference numeral and follows a hyphen to indicate one of multiple similar components. When referring to a reference numeral without specifying an existing sub-label, it is intended to refer to all of such multiple similar components.

[0015] Some of the figures are included as schematic diagrams. It should be understood that the figures are for illustrative purposes and should not be considered to scale unless specifically stated to be to scale. Additionally, as schematic diagrams, the figures are provided to aid in understanding and may not include all aspects or information as compared to realistic representations and may include exaggerated material for illustrative purposes.

[0016] In the figures, similar components and / or features may have the same reference numeral label. Furthermore, various components of the same type may be distinguished by following the reference label with a letter that distinguishes the similar components and / or features. If only a first numeric reference label is used herein, the description is applicable to any one of the similar components and / or features having the same first numeric reference label, regardless of a letter suffix.

[0017] Whey protein, as referred to herein, is actually a collection of various proteins, including primarily β-lactoglobulin (β-Lg) and α-lactalbumin (α-La), as well as glycomacropeptide (sometimes called GMP, cGMP or CMP), which is cleaved by chymosin activity from native κ-casein protein in milk to cause milk coagulation into cheese curd. Depending on the purification process and extent of purification, whey protein concentrates (WPCs) can be formed by concentrating whey proteins to 25-90% protein by weight as a percentage of the total weight of solids, or whey protein isolates (WPIs) can be formed by concentrating whey proteins to 90-99% protein by weight as a percentage of the total weight of solids.

[0018] Whey protein from cheese production also includes cheese-making enzymes and additional by-products such as protein hydrolysates that cheese-making enzymes produce. For example, enzymatically coagulated milk * A conventional composition of whey obtained from typically contains:

[0019] [Table 1]

[0020] * 1 Walstra P,Wouters JTM,Geurts TJ.Milk Components,Dairy Science and Technology.2nd ed.CRC Press;2006:Chapter 2. 2 Foegerding EA, Luck P, Vardhanabhuti B. Encyclopedia of Dairy Sciences.2 nd ed.Elsevier Ltd.;2011:Whey Protein Products. Protein hydrolysates contain glycomacropeptides (GMP) hydrolyzed from κ-casein, whereby the resulting para-κ-casein can form the main component of cheese curd. The smaller and more soluble GMP is carried away with the whey protein and can constitute 13-20% by weight of the protein present in the whey protein fraction on a dry weight basis. Unfortunately, GMP is considered an inferior source of protein for muscle recovery, as it contains less branched chain amino acids, which stimulate muscle protein synthesis and are the main building blocks in muscle tissue after periods of intense exercise and resistance training.

[0021] In addition, high native GMP content in whey protein composition may result in undesirable flavor and poor process incorporation. That is, high native GMP content (such as 12% by weight or more) of protein present in whey protein fraction on dry weight basis contributes to cardboard flavor, general off-flavor and / or artificial flavor increase, and natural milk flavor decrease in liquid whey, dry whey, milk protein concentrate and milk. In addition, native whey protein may also interact with water in food or beverage products, adversely increasing the viscosity of the food or beverage product. This interaction is problematic because it may limit the amount of whey protein composition that can be incorporated, reducing the total amount of protein that is enriched into the product.

[0022] The present technology overcomes these problems by providing denatured whey protein compositions (such as powdered or denatured whey protein compositions) that exhibit a high total weight percentage of protein but a reduced percentage of such protein attributable to native GMP. That is, the present technology has surprisingly found that it is possible to provide high protein denatured whey protein compositions with a low percentage of native GMP by carefully processing the whey protein composition to selectively reduce the GMP level without hydrolyzing the remaining proteins in the whey protein composition (e.g., β-lactoglobulin (β-Lg) and α-lactalbumin (α-La)). It has been observed that such denatured whey protein compositions do not exhibit the negative effects of compositions containing a high weight percentage of native GMP.

[0023] For example, compositions according to one or more embodiments of the present disclosure can exhibit lower process viscosity and reduced cardboard odor and stronger milky flavor. That is, the present disclosure has surprisingly found that when native GMP is enzymatically reduced in a whey protein composition, the process viscosity is reduced such that the viscosity is about 10% lower than the viscosity of a composition in which native GMP is not enzymatically reduced (e.g., about 20%, e.g., about 30%, e.g., about 40%, e.g., about 50% lower than the viscosity of a non-enzymatically reduced composition). For example, in a composition that is not enzymatically reduced as described herein, the process viscosity of the composition can be greater than 200 mPa·s (e.g., 201 mPa·s to 500 mPa·s). Conversely, compositions according to the present technology exhibit a process viscosity of less than 200 mPa·s (e.g., about 175 mPa·s or less, such as about 150 mPa·s or less, such as about 125 mPa·s or less, such as about 100 mPa·s or less, such as about 75 mPa·s or less, such as about 50 mPa·s or less, such as up to about 25 mPa·s, or any range or value therebetween). In some embodiments, compositions according to the present technology can also have a reduced ability to bind water. Thus, compositions according to the present technology can be uniquely suitable for fortifying water-containing foods to a higher level than previously thought possible in whey protein compositions, since the observed viscosity increase typically associated with these formulations is lower, at least in part, due to reduced interaction with water.

[0024] 1 shows example operations in a method 100 according to some embodiments of the present technology. The method may be performed in a variety of processing equipment known in the art. The method 100 may include some optional operations that are / are not specifically related to some embodiments of the method according to the present technology. For example, many of the operations are described to provide a broader scope of composition formation, but may be implemented by alternative methodologies that are not critical to the present technology or may be readily understood.

[0025] The whey composition raw material utilized herein may be obtained from a cheese making process, a whey protein concentrate, a whey protein isolate (such as from cow's milk), or a combination thereof. In some embodiments, the whey raw material may be produced from a cheese making process and may be referred to as "sweet whey" if the cheese making process uses a rennet enzyme such as chymosin, or may be referred to as "acid whey" if an acid is used to form the curd. The pH of sweet whey typically ranges from about 5.6 to 6.6, while the pH of acid whey typically ranges from 4.3 to 4.6. In some embodiments, the whey raw material utilized to form the denatured whey protein composition is considered to be "sweet whey" and thus filtered from lactose and minerals (102), although any suitable whey raw material may be utilized.

[0026] For example, in some embodiments, the whey protein material may be a whey protein retentate filtered (102) from sweet whey having a protein composition of 25% or more, such as about 50% or more, such as about 60% or more, such as about 70% or more, such as about 80% or more, or any range or value therebetween, on a dry weight basis. In embodiments, the whey protein retentate may be concentrated using ultrafiltration or other methods known in the art. Nevertheless, in some embodiments, the whey protein retentate may be diluted, for example, by mixing with water, prior to processing to form a whey protein material having a protein concentration in solution of about 30% or less, such as about 18% or less, such as about 16% or less, such as about 15% or less, such as about 14% or less, or any range or value therebetween.

[0027] In some embodiments, the native GMP level of the whey protein raw material may be reduced by utilizing one or more enzymes that selectively reduce the native GMP level without hydrolyzing β-lactoglobulin and / or α-lactalbumin (103). GMP may also be reduced by the use of expensive chromatography systems or by blending native whey protein isolates purified directly from milk that has not undergone cheese manufacture with whey protein concentrates from cheese manufacture. In embodiments, the one or more enzymes may be one or more protease enzymes. Sources of the one or more protease enzymes may include, among others, microbial, fungal, plant, and / or animal sources. For example, the one or more protease enzymes may be derived from fungi of the genus Aspergillus, bacteria of the genus Bacillus (e.g., Bacillus subtilis), and / or animals (e.g., trypsin, chymotrypsin, etc.), among other sources. Nevertheless, in some embodiments, the one or more protease enzymes include an acidic protease enzyme, a neutral protease enzyme, an alkaline protease enzyme, or a combination thereof. However, in some embodiments, the one or more protease enzymes include a neutral protease enzyme, an alkaline protease enzyme, or a combination thereof. Additionally or alternatively, the protease enzyme can be an endoprotease, an exoprotease, or a combination thereof. Thus, in some embodiments, the one or more protease enzymes can include an aspartic acid protease, a serine protease, a cysteine ​​protease, or a combination thereof. Nevertheless, in one embodiment, the one or more protease enzymes can include a serine protease, such as an alkaline serine protease, alone or in combination with one or more neutral protease enzymes.

[0028] Regardless of the enzyme(s) selected, the enzyme(s) selected may be added to the whey protein material in an amount of about 0.001% or more by weight based on the weight of the total protein in the composition, such as about 0.0025% or more by weight, such as about 0.005% or more by weight, such as about 0.0075% or more by weight, such as about 0.01% or more by weight, or any range or value therebetween, It is understood that the foregoing ranges may refer to the total amount of enzyme contained in the whey protein material or the amount of each enzyme added to the whey protein material.

[0029] However, in one aspect, the amount of one or more enzymes added is selected to hydrolyze at least about 10% by weight or more of the native GMP present in the whey protein material, such as about 15% by weight or more, such as about 20% by weight or more, such as about 25% by weight or more, such as about 30% by weight or more, such as about 35% by weight or more, such as about 40% by weight or more, such as about 45% by weight or more, such as about 50% by weight or more, such as about 60% by weight or more, such as about 65% by weight or more, such as about 70% by weight or more, such as about 72.5% by weight or more, such as about 75% by weight or more, such as about 80% by weight or more, such as about 85% by weight or more, or any range or value therebetween. In other words, in some embodiments, the denatured whey protein composition according to the present technology may have a reduced amount of native GMP compared to the whey protein material according to any one or more of the above percentages.

[0030] Regardless of the amount of one or more enzymes selected, the GMP selective enzyme is added to the whey protein raw material to hydrolyze the native GMP in the whey protein composition. In some embodiments, the hydrolysis step can last for about 72 hours or less, such as about 60 hours or less, such as about 48 hours or less, such as about 36 hours or less, such as about 24 hours or less, such as about 12 hours or less, such as about 10 hours or less, such as about 8 hours or less, such as about 5 hours or more, or any range or value therebetween. The hydrolysis can occur at a temperature of about 60°F or less, such as about 55°F or less, such as about 50°F or less, such as about 45°F or less, or any range or value therebetween.

[0031] Nevertheless, in some embodiments, the native GMP level of the whey protein raw material may be reduced by utilizing a high fat raw material (103). By using the whey protein retentate from the microfiltration process, in which a portion of the GMP permeates the microfiltration membrane, it is possible to provide the whey protein raw material at a desirably low native GMP level and a high denatured whey protein level. Thus, in some embodiments of the present technology, it is possible to utilize a high fat content raw material having a fat content of about 7% or more, such as about 8% or more, such as about 9% or more, such as about 10% or more, such as about 11% or more, such as about 12% or more, such as about 13% or more, such as about 14% or more, such as about 15% or more, such as about 16% or more, such as about 17% or more, such as about 18% or more, such as about 19% or more, such as about 20% or more, such as about 20.5% or more, or any range or value therebetween, based on the dry basis weight of the whey protein raw material.

[0032] In some embodiments, the above-described low native GMP levels and high fat levels in the high fat feedstock can be obtained or improved by utilizing a microfiltration membrane filtration process (such as a microfiltration membrane having a pore size of about 0.5 micrometers or less, e.g., about 0.4 micrometers or less, e.g., about 0.3 micrometers or less, or e.g., about 0.08 micrometers or more, or any range therebetween). That is, in some embodiments, a microfiltration membrane process can be selected to retain denatured whey proteins and fat while allowing some or all of the native proteins (including native GMP) to pass through to the permeate side. It is understood that in some embodiments, other filtration methods can be utilized to provide a high fat, low native GMP feedstock.

[0033] However, in embodiments utilizing microfiltration membranes, it has also been surprisingly found that it is possible to increase the ratio of β-lactoglobulin to α-lactalbumin. That is, without wishing to be bound by theory, β-lactoglobulin may be more prone to denaturation earlier than α-lactalbumin. Thus, β-lactoglobulin may be largely retained by the membrane with denatured whey protein, while α-lactalbumin passes through with the permeate at a higher rate. In some embodiments, the whey protein raw material composition according to the present technology exhibits a ratio of β-lactoglobulin to α-lactalbumin of about 2.75 or more, such as about 3 or more, such as about 3.5 or more, such as about 4 or more, such as about 4.5 or more, such as about 5 or more, such as about 5.5 or more, such as about 6 or more, such as about 6.5 or more, such as about 7 or more, such as about 7.5 or more, or any range or value therebetween.

[0034] For example, in some embodiments, the whey protein source composition may comprise about 65% by weight or more, such as about 67.5% by weight or more, such as about 70% by weight or more, such as about 72.5% by weight or more, such as about 75% by weight or more, or any range or value therebetween. Additionally or alternatively, in embodiments, the whey protein source composition may contain about 15% by weight or less, such as about 12.5% ​​by weight or less, such as about 10% by weight or less, such as about 7.5% by weight or less, or any range or value therebetween.

[0035] Regardless of the method utilized to reduce native GMP, the reduced native GMP material may be subjected to denaturation (104) as known in the art. For example, in some embodiments, the whey protein composition may be heated to a temperature of about 80° C. (about 176° F.) or higher, such as about 60° C. (about 140° F.) to about 148.9° C. (about 300° F.), such as about 71.11° C. (about 160° F.) to about 98.89° C. (about 170° F.) to about 93.33° C. (about 200° F.), or any range or value therebetween, whereby at least a portion of the starting whey protein is converted to denatured whey protein. Advantageously, such heating also denatures any enzymes, if utilized. Concurrent with heating, the slurry may be mixed or agitated to reduce the level of aggregation of the whey protein to be denatured. The slurry may be mixed and heated for a period of time from about 1 second to about 120 seconds, such as from about 2.5 seconds to about 105 seconds, such as from about 5 seconds to about 90 seconds, or any range or value therebetween.

[0036] During or after heating, the denatured whey protein composition can be subjected to mechanical shear conditions (105). In some embodiments, the mechanical shear conditions may further denature the whey proteins and / or inactivate one or more enzymes or reduce aggregates that may form as the whey proteins denature. Mechanical shear conditions as used herein generally refer to conditions having a shear strength of about 1,000 s -1A shear of more than 10,000 s is applied. -1 A shear of more than 50,000 s is applied. -1 More than 100,000 shear is applied, e.g. -1 More than 500,000 shear is applied. -1 In some embodiments, the denatured whey protein composition is typically sheared in a high shear mixer, colloid mill, or swept surface heat exchanger at a temperature of about 120° F. to about 300° F. for a period of about 0.1 seconds to 120 seconds.

[0037] However, it is understood that in some embodiments, at least a portion of the protein in the whey protein composition is denatured prior to heating. For example, in some embodiments, the whey protein material may have about 5% or more by weight, such as about 20% or more by weight, such as about 25% or more by weight, such as about 30% or more by weight, such as about 35% or more by weight, such as about 40% or more by weight, or any range or value therebetween, of denatured protein based on the total weight of protein in the whey protein material.

[0038] Nevertheless, after heating, or in the denatured whey protein composition of the present technology, the final protein contains about 45 wt.% or more, such as about 50 wt.% or more, such as about 55 wt.% or more, such as about 60 wt.% or more, such as about 65 wt.% or more, such as about 70 wt.% or more, such as about 75 wt.% or more, such as about 77.5 wt.% or more, such as about 80 wt.% or more, such as about 85 wt.% or more, such as about 90 wt.% or more, or any range or value therebetween, of denatured whey protein based on the total weight of protein in the whey protein composition.

[0039] As mentioned above, in some embodiments the denatured whey protein composition may be a high protein denatured whey protein composition and thus may contain about 50% or more by weight protein on a dry weight basis, such as about 55% or more by weight, such as about 60% or more by weight, such as about 65% or more by weight, such as about 70% or more by weight, such as about 75% or more by weight, such as about 80% or more by weight, or any range or value therebetween.

[0040] Regardless of the final protein composition, the denatured whey protein composition may be optionally cooled and concentrated after heating and shearing, and then dried (106) to produce a powdered denatured whey protein composition or a denatured whey protein composition. The drying process may include spray drying, heating, and evaporation, among other processes. As described in more detail below, the denatured whey protein composition may then be packaged or added directly to other ingredients to produce a food or beverage composition.

[0041] Regardless of the method utilized to reduce native GMP, the denatured whey protein compositions according to the present technology can contain less than 12 wt.% of native GMP, based on the total weight of protein in the denatured whey protein composition, such as about 11 wt.% or less, such as about 10 wt.% or less, such as about 9 wt.% or less, such as about 8 wt.% or less, such as about 7 wt.% or less, such as about 6.5 wt.% or less, such as about 6 wt.% or less, such as about 5.9 wt.% or less, such as about 5 wt.% or less, such as about 4 wt.% or less, such as about 3 wt.% or less, such as about 2 wt.% or less, such as about 1 wt.% or less, or any range or value therebetween.

[0042] Thus, in some embodiments, the denatured whey protein compositions may exhibit a weight ratio of undenatured GMP to denatured whey protein of about 0.15 or less, such as about 0.125 or less, such as about 0.1 or less, such as about 0.09 or less, such as about 0.085 or less, or any range or value therebetween.

[0043] In addition, as can be understood from the above, during hydrolysis of GMP in whey protein raw material, hydrolyzed GMP is formed and can advantageously remain in the denatured whey protein composition based on the desired end use. That is, the present technology has found that denatured GMP (GMP that has undergone one or more hydrolysis reactions, also referred to herein as enzymatically hydrolyzed GMP) does not exhibit the same adverse effects (such as cardboard odor / artificial flavor) as undenatured GMP. Thus, in some embodiments, the denatured whey protein composition can contain about 1 wt% or more, such as about 2 wt% or more, such as about 3 wt% or more, such as about 4 wt% or more, such as about 5 wt% or more, such as about 6 wt% or more, such as about 7 wt% or more, such as about 8 wt% or more, such as about 9 wt% or more, or any range or value therebetween, of denatured GMP based on the total weight of protein in the denatured whey protein composition.

[0044] Similarly, since unmodified GMP is acted upon by one or more enzymes, the denatured whey protein composition may have an increased proteolytic index in some embodiments. Proteolytic index is a measure of the increase in non-protein nitrogen (NPN) relative to the total Kjeldahl nitrogen (TKN) of the sample, and its determination method is described in the following examples. That is, proteolytic index (PI) can be an indicator of protein hydrolyzates, since it increases in a sample as proteins are broken down by enzyme activity into their primary amino acids or small peptides (known as non-protein nitrogen) that are soluble in trichloroacetic acid. Thus, in some embodiments, the denatured whey protein composition according to the present technology may have a proteolytic index of about 6 wt% or more, such as about 7 wt% or more, such as about 8 wt% or more, such as about 9 wt% or more, such as about 10 wt% or more, such as about 12.5 wt% or more, such as about 15 wt% or more, such as about 17.5 wt% or more, such as about 20 wt% or more, such as about 22.5 wt% or more, such as about 25 wt% or more, or any range or value therebetween.

[0045] Further, in some embodiments described above, the denatured whey protein composition may be considered to be "high fat" and may have a fat content of about 7% or more, such as about 8% or more, such as about 9% or more, such as about 10% or more, such as about 11% or more, such as about 12% or more, such as about 13% or more, such as about 14% or more, such as about 15% or more, such as about 16% or more, such as about 17% or more, such as about 18% or more, such as about 19% or more, such as about 20% or more, such as about 20.5% or more, or any range or value therebetween, based on the dry basis weight of the whey protein raw material. However, in some embodiments, the denatured whey protein composition contains less than 7% by weight fat, such as about 6.5% by weight or less, such as about 6% by weight or less, such as about 2% by weight or more, or any range or value therebetween.

[0046] Nevertheless, the particles of the denatured whey protein composition according to the present technology can have an average particle size of about 0.001 μm to about 11 μm, for example, about 0.005 μm to about 9 μm, for example, about 0.01 μm to about 7 μm, for example, about 0.015 μm to about 5 μm, or any range or value therebetween.

[0047] Surprisingly, the present technology has found that by forming low native GMP denatured whey protein composition as described herein, it is possible to obtain whey protein with narrow particle size distribution, and thus the flavor characteristics of the denatured whey protein composition of the present technology can be further improved.For example, the particles can have a D90 particle size distribution value (the particle size that 90% of the mass of sample contains particles of this size or less) of about 8 μm or less, for example about 7 μm or less, for example about 6 μm or less, for example about 5 μm or less, for example about 4 μm or less, for example about 3 μm or less, for example about 2 μm or less, for example about 1.75 μm or less, for example about 1.5 μm or less, for example about 1.25 μm or less, or any range or value therebetween.

[0048] Further, the particles may have a D50 particle size distribution value (the particle size at which 50% of the mass of a sample contains particles of this size or less) of about 5 μm or less, such as about 4.5 μm or less, for example about 4 μm or less, such as about 3.5 μm or less, for example about 3 μm or less, such as about 2.5 μm or less, for example about 2 μm or less, such as about 1.5 μm or less, for example about 1 μm or less, such as about 0.75 μm or less, for example about 0.5 μm or less, such as about 0.3 μm or less, or any range or value therebetween.

[0049] Additionally or alternatively, the particles may have a D10 particle size distribution value (the particle size at which 10% of the mass of a sample contains particles of this size or less) of about 3 μm or less, such as about 2.5 μm or less, for example about 2 μm or less, such as about 1.5 μm or less, for example about 1 μm or less, such as about 0.5 μm or less, for example about 0.4 μm or less, such as about 0.3 μm or less, for example about 0.2 μm or less, such as about 0.1 μm or less, for example about 0.05 μm or less, or any range or value therebetween.

[0050] As discussed above, the denatured whey protein compositions can be packaged in denatured form or can be incorporated into food or beverage products to produce fortified foods and / or beverages. Suitable food and beverage products can include protein bars, granola bars, yogurt, drinking yogurt, pudding products, ready-to-drink beverages, ready-to-mix beverage powders, bakery products, medical nutrition products, dietary supplement products, meat products, cheese, butter, grain products, cream cheese, dairy products, and the like.

[0051] As merely an example of a product and method for enriching a product using the denatured whey protein composition described herein, a yogurt composition can be formed as known in the art. For example, spoonable or drinkable yogurt milk (which may contain whole milk, skim milk, or a combination thereof enriched with the denatured whey protein composition according to the present technology) can be sent to a fermenter, where a yogurt culture is added to obtain a yogurt mix. The yogurt mix can then be combined with additional ingredients or flavors and packaged.

[0052] The fortified food and / or beverage products described herein may have a viscosity of about 500 mPa·s (500 centipoise (cP)) or less, such as about 400 mPa·s or less, such as about 300 mPa·s or less, such as about 250 mPa·s or less, such as about 200 mPa·s or less, such as about 150 mPa·s or less, such as about 100 mPa·s or less, such as about 50 mPa·s or less, or any range or value therebetween, which methods may be described in more detail in the examples.

[0053] Further, the fortified food and / or beverage products described herein may be fortified to a protein level of greater than 3%, or about 8% or more, such as about 8.5% or more, such as about 9% or more, such as about 9.5% or more, for example about 10% or more, such as about 12.5% ​​or more, for example about 15% or more, such as about 17.5% or more, for example about 20% or more, such as about 22.5% or more, for example about 25% or more, such as about 27.5% or more, for example about 30% or more, or any range or value therebetween, based on the weight of the food and / or beverage product.

[0054] Moreover, certain embodiments of the present disclosure may be better understood by reference to the following examples, which are intended to be non-limiting and exemplary in nature. example Test methods and procedures Quantitative determination of glycomacropeptide (GMP), α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) Quantitation of GMP was determined by a Beckman capillary electrophoresis system. The capillary was DOV-1701OH Deactivated TSP standard FS tubing (600 mm x 50 μm) with a 100 x 800 μm slit opening and regenerated / activated with 0.1 N HCl solution.

[0055] Preparation of sample solutions: -Prepare a 1% protein solution of each sample using deionized (DI) water. -Vortex the sample until homogenous.

[0056] - Allow powder samples to hydrate for at least 30 minutes before continuing with sample preparation. Prepare sample buffer using 0.0787 g of DTT (threo-1,4-dimercapto-2,3-butanediol) and 30 g of reducing buffer, which consists of 167 mM Tris, 42 mM 3-morpholino-propanesulfonic acid, 67 mM disodium ethylenedinitrilotetraacetate, 0.5 g / L methylhydroxypropylcellulose in 8 M urea solution.

[0057] -After hydrating the sample, mix sample buffer with sample in a 1:1 ratio to make a total of 4 mL. -Vortex the samples and let sit for 1 hour.

[0058] - Filter the sample into a glass vial using a PVDF 0.22 μm syringe filter. Place a cap on the glass vial. Inject the sample solution at 3.4 Kpa for 10 seconds. Separation is performed at 45° C. and 25 KV (initially increasing from 0 to 25 KV within 3 minutes). Detection of milk proteins is performed at 214 nm. The amount of each protein component is determined by comparing the peak area of ​​each component peak with the total peak area. In this example, it is determined as follows: GMP% = ((GMP peak area) / (sum of all protein peak areas)) x 100% (β_Lg) / (α_La)=(β_Lg peak area) / (α_La peak area) Fat quantification The fat content is determined by the Mojonnier modification of the Roese-Gottlieb method for fat extraction (reference method AOAC 989.05), which uses ether to extract fat from dairy products.

[0059] Calculation: Fat % = ((fat weight - blank) / (sample weight)) x 100% Where: - Fat weight: (weight of sample beaker after extraction) - (weight of empty beaker).

[0060] - Blank: The analytical blank measurement must be subtracted from the fat weight obtained. - Sample weight: sample weight before the extraction procedure.

[0061] Quantitative Total Kjeldahl Nitrogen (TKN) Protein Analysis Protein analysis by Kjeldahl nitrogen (reference method AOAC 991.20) is used to determine the weight percentage of nitrogen compounds. Sulfuric acid breaks down proteins and other nitrogen compounds, converting the nitrogen to ammonium sulfate. A catalyst is used to increase the reaction rate and to raise the boiling point of the sulfuric acid. Titration of ammonia with standard hydrochloric acid gives the amount of nitrogen associated with protein and soluble nitrogen.

[0062] Determination of TKN (total crude protein) TKN%=(ΔmL×N×14.007×6.38) / (10×W) Where: -ΔmL = amount of standardized HCl added to sample - amount added to blank (in mL) (often calculated by the distillation apparatus and given as ΔmL).

[0063] -N = exact normality of standardized HCl from the Certificate of Analysis in meq / mL. -14.007 = formula amount of nitrogen (mg / meq). -The constant 6.38 is the grams of milk protein per gram of nitrogen. The other constants are 4.7218 for ammonium sulfate and 7.2904 for l-tryptophan.

[0064] -W = sample size (grams). Divide by -10 to get the result as g per 100 grams. - Results are expressed as percentage by weight of protein (grams per 100 grams of sample).

[0065] Determination of NPN (non-protein nitrogen) Non-protein nitrogen (NPN) consists of urea, ammonia, free amino acids, creatine, uric acid, peptides, and amino alcohols of phospholipids that are soluble in trichloroacetic acid (Ruska and Jonkus, 2014). In general, although not a definitive rule, more than 30 amino acids are sufficient to consider a polypeptide as a protein, and peptides consisting of less than 30 amino acids are likely to be found in the TCA-soluble fraction and classified as non-protein nitrogen. This method uses the addition of trichloroacetic acid (TCA) to precipitate proteins. The proteins are filtered off and the non-protein nitrogen in the filtrate is measured. It is then possible to determine the amount of non-protein nitrogen.

[0066] Sample preparation A. Mix the sample thoroughly. B. Tare a 150 mL beaker or approximately 118 mL (4 oz) snap cap. For powdered or solid samples, add 10 to 15 glass balls to the beaker or snap cap before taring.

[0067] C. Transfer the appropriate number of samples to a tared beaker based on the table below. Record the sample weight to the nearest 0.0001 g. For powdered or solid samples, add 20 mL of DI water and shake to constitute the sample.

[0068] D. Using a graduated cylinder or automated dispenser, add 15 mL of 33% TCA to the sample. E. Place the beaker or snap cap back on the balance.

[0069] F. Add DI water to the sample until the combined mass of sample, TCA solution, and added water is approximately 50 g. Record the total weight. G. Mix well and allow the solution to stand for 10 minutes.

[0070] H. Filter through slow filter paper into a clean snap cap or beaker. I. Transfer approximately 7-10 g of filtrate to a Kjeldahl digestion tube. Record the exact mass of filtrate added.

[0071] Test in the J. TKN (Total Kjeldahl Nitrogen) method to determine nitrogen (N) in the filtrate for the following calculations. NPN%=(mL×N×14.007×6.38) / (W×A / B / 10) • mL = amount of standardized HCl needed to titrate the sample distillate.

[0072] • N = exact normality (meq / mL) of standardized HCl from the lot Certificate of Analysis (COA) or as determined in the laboratory. ● 14.007 = formula weight of nitrogen (mg / meq).

[0073] • 6.38 is the factor for converting nitrogen to milk protein. ● W = grams of sample filtrate used. ● A = number of grams of sample used.

[0074] ● B=total grams of sample solution. ● 10 to convert the result to grams per 100 grams. True Protein Determination Net protein is a measure of total nitrogen (TKN) (sometimes called crude protein) minus the non-protein nitrogen (NPN) content: Net protein = TKN - NPN, expressed as a percentage by weight of net protein (grams of net protein per 100 grams of sample).

[0075] Determination of proteolytic index (PI) The proteolytic index is a measure of the increase in non-protein nitrogen (NPN) relative to the total Kjeldahl nitrogen (TKN) of a sample. The proteolytic index (PI) increases in a sample as proteins are broken down by enzymatic activity into their primary amino acids or small peptides (known as non-protein nitrogen) that are soluble in trichloroacetic acid.

[0076] PI = ((NPN%) / (TKN%)) x 100% The proteolytic index is expressed as the weight percentage of NPN to total crude protein (TKN) (grams of NPN per 100 grams of total crude protein).

[0077] Denatured whey protein measurement The denatured whey protein (DWP) method is a measure of whey protein that has undergone disruption and possible destruction of both secondary and tertiary structure, rendering the protein insoluble in an environment in which the undenatured protein would typically be soluble.

[0078] Sample preparation - Prepare a sample solution at approximately 1.2% (w / w) protein. Adjust the pH to 6.8 using either 0.1N HCl or 0.1N NaOH.

[0079] -Record the sample weight and the final solution weight after pH adjustment. -The volume is divided into two fractions for testing. -10mL for total TKN. Do a test for TKN. This can be % total TKN.

[0080] -25 g of the DWP fraction is placed in a beaker and treated as follows. Determination of denatured whey protein (pH 4.6) fraction -Add ∼10 mL of distilled water to the beaker containing the DWP fraction.

[0081] - Place a small magnetic stir bar into the beaker. Place the beaker on a stir plate and insert the pH probe and temperature compensator into the solution. Start the stirrer. -Adjust the pH to 4.60±0.02 by adding 1 Normal HCl for coarse adjustment and 0.1 Normal HCl for fine adjustment.

[0082] -Place the beaker on the balance. Bring the solution to a weight of ~50g (e.g., tare weight + 50g) using distilled water. Record the weight to the nearest 0.0001g. -Allow the solution to stand at room temperature for 1 hour. Swirl the contents of the beaker for 10-15 seconds to mix. Transfer the contents to a centrifuge tube.

[0083] -Place the tube in the centrifuge, making sure the tube is balanced. Centrifuge for 15 minutes at 10,000 rpm at 10°C. Do not use the brake to speed up deceleration. -Without transferring any of the pellet material, transfer ~10mL of the supernatant to a certified culture tube. This is the Undenatured Whey Protein Fraction. Use this supernatant to test for TKN. This is the "%TKN in Undenatured Whey Protein Fraction."

[0084] Denatured whey protein (DWP) is calculated as follows: DWP=1-((TKN% in undenatured whey protein fraction × (final weight of diluent / weight of diluted solution)) / TKN%) Determination of particle size distribution Particle size distribution analysis was determined using a Malvern Mastersizer 3000 equipped with a Hydro EV. The method parameters were particle refractive index 1.46, particle absorptivity 0.0001 and dispersant refractive index 1.33, with water as dispersant. The Mie scattering model was used for the analysis.

[0085] Example 1 A whey protein composition (WPC) that is greater than 25% protein on a dry weight basis from sweet whey in Mozzarella cheese production was used to produce a glycomacropeptide (GMP) reduced denatured whey protein composition. The process begins with a WPC retentate (80% protein on a dry weight basis) concentrated using ultrafiltration (UF) of pasteurized sweet whey separated from cheese curd. The 80% WPC (WPC80) retentate is transferred to a temperature-controlled holding tank and kept chilled at about 45°F or less, where it is mixed with water to produce a 14% protein solution. The holding tank contains a 5,000 lb batch of whey protein mixture, where about 700 lbs of protein from the 80% WPC retentate is mixed with water to form a diluted whey protein solution. The diluted whey protein solution remains in a holding tank at about 45°F or below until the addition of the protease enzyme.

[0086] The addition of one or more enzymes (in this case one or more protease enzymes) initiates a proteolytic incubation stage that selectively hydrolyzes GMP in the whey protein mixture while leaving other whey proteins (such as α-lactalbumin and β-lactoglobulin) largely unhydrolyzed. In this experiment, the protease enzymes included one or more alkaline serine protease enzymes and one or more neutral protease enzymes. In this example, the one or more protease enzymes were added to the whey protein mixture at a level of about 0.001% to about 5% by weight of the total protein in the substrate, or up to about 0.012% by weight. For a 5,000 pound batch, about 38 g of enzyme was added.

[0087] The hydrolysis step continued for at least 5 hours with stirring at or below about 45°F, but can continue for up to 72 hours or more without hydrolyzing the major whey proteins (i.e., α-lactalbumin and β-lactoglobulin). The enzyme-treated whey protein mixture was then subjected to heating to about 190°F for 6 seconds (operating range of about 80°C-about 176-195°F and 5-90 seconds) and simultaneous mechanical shear to achieve enzyme inactivation and whey protein denaturation. Following heating and mechanical shear, the resulting denatured whey protein mixture was subjected to optional cooling (e.g., to about 50°F) and concentration (e.g., by evaporation or nanofiltration), followed by spray drying to produce a powdered GMP-reduced denatured whey protein composition.

[0088] As shown in Figures 2A-2C, the particle size distribution of the particulate denatured whey protein composition exhibited a narrower range than the whey protein raw material, being about 1.7 micrometers (mm) or less (characterized by D90).

[0089] Figure 2A shows the unmodified (feed) particle size with a particle size range of 0.011-9.86 micrometers. After enzymatic hydrolysis of GMP and subsequent enzyme inactivation and whey protein denaturation, the particle size is reduced to a range of 0.017-4.03 micrometers, as shown in Figure 2B. Figure 2C provides a comparative overlay of the particle size distribution for both the whey protein raw material and Sample 1.

[0090] The level of native GMP by weight of total protein in the whey protein composition raw material and the particulate denatured whey protein composition was determined by capillary electrophoresis (CE) and is defined as the native GMP peak area on the CE graph divided by the total protein peak area, as shown in Figures 3A and 3B.

[0091] As mentioned above, denatured whey protein (DWP) and the proteolytic index (PI), defined as the division of non-protein nitrogen by total nitrogen, are determined by wet chemical analysis. Table 1 showed the reduction of native GMP from a typical cheese whey level of 12-25% (20.52% in this case) to less than 8% (specifically 5.84%). Similarly, as GMP hydrolysis occurs, there is a concomitant increase in the proteolytic index as the native GMP protein breaks down into smaller fragments and the amount of non-protein nitrogen increases. Figures 3A and 3B show that GMP is substantially reduced during hydrolysis, while α-lactalbumin (a-La) and β-lactoglobulin (b-Lg) remain largely unhydrolyzed, a result of the controlled hydrolysis, which is further indicated by the minimal reduction (less than 10%) in the β-lactoglobulin to α-lactalbumin ratio (Table 1). The increase in denatured whey protein is a direct result of the time and temperature treatment during the enzyme inactivation procedure.

[0092] Table 1:

[0093] [Table 2]

[0094] *-Denatured Whey Protein % ^-% Fat on dry basis 1- Proteolytic index 2-% Protein on Dry Basis Example 2 The high fat whey protein composition (hfWPC) raw material feedstock was obtained from a microfiltration membrane filtration process. The composition of the feedstock taken from the retentate side of the microfiltration process was 75.48% protein on a dry basis and 17.66% fat on a dry basis. The high fat whey protein composition feed was adjusted to 14% protein (operating range 10-24%) by adding water.

[0095] Denaturation of the protein was achieved by preheating the feed to 130°F (operating range 120-150°F), then heating to the denaturation temperature of 176-195°F, holding for 5-90 seconds, and simultaneously mechanically shearing during heating for particle size control. Following the heating and shearing process, the denatured whey protein composition was cooled to a temperature below 50°F and dried to a powder by spray drying to form Sample 2.

[0096] The denatured high fat whey protein compositions were analyzed for total solids, fat, protein, denatured whey protein, and particle size distribution, and the results (i.e., results for the undenatured high fat whey protein compositions before (feed) and after the denaturation-shear process) are shown in Table 2 and Figures 4A-4C. Figure 4A showed that the high fat WPC ingredients had a particle size range of 0.011-11.2 micrometers. After the denaturation and shear process, the particle size was reduced to a range of 0.011-2.75 micrometers, as shown in Figure 4B. Figure 4C provides a comparative overlay of particle size distribution for both the feed high fat WPC ingredients and the denatured high fat WPC.

[0097] As mentioned above, the present technology has found that the high fat WPC formed herein exhibits different chemical properties compared to WPC 80, as shown in Table 1. The starting material of the high fat WPC has lower GMP (10.5 vs. 20.5%), higher denatured whey protein (DWP) (45.10 vs. 17.27%), higher fat on dry basis (17.66 vs. 6.35), and higher β-lactoglobulin to α-lactalbumin ratio (7.65 vs. 3.37) compared to the starting feed WPC 80. The production of high fat WPC uses ultrafiltration and microfiltration, while the production of WPC 80 uses only ultrafiltration. One explanation could be that due to the pore size of the microfiltration membrane, most of the DWP and fat are captured in the retentate, while some of the GMP, α-lactalbumin, β-lactoglobulin and other whey proteins pass through to the permeate side. Since β-lactoglobulin is more susceptible to denaturation during milk pasteurization and subsequent sweet whey pasteurization compared to α-lactalbumin, the retained proteins are likely to contain more denatured β-lactoglobulin than α-lactalbumin. Thus, the ratio of β-lactoglobulin to α-lactalbumin in high fat WPC is higher than that in WPC80. Interestingly, despite the different DWP values ​​in the starting feedstocks, the final denatured high fat WPC (hfWPC) and denatured WPC80 achieved similar particle size distributions and denatured whey protein (DWP) values ​​(compare Figure 2C vs. Figure 4C and Table 1 vs. Table 2).

[0098] Table 2:

[0099] [Table 3]

[0100] Example 3 Denatured whey protein compositions have been utilized to enhance drinking yogurt applications to observe functional benefits in viscosity management of high protein products.

[0101] Samples according to Example 3 were made using the following yogurt making process. 1. Mix the powdered and liquid ingredients of the base recipe (Table 3) to obtain a homogenous solution. 2. Pasteurize at 80-85°C (176-185°F) for 30 minutes.

[0102] 3. Cool to 42°C (108°F). 4. Inoculate with starter culture (CHR Mild 2.0) at 0.02%.

[0103] 5. Maintain temperature at 42°C (108°F) during the fermentation process. 6. The fermentation process is stopped when the pH reaches 4.6. 7. Store at 4°C (39°F).

[0104] Table 3

[0105] [Table 4]

[0106] The samples and controls were then analyzed for protein, percent total solids, and viscosity, and the results are shown in Table 4. Table 4

[0107] [Table 5]

[0108] *Brookfield Viscometer, spindle #6 @ 100 rpm, temperature approximately 5.56°C (42°F). Various levels of protein enrichment can be interesting for consumers. Examples of protein enrichment in drinking yogurt are shown in Table 3 and Table 4 and Figure 5. As shown, drinking yogurt enriched to 10% protein with GMP-reduced modified WPC80 composition and GMP-reduced modified hfWPC according to the present technology has a favorable lower viscosity when compared with a commercial product with a protein level of 7.54%. Thus, the present technology shows a significant reduction in viscosity even at higher enrichment levels. The reduced viscosity is beneficial to the consumer experience due to the increased protein per serving and the ease of consumption of the product.

[0109] As shown, increasing protein in yogurt applications is difficult. Yogurt viscosity generally increases as protein is increased. This is because proteins commonly used to fortify foods (such as casein protein and undenatured whey protein) bind and interact with water resulting in a more viscous texture. The advantage of using the denatured whey composition according to the present technology in products such as yogurt is to fortify the protein content and maintain acceptable viscosity. This is shown in Table 4, which compares the viscosity data of yogurt fortified with control (no WPC), standard GMP undenatured WPC80, and GMP reduced denatured WPC80, demonstrating the practical solution that the GMP reduced denatured whey protein composition brings to viscosity. As shown, the control yogurt (no WPC) is very viscous, having a viscosity greater than 25000 mPa·s, and therefore is not pourable and is not acceptable as a drinkable yogurt product. Similarly, drinking yoghurt fortified with standard GMP unmodified WPC80 had a viscosity of 4040 mPa·s, which is still too viscous to be acceptable for a drinking yoghurt product. On the other hand, yoghurt fortified with GMP reduced modified WPC80 according to the present technology showed a viscosity of 90 mPa·s, which is acceptable for pourability and as a drinking yoghurt product. In addition, the GMP reduced modified WPC80 performed very favourably compared to the commercial reference (viscosity of 580 mPa·s).

[0110] Table 4 shows viscosity data for a control (no WPC), GMP-reduced non-denatured hfWPC, and GMP-reduced modified hfWPC in one example demonstrating the practical solution that the GMP-reduced denatured whey protein composition provides for a product with a desired low viscosity. As the data shows, the control yogurt (no WPC) was very viscous, having a viscosity greater than 25,000 mPa·s, and therefore was not pourable and was not acceptable for a drinking yogurt product. Similarly, the drinking yogurt fortified with GMP-reduced non-denatured hfWPC exhibited a lower viscosity of 860 mPa·s, which is still too viscous and unacceptable for a drinking yogurt product. On the other hand, the yogurt fortified with GMP-reduced modified hfWPC according to the present technology exhibited a viscosity of 80 mPa·s, which is acceptable for pourability and as a drinking yogurt product.

[0111] Example 4 Modified whey protein compositions were utilized to enhance spoonable yogurt applications to observe functional benefits in managing the viscosity of the high protein product.

[0112] Table 5:

[0113] [Table 6]

[0114] The samples and controls were then analyzed for protein, percent total solids, and viscosity, and the results are shown in Table 6. Table 6

[0115] [Table 7]

[0116] Tables 5 and 6 show examples of protein-enriched spoonable yogurt. The data show that the GMP-reduced denatured whey protein composition according to the present disclosure exhibits higher impact in increasing the protein content of spoonable yogurt without a corresponding increase in viscosity or change in acceptable texture. A commercially available reference spoonable yogurt with 10% protein had a viscosity of 11,000 mPa·s. When the protein was increased to 14.7% using GMP-reduced non-denatured hfWPC, the viscosity was 63,000 mPa·s, which was too high for a spoonable yogurt product. However, when the protein was increased to 14.7% using GMP-reduced denatured hfWPC or GMP-reduced denatured WPC80 according to the present technology, the viscosity was 9,000-12,000 mPa·s, which was comparable to the commercially available reference yogurt at 10% protein. This demonstrates the advantage of using the GMP-reduced denatured whey protein composition according to the present technology to achieve an increase in the protein content of spoonable yogurt while maintaining viscosity. Such improvements also improve the consumer experience due to a more familiar viscosity and texture.

[0117] Example 5 Samples of undenatured whey protein concentrate at 80% protein on a dry basis, GMP reduced denatured WPC 80, undenatured high fat WPC, and denatured WPC were each prepared for descriptive flavor analysis. Whey protein was rehydrated at 10% (w / v). Products were dispensed into lidded soufflé cups with a three-digit code and evaluated. Beverages were evaluated in duplicate by seven trained panelists using an established sensory language for whey protein. Descriptive analysis of flavor utilizes a 0-15 point universal intensity scale using the Spectrum™ method (Meilgaard et al. 1999; Drake and Civille 2003). Paper ballots were used. Each panelist evaluated each product in duplicate in different sessions. Data were analyzed by general linear model analysis of variance with Fisher's least significant difference (LSD) as a post-hoc test (SAS version 9.1, Cary, NC).

[0118] Table 7 summarizes the trained panelist analysis of the samples. An unexpected observation is that reducing GMP and denaturing whey proteins according to the present technology shows a significant reduction in the cardboard flavor often considered an off-flavor and present in many dairy proteins. In addition, the reduction of GMP resulted in an improvement in dairy flavor, which is considered a beneficial flavor attribute in products suitable for dairy applications.

[0119] The GMP-reduced denatured WPC results are further substantiated by similar flavor observations when denatured high fat whey protein compositions originally lower in GMP were evaluated: again, lower GMP was observed to result in a trend towards less carboard notes and a significant increase in dairy flavor, coupled with protein denaturation.

[0120] Table 7

[0121] [Table 8]

[0122] Aroma and flavour intensity was scored on a universal intensity scale (Spectrum method, Meilgaard et al., 1999) from 0 to 15 points. ND - not detectable. Means in columns followed by different letters are different (p less than 0.05). Characteristics not listed were not detected in these samples.

Claims

1. 1. A denatured whey protein composition comprising: 60% or more by weight of whey protein on a dry weight basis; less than 8% by weight of native glycomacropeptide (GMP) and more than 2% by weight of enzymatically hydrolyzed GMP based on the total weight of protein in the denatured whey protein composition; A proteolytic index of 8.0% by weight or more; and greater than 50% by weight of denatured whey protein based on the total weight of protein in said denatured whey protein composition.

2. 2. The denatured whey protein composition of claim 1, wherein the denatured whey protein comprises enzymatically hydrolyzed denatured cheese whey protein.

3. 3. The denatured whey protein composition of claim 2, wherein said undenatured GMP is about 7% or less by weight based on the total weight of protein in said denatured whey protein composition.

4. 2. The denatured whey protein composition of claim 1, wherein the denatured whey protein is characterized by a D50 particle size distribution value of about 4.5 μm or less.

5. 5. The denatured whey protein composition of claim 4, wherein the denatured whey protein is further characterized by a D10 particle size distribution value of about 2.5 μm or less.

6. 5. The denatured whey protein composition of claim 4, wherein the denatured whey protein is further characterized by a D90 particle size distribution value of about 8.0 μm or less.

7. 10. The denatured whey protein composition of claim 1, further comprising up to 7.0% fat by weight on a dry weight basis.

8. 1. A method for producing a denatured whey protein composition, comprising: filtering the cheese whey from the enzymatically coagulated milk into a cheese whey retentate and a permeate; reducing native glycomacropeptide (GMP) in the cheese whey retentate to form a GMP-reduced cheese whey retentate composition; and heating the GMP reduced cheese whey retentate composition to form the denatured whey protein composition; The denatured whey protein composition comprises: 60% or more by weight of whey protein on a dry weight basis; less than 11% by weight of undenatured GMP based on the total weight of protein in the denatured whey protein composition; a proteolytic index of 8.0% by weight or more or a β-lactoglobulin to α-lactalbumin ratio of greater than 5.00; greater than 50% by weight of denatured whey protein based on the total weight of protein in said denatured whey protein composition.

9. 9. The method of claim 8, wherein the reducing step comprises combining the cheese whey retentate with one or more enzymes that selectively hydrolyze GMP in the cheese whey retentate to form the GMP reduced cheese whey retentate composition, wherein the one or more enzymes that selectively hydrolyze GMP in the cheese whey retentate comprise one or more alkaline serine protease enzymes and one or more neutral protease enzymes, or the reducing step occurs by microfiltration of the cheese whey retentate.

10. 9. The method of claim 8, wherein the heating step further inactivates the one or more enzymes that selectively hydrolyze the GMP in the cheese whey retentate.

11. 10. The method of claim 8, wherein the GMP reduced cheese whey retentate composition is heated to a temperature of about 160°F or greater.

12. 9. The method of claim 8, wherein the heating step further comprises subjecting the GMP reduced cheese whey retentate composition to high shear conditions.

13. 9. The method of claim 8, wherein the denatured whey protein composition is characterized by a weight ratio of undenatured GMP to total whey protein of about 0.15 or less, the denatured whey protein composition is characterized by about 11% by weight or less GMP relative to the total weight of protein in the denatured whey protein composition, or both.

14. 1. A denatured whey protein composition comprising: 60% or more by weight of protein on a dry weight basis; less than 11% by weight of native glycomacropeptide (GMP) based on the total weight of said protein; More than 7% fat by weight on a dry basis; a β-lactoglobulin to α-lactalbumin ratio of greater than 5.00; and greater than 50% by weight of denatured whey protein based on said total weight of said protein.

15. 9. The method of claim 8, wherein the GMP reduced cheese whey retentate already contains 30% or more by weight denatured protein prior to the heating step.

16. 15. A denatured whey protein composition according to claim 14, which contains 60% or more by weight of beta-lactoglobulin relative to the total weight of protein, or 12% or less by weight of alpha-lactalbumin relative to the total weight of protein, or both.

17. 15. The denatured whey protein composition of claim 14 comprising a weight ratio of beta-lactoglobulin to alpha-lactalbumin of about 5 or greater.

18. 15. The denatured whey protein composition of claim 14, wherein the denatured whey protein is characterized by a D50 particle size distribution value of about 0.3 μm or less.

19. 15. The denatured whey protein composition of claim 14, wherein the denatured whey protein is further characterized by a D10 particle size distribution value of about 0.1 μm or less.

20. 15. The denatured whey protein composition of claim 14, wherein the denatured whey protein is further characterized by a D90 particle size distribution value of about 1.0 μm or less.

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