Denatured milk protein and process for producing the same

Abstract

To provide a denatured whey protein composition containing denatured whey protein having a low native glycomacropeptide level.SOLUTION: The denatured whey protein composition comprises, on a dry weight basis, greater than or equal to 60% by weight whey protein, less than 8% by weight undenatured glycomacropeptide (GMP) and greater than 2% by weight enzymatically hydrolyzed GMP relative to the total weight of protein in the denatured whey protein composition, a proteolytic index of greater than or equal to 8.0% by weight, and greater than 50% by weight denatured whey protein relative to the total weight of protein in the denatured whey protein composition.SELECTED DRAWING: None

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 major sources of ingredients in a wide variety of foods and beverages. For example, milk-derived proteins are a major 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 production. During cheese production, casein proteins in milk are converted into cheese curds, while liquid whey is drained from the curds and diverted for further processing. In most cheese-making processes, 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. Native glycomacropeptide (GMP) is considered a poor source of protein for muscle recovery after periods of intense exercise and resistance training because it contains little branched-chain amino acids (especially leucine), which stimulate muscle protein synthesis and are the primary building blocks in muscle tissue. Furthermore, high native GMP content in whey protein compositions can result in undesirable flavors and poor process incorporation, reducing the total amount of protein available for enrichment in products. These and other challenges are addressed by the present technology. [Brief explanation of the drawings]

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

[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 native 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 may comprise enzymatically hydrolyzed denatured cheese whey protein. In further or alternative embodiments, the native 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 may further comprise 7.0% by weight or less fat on a dry weight basis. In embodiments, the denatured whey protein composition may comprise 2% or more fat.

[0007]

[0010] Embodiments of the present technology also include a method for producing a denatured whey protein composition, comprising filtering cheese whey from enzymatically coagulated milk to produce 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, on a dry weight basis, 60% or more whey protein by weight, 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] Embodiments of the present technology also include a method for producing a denatured whey protein composition, comprising filtering cheese whey from enzymatically coagulated milk to produce 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, on a dry weight basis, 60% or more protein by weight, less than 11% GMP 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 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 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 undenatured GMP to total whey protein of about 0.15 or less. Additionally, or alternatively, the denatured whey protein composition is characterized by about 11% or less GMP by weight, based on the total weight of the protein. In some embodiments, the denatured whey protein composition is characterized by about 7% or less GMP by weight, based on the total weight of the protein. In additional embodiments, the denatured whey protein composition is characterized by 7% or less fat 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, on a dry weight basis, 60% or more by weight of protein, less than 11% by weight of undenatured GMP based on the total weight of the protein, more than 7% by weight of fat based on a dry weight basis, a β-lactoglobulin to α-lactalbumin ratio 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 by weight of denatured protein prior to denaturation. In additional embodiments, the whey protein contains 60% or more by weight of beta-lactoglobulin based on the total weight of protein. Additionally, or alternatively, in embodiments, the whey protein contains 12% or less by weight of alpha-lactalbumin based on the total weight of protein. In other embodiments, the whey protein comprises a weight ratio of beta-lactoglobulin to alpha-lactalbumin of about 7 or greater. 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] Embodiments of the present technology include protein-enriched food products, including those containing at least 3% by weight of total protein. In embodiments, the protein comprises a denatured whey protein composition, the denatured whey protein composition containing less than 8% by weight of native 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 a protein-enriched food product, the food product containing 3% or more by weight of total protein, the 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 the 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, wherein 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 be 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 between the similar components and / or features. When 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 suffix letter.

[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 from native κ-casein protein in milk by chymosin activity 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% by weight protein as a percentage of total solids, or whey protein isolates (WPIs) can be formed by concentrating whey proteins to 90-99% by weight protein as a percentage of total solids.

[0018] Whey proteins derived from cheese production also include cheese-making enzymes and additional by-products such as protein hydrolysates produced by cheese-making enzymes. For example, enzymatically coagulated milk * Conventional compositions of whey obtained from typically contain:

[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 glycomacropeptide (GMP) hydrolyzed from κ-casein, and the resulting para-κ-casein can form the main component of cheese curd. The smaller, more soluble GMP is carried away with whey proteins and can comprise 13-20% by weight of the protein present in the whey protein fraction on a dry weight basis. Unfortunately, GMP is considered a poor source of protein for muscle recovery after periods of intense exercise and resistance training because it contains fewer branched-chain amino acids, which stimulate muscle protein synthesis and are the primary building blocks in muscle tissue.

[0021] In addition, a high content of native GMP in a whey protein composition can result in undesirable flavors and poor process incorporation. That is, a high content of native GMP (e.g., 12% by weight or more) of protein present in a whey protein fraction on a dry weight basis contributes to an increase in cardboard odor, general off-flavors and / or artificial flavors, and a decrease in natural milk flavor in liquid whey, dry whey, milk protein concentrate, and milk. In addition, native whey protein can 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 can limit the amount of whey protein composition that can be incorporated and reduce the total amount of protein enriched in 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 surprisingly discovered that by carefully processing a 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 is possible to provide high-protein denatured whey protein compositions with a low percentage of native GMP. 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, reduced cardboard notes, and stronger dairy flavors. That is, the present disclosure surprisingly found that enzymatically reducing native GMP in a whey protein composition reduces the process viscosity such that the viscosity is about 10% lower than the viscosity of a composition in which the native GMP has not been 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 has not been enzymatically reduced as described herein, the process viscosity of the composition may 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, for example about 150 mPa·s or less, for example about 125 mPa·s or less, for example about 100 mPa·s or less, for example about 75 mPa·s or less, for example about 50 mPa·s or less, for example up to about 25 mPa·s, or any range or value therebetween). In some embodiments, compositions according to the present technology may also have a reduced ability to bind water. Thus, compositions according to the present technology may be uniquely suitable for fortifying water-containing foods to levels higher than previously thought possible in whey protein compositions, as the observed viscosity increase typically associated with these formulations is lower, at least in part due to reduced interaction with water.

[0024] 1 illustrates 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. Method 100 may include several optional operations that may or may not be 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 that may be readily understood.

[0025] The whey composition raw material utilized herein may be derived from a cheese-making process, whey protein concentrate, whey protein isolate (e.g., 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 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, while any suitable whey raw material may be utilized, the whey raw material utilized to form the denatured whey protein composition is considered to be "sweet whey" and, therefore, filtered from lactose and minerals (102).

[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, e.g., about 50% or more, e.g., about 60% or more, e.g., about 70% or more, e.g., about 80% or more, on a dry weight basis, protein, or any range or value therebetween. 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, e.g., by blending with water, prior to processing to form a whey protein material having a protein concentration in solution of about 30% or less, e.g., about 18% or less, e.g., about 16% or less, e.g., about 15% or less, e.g., about 14% or less, or any range or value therebetween.

[0027] In some embodiments, the native GMP level of a whey protein material may be reduced by utilizing one or more enzymes that selectively reduce native GMP levels 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 isolate purified directly from milk that has not undergone cheesemaking with whey protein concentrate from cheesemaking. 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% by weight or more, such as about 0.0025% by weight or more, such as about 0.005% by weight or more, such as about 0.0075% by weight or more, for example about 0.01% by weight or more, based on the weight of the total protein in the composition, or any range or value therebetween. It will be 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, for example about 20% by weight or more, for example about 25% by weight or more, such as about 30% by weight or more, for example about 35% by weight or more, such as about 40% by weight or more, for example about 45% by weight or more, for example about 50% by weight or more, such as about 60% by weight or more, for example about 65% by weight or more, such as about 70% by weight or more, for example about 72.5% by weight or more, for example about 75% by weight or more, such as about 80% by weight or more, for example about 85% by weight or more, or any range or value therebetween. In other words, in some embodiments, a 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 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, for example, about 60 hours or less, for example, about 48 hours or less, for example, about 36 hours or less, for example, about 24 hours or less, for example, about 12 hours or less, for example, about 10 hours or less, for example, about 8 hours or less, for example, about 5 hours or more, or any range or value therebetween. Hydrolysis can occur at a temperature of about 15.6°C (about 60°F) or less, for example, about 12.8°C (about 55°F) or less, for example, about 10°C (about 50°F) or less, for example, about 7.22°C (about 45°F) or less, or any range or value therebetween.

[0031] Nevertheless, in some embodiments, the native GMP level of a whey protein material may be reduced by utilizing a high-fat raw material (103). By using a whey protein retentate from a microfiltration process in which a portion of the GMP permeates the microfiltration membrane, it is possible to provide a whey protein material with 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, for example, about 8% or more, for example, about 9% or more, for example, about 10% or more, for example, about 11% or more, for example, about 12% or more, for example, about 13% or more, for example, about 14% or more, for example, about 15% or more, for example, about 16% or more, for example, about 17% or more, for example, about 18% or more, for example, about 19% or more, for example, about 20% or more, for example, about 20.5% or more, or any range or value therebetween, based on the dry basis weight of the whey protein material.

[0032] In some embodiments, the above-described low native GMP levels and high fat levels in the high-fat feedstock can be achieved 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, the 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 other filtration methods can be utilized in some embodiments to provide a high-fat, low-native GMP feedstock.

[0033] However, in embodiments utilizing microfiltration membranes, it has surprisingly also been found that the ratio of β-lactoglobulin to α-lactalbumin can be increased. That is, without wishing to be bound by theory, β-lactoglobulin may be more likely to denature earlier than α-lactalbumin. Thus, β-lactoglobulin may be largely retained by the membrane along with the denatured whey proteins, while α-lactalbumin passes through at a higher rate with the permeate. In some embodiments, the whey protein raw material composition of the present technology exhibits a ratio of β-lactoglobulin to α-lactalbumin of about 2.75 or more, such as about 3 or more, for example about 3.5 or more, for example about 4 or more, for example about 4.5 or more, for example about 5 or more, for example about 5.5 or more, for example about 6 or more, for example about 6.5 or more, for example about 7 or more, for example 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, for example about 70% by weight or more, such as about 72.5% by weight or more, for example about 75% by weight or more, or any range or value therebetween of β-lactoglobulin. 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, for example about 10% by weight or less, such as about 7.5% by weight or less of α-lactalbumin, 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, e.g., about 60°C (about 140°F) to about 148.9°C (about 300°F), e.g., about 71.11°C (about 160°F) to about 98.89°C (about 210°F), e.g., about 76.67°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 denatured whey protein. The slurry may be mixed and heated for about 1 second to about 120 seconds, such as about 2.5 seconds to about 105 seconds, such as 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. As used herein, mechanical shear conditions generally refer to shear conditions of about 1,000 s -1A shear of more than 10,000 s is applied. -1 A shear of greater than 50,000 s is applied. -1 A shear of more than 100,000 s is applied, e.g. -1 More than 500,000 shear forces are applied. -1 In some embodiments, the denatured whey protein composition is 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% 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, 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 compositions of the present technology, the final protein contains about 45 wt. % or more, such as about 50 wt. % or more, for example about 55 wt. % or more, such as about 60 wt. % or more, for example about 65 wt. % or more, such as about 70 wt. % or more, for example about 75 wt. % or more, such as about 77.5 wt. % or more, for example about 80 wt. % or more, such as about 85 wt. % or more, for example about 90 wt. % or more, or any range or value therebetween, of denatured whey protein relative to the total weight of protein in the whey protein composition.

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

[0040] Regardless of the final protein composition, the denatured whey protein composition, after heating and shearing, may optionally be cooled and concentrated, 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 may 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, for example about 10 wt. % or less, such as about 9 wt. % or less, for example about 8 wt. % or less, such as about 7 wt. % or less, for example about 6.5 wt. % or less, such as about 6 wt. % or less, for example about 5.9 wt. % or less, such as about 5 wt. % or less, for example about 4 wt. % or less, such as about 3 wt. % or less, for example about 2 wt. % or less, for example about 1 wt. % or less, or any range or value therebetween.

[0042] Thus, in some embodiments, the denatured whey protein composition 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 the hydrolysis of GMP in whey protein raw materials, hydrolyzed GMP is formed, which 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, for example, about 2 wt% or more, for example, about 3 wt% or more, for example, about 4 wt% or more, for example, about 5 wt% or more, for example, about 6 wt% or more, for example, about 7 wt% or more, for example, about 8 wt% or more, for example, 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, because native GMP is acted upon by one or more enzymes, the denatured whey protein composition may, in some embodiments, have an increased proteolytic index. The proteolytic index is a measure of the increase in non-protein nitrogen (NPN) relative to the total Kjeldahl nitrogen (TKN) of a sample, and its determination method is described in the Examples below. That is, the proteolytic index (PI) 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 become soluble in trichloroacetic acid, and can therefore be an indicator of protein hydrolysis. 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, for example, about 7 wt.% or more, for example, about 8 wt.% or more, for example, about 9 wt.% or more, for example, about 10 wt.% or more, for example, about 12.5 wt.% or more, for example, about 15 wt.% or more, for example, about 17.5 wt.% or more, for example, about 20 wt.% or more, for example, about 22.5 wt.% or more, for example, about 25 wt.% or more, or any range or value therebetween.

[0045] Further, in some embodiments described above, the denatured whey protein compositions may be considered "high fat" and may have a fat content of about 7% or more, such as about 8% or more, for example about 9% or more, for example about 10% or more, such as about 11% or more, for example about 12% or more, such as about 13% or more, for example about 14% or more, such as about 15% or more, for example about 16% or more, such as about 17% or more, for example about 18% or more, such as about 19% or more, for example about 20% or more, for example about 20.5% or more, or any range or value therebetween, based on the dry basis weight of the whey protein material. However, in some embodiments, the denatured whey protein compositions contain less than 7% by weight fat, such as about 6.5% by weight or less, for example 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 compositions as described herein, it is possible to obtain whey protein with narrow particle size distribution, thereby further improving the flavor characteristics of the denatured whey protein compositions of the present technology.For example, the particle can have the D90 particle size distribution value (the particle size that 90% of the mass of sample comprises particles of this size or less) of about 8 μ m or less, for example about 7 μ m or less, for example about 6 μ m or less, for example about 5 μ m or less, for example about 4 μ m or less, for example about 3 μ m or less, for example about 2 μ m or less, for example about 1.75 μ m or less, for example about 1.5 μ m or less, for example about 1.25 μ m 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 that size or less) of about 5 μm or less, such as about 4.5 μm or less, for example about 4 μm or less, for example about 3.5 μm or less, such as about 3 μm or less, for example about 2.5 μm or less, such as about 2 μm or less, for example about 1.5 μm or less, such as about 1 μm or less, for example 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 the sample contains particles of that size or less) of about 3 μm or less, such as about 2.5 μm or less, for example about 2 μm or less, for example about 1.5 μm or less, such as about 1 μm or less, for example about 0.5 μm or less, such as about 0.4 μm or less, for example about 0.3 μm or less, such as about 0.2 μm or less, for example 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 their denatured form or 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 just one example of a product and method for fortifying a product using the denatured whey protein composition described herein, a yogurt composition can be formed as known in the art. For example, spoonable yogurt milk or drinking yogurt milk (which may contain whole milk, skim milk, or a combination thereof fortified 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 flavorings 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, for example about 300 mPa·s or less, such as about 250 mPa·s or less, for example about 200 mPa·s or less, such as about 150 mPa·s or less, for example 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] Furthermore, 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, for example 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 Quantitation of glycomacropeptide (GMP), α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) Quantitative determination of GMP was performed using a Beckman capillary electrophoresis system. The capillary was DOV-1701OH Deactivated TSP standard FS tubing (600 mm × 50 μm) with a 100 × 800 μm slit opening and regenerated / activated with 0.1 N HCl solution.

[0055] Preparation of sample solution: -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 ethylenedinitrilotetraacetic acid, and 0.5 g / L methylhydroxypropylcellulose in 8 M urea.

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

[0058] - The sample is filtered into a glass vial using a PVDF 0.22 μm syringe filter. A cap is placed on the glass vial. The sample solution is injected for 10 seconds at 3.4 Kpa. Separation is carried out at 45°C and 25 KV (initially increasing from 0 to 25 KV within 3 minutes). Detection of milk proteins is carried out 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) / (total peak area of ​​all proteins)) × 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 extraction procedure.

[0061] Quantitative protein analysis by total Kjeldahl nitrogen (TKN) Protein analysis by Kjeldahl nitrogen (reference method AOAC 991.20) is used to determine the weight percentage of nitrogen compounds. Sulfuric acid breaks down protein and other nitrogen compounds, converting the nitrogen to ammonium sulfate. A catalyst is used to increase the reaction rate and 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 normalized HCl added to sample - amount (in mL) added to blank (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 weight of nitrogen (mg / meq). - The constant 6.38 is the number of grams of milk protein per gram of nitrogen. 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, all of which are soluble in trichloroacetic acid (Ruska and Jonkus, 2014). Generally, although not a definitive rule, more than 30 amino acids are sufficient to qualify a polypeptide as a protein; peptides consisting of fewer than 30 amino acids are likely to be found in the TCA-soluble fraction and classified as non-protein nitrogen. This method involves precipitating proteins using the addition of trichloroacetic acid (TCA). The proteins are then filtered off, and the non-protein nitrogen in the filtrate is measured. The amount of non-protein nitrogen can then be determined.

[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 10-15 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 the sample, TCA solution, and added water is approximately 50 g. Record the total weight. G. Mix well and let the solution 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 tube. Record the exact mass of filtrate added.

[0071] J. Test in the 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 required to titrate the sample distillate.

[0072] • N = exact normality (meq / mL) of standardized HCl from the lot certificate of analysis (COA) or 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 = number of grams of sample filtrate used. ● A = number of grams of sample used.

[0074] ● B = total number of grams of sample solution. ● 10 converts the result to grams per 100 grams. Determination of True Protein 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 of net protein by weight (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] Measurement of denatured whey protein 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 native 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 0.1 N HCl or 0.1 N NaOH.

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

[0080] - 25g 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 a coarse adjustment and 0.1 Normal HCl for a fine adjustment.

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

[0083] - Place the tube in the centrifuge and ensure the tube is balanced. Centrifuge at 10,000 rpm for 15 minutes at 10°C. Do not use the brake to speed up deceleration. -Without transferring any of the pellet material, transfer ~10 mL 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 dilution / 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 absorption index 0.0001, and dispersant refractive index 1.33, with water as the dispersant. The Mie scattering model was used for the analysis.

[0085] Example 1 A glycomacropeptide (GMP)-reduced denatured whey protein composition was produced using a whey protein composition (WPC) with a dry weight basis of greater than 25% protein from sweet whey in mozzarella cheese production. The process begins with a WPC retentate (80% protein on a dry basis) concentrated using ultrafiltration (UF) of pasteurized sweet whey separated from cheese curds. The 80% WPC (WPC80) retentate is transferred to a temperature-controlled holding tank and kept at or below about 45°F (7.22°C), 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 phase 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, or up to about 0.012% by weight, of the total protein in the substrate. 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 7.22°C (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 87.78°C (190°F) for 6 seconds (operating range: about 80°C to about 90.56°C (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 optionally cooled (e.g., to about 10°C (50°F)) and concentrated (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 micronized denatured whey protein composition was approximately 1.7 micrometers (mm) or less, showing a narrower range than that of the whey protein raw material (characterized by D90).

[0089] Figure 2A shows the unmodified (feed) particle size, which ranges from 0.011 to 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 to 4.03 micrometers, as shown in Figure 2B. Figure 2C provides a comparative overlay of the particle size distributions 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 micronized denatured whey protein composition was determined by capillary electrophoresis (CE) and is defined as the native GMP peak area divided by the total protein peak area on the CE graph, as shown in Figures 3A and 3B.

[0091] As mentioned above, denatured whey protein (DWP) and the proteolysis index (PI), defined as the division of non-protein nitrogen by total nitrogen, are determined by wet chemical analysis. Table 1 shows 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, the proteolysis index increases concomitantly as the native GMP protein breaks down into smaller fragments, increasing the amount of non-protein nitrogen. Figures 3A and 3B show that while GMP is substantially reduced during hydrolysis, α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) remain largely unhydrolyzed, a result of controlled hydrolysis, further indicated by a minimal decrease (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 treatments during the enzyme inactivation procedure.

[0092] Table 1:

[0093] [Table 2]

[0094] *-Denatured Whey Protein % ^-% Fat on dry basis 1-Proteolysis 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] Protein denaturation was achieved by preheating the feed to about 130°F (operating range 120-150°F), then heating to the denaturation temperature of about 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 to 11.2 micrometers. After the denaturation and shear process, the particle size decreased to a range of 0.011 to 2.75 micrometers, as shown in Figure 4B. Figure 4C provides a comparative overlay of particle size distributions 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 for high-fat WPC has lower GMP (10.5 vs. 20.5%), higher denatured whey protein (DWP) (45.10 vs. 17.27%), higher fat on a dry basis (17.66 vs. 6.35), and a higher β-lactoglobulin to α-lactalbumin ratio (7.65 vs. 3.37) compared to the starting feed WPC 80. While the production of high-fat WPC uses ultrafiltration and microfiltration, the production of WPC 80 uses only ultrafiltration. One explanation may 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. Because β-lactoglobulin is more susceptible to denaturation than α-lactalbumin during milk pasteurization and subsequent sweet whey pasteurization, the retained protein is likely to contain more denatured β-lactoglobulin than α-lactalbumin. Therefore, 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 were utilized to enhance drinking yogurt applications to observe functional benefits in viscosity management of high protein products.

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

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

[0103] 5. Maintain the 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 fortification can be of interest to consumers. Examples of protein fortification in drinking yogurt are shown in Tables 3 and 4 and Figure 5. As shown, drinking yogurt fortified to 10% protein using the GMP-reduced modified WPC80 composition and GMP-reduced modified hfWPC according to the present technology has a preferable lower viscosity when compared to a commercially available product with a protein level of 7.54%. Thus, the present technology shows a significant reduction in viscosity even at higher fortification levels. The reduced viscosity is beneficial to the consumer experience due to increased protein per serving and ease of product consumption.

[0109] As shown, increasing protein in yogurt applications is challenging. Yogurt viscosity generally increases as protein is added. This is because proteins commonly used to fortify foods (such as casein and undenatured whey proteins) bind and interact with water, resulting in a more viscous texture. The advantage of using the denatured whey composition of the present technology in products such as yogurt is the ability to fortify protein content while maintaining acceptable viscosity. This is shown in Table 4, which compares viscosity data for yogurts fortified with a control (no WPC), standard GMP undenatured WPC 80, and GMP-reduced denatured WPC 80, demonstrating the practical viscosity solution provided by the GMP-reduced denatured whey protein composition. As shown, the control yogurt (no WPC) was very viscous, with a viscosity greater than 25,000 mPa·s, and therefore unpourable and unacceptable as a drinking yogurt product. Similarly, drinking yogurt fortified with standard GMP unmodified WPC80 had a viscosity of 4040 mPa·s, which is still too viscous to be acceptable for a drinking yogurt product. On the other hand, yogurt fortified with the GMP-reduced modified WPC80 according to the present technology exhibited a viscosity of 90 mPa·s, which is acceptable for pourability and as a drinking yogurt product. In addition, the GMP-reduced modified WPC80 performed very favorably compared to the commercial reference (viscosity of 580 mPa·s).

[0110] Table 4 shows viscosity data for a control (no WPC), GMP-reduced unmodified hfWPC, and GMP-reduced denatured 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 show, the control yogurt (no WPC) was very viscous, having a viscosity greater than 25,000 mPa·s, and therefore was not pourable or acceptable as a drinking yogurt product. Similarly, the drinking yogurt fortified with GMP-reduced unmodified hfWPC exhibited a lower viscosity of 860 mPa·s, which is still too viscous and unacceptable for a drinking yogurt product. In contrast, the yogurt fortified with GMP-reduced denatured 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 A denatured whey protein composition was utilized to enhance a spoonable yogurt application 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 yogurts. The data demonstrate that the GMP-reduced denatured whey protein composition according to the present disclosure exhibits greater impact in increasing the protein content of spoonable yogurts without a corresponding increase in viscosity or a change in acceptable texture. A commercially available reference spoonable yogurt containing 10% protein had a viscosity of 11,000 mPa·s. When the protein was increased to 14.7% using GMP-reduced undenatured 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 increased protein content in spoonable yogurts 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 (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 three-digit codes and evaluated. Beverages were evaluated in duplicate by seven trained panelists using an established sensory language for whey protein. Descriptive flavor analysis utilized 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 (SAS version 9.1, Cary, NC) with Fisher's least significant difference (LSD) as a post-hoc test.

[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 significantly reduces the cardboard flavor often considered an off-flavor and present in many dairy proteins. In addition, GMP reduction resulted in improved dairy flavor, which is considered a beneficial flavor attribute in products suitable for dairy applications.

[0119] The results of the GMP-reduced denatured WPC are further substantiated by similar flavor observations when denatured high-fat whey protein compositions originally with lower GMP were evaluated. Here again, it was observed that the lower GMP, coupled with protein denaturation, resulted in a trend toward less carbonation and a significant increase in dairy flavor.

[0120] Table 7

[0121] [Table 8]

[0122] Aroma and flavor intensity was scored on a universal intensity scale (Spectrum method, Meilgaard et al., 1999) from 0 to 15 points. ND - not detected. Means of columns followed by different letters are different (p<0.05). No traits not listed were 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 greater; and greater than 50% by weight of denatured whey protein based on the total weight of said protein in said denatured whey protein composition.

2. 10. 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 the undenatured GMP is about 7% or less by weight based on the total weight of the protein in the 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 no more than 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 greater 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 the 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 wherein 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, or the denatured whey protein composition is characterized by about 11% by weight or less GMP relative to the total weight of the protein in the denatured whey protein composition, or both.

14. 1. A denatured whey protein composition comprising: 60% by weight or more of protein on a dry weight basis; less than 11% by weight of native glycomacropeptide (GMP) based on the total weight of the protein; greater than 7% by weight fat 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 the 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 of 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 based on the total weight of protein, or 12% or less by weight of alpha-lactalbumin based on 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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