Polyelectrolyte complexes of proteins and uses thereof

Abstract

The present disclosure relates generally to polyelectrolyte complexes of non-animal proteins and their use in a variety of edible products (e.g., food, beverage and nutritional products, including meat analogue products and dairy analogue products). In some embodiments, the polyelectrolyte complex comprises a vegetable protein such as a pea protein, a soy protein, a canola protein, a potato protein, and a pulse protein such as a broad bean protein. In some embodiments, the polyelectrolyte complex masks certain unpleasant tastes of one or more proteins and improves the mouth feel of edible compositions including the protein complex. In some embodiments, the polyelectrolyte complex is used in combination with certain fibers, which makes the blend suitable for addition to ingestible compositions useful in the manufacture of meat analogue products and dairy analogue products. In some embodiments, a flavouring or flavor modifying agent is also used in combination with the polyelectrolyte complex.

Description

Technical Field

[0001] The present disclosure generally relates to polyelectrolyte complexes of non-animal proteins and their use in various edible products (e.g., food products, beverage products, and nutritional products, including meat analog products and dairy analog products). In some embodiments, the polyelectrolyte complex comprises plant proteins such as pea protein, soy protein, canola protein, potato protein, and legume protein such as faba bean protein. In some embodiments, the polyelectrolyte complex masks certain unpleasant tastes of one or more proteins and improves the mouthfeel of edible compositions including the protein complex. In some embodiments, the polyelectrolyte complex is used in combination with certain fibers, which makes the blend suitable for addition to ingestible compositions that can be used to make meat analog products and dairy analog products. In some embodiments, flavorings or flavor-modifiers are also used in combination with the polyelectrolyte complex. Background Art

[0002] The human diet typically includes products of both animal and non-animal origin. The proportion of calories consumed from products of animal origin has increased in recent years. This presents some health concerns, as eating too much meat, especially meat that is high in fat and cholesterol, often leads to heart disease and related problems. Another issue has to do with sustainability. Raising meat-eating animals typically requires large amounts of grain or grass as animal feed. The area of ​​land required to grow grass or grain to feed these animals is several times the area of ​​land required to grow plants for direct human consumption. Therefore, as the global population continues to rise, the need for increased agricultural space is becoming increasingly unsustainable.

[0003] Therefore, there is a growing need to replace animal-derived foods in the human diet with similar materials from plants, algae, fungi, etc. In many cases, since consumers are accustomed to eating animal-derived foods, these alternative non-animal-derived foods are intended to simulate the flavor, texture, and cooking experience of eating animal-derived foods. Such non-animal-derived foods are often referred to as meat analogs or dairy analogs. But making such meat and dairy analog materials brings many challenges, especially when people try to use plant-derived materials to make food products that simulate meat and dairy products.

[0004] One of the challenges is masking certain unpleasant tastes and improving the mouthfeel of plant-based proteins. For example, pea protein is often used to make plant-based alternatives to meat and dairy products. But pea protein can bring unpleasant plant and grain flavors, and many consumers think it tastes chalky. Combining plant proteins with certain masking agents can solve this problem to some extent. But these solutions usually have to be tailored to specific proteins or batches of proteins.

[0005] Therefore, there is an ongoing need to develop a more universal approach to mask off-flavors or improve the taste of non-animal proteins. Summary of the invention

[0006] The present disclosure relates to the discovery that forming certain polyelectrolyte complexes of non-animal proteins can provide improved taste (ie, by masking off-flavors) and improved mouthfeel relative to using non-animal proteins without including them in such polyelectrolyte complexes.

[0007] In the first form, the present disclosure provides a polyelectrolyte complex comprising (a) a non-animal protein having a net positive charge (i.e., a polycationic non-animal protein) and (b) a polyionic polymer having a net negative charge (i.e., a polyanionic polymer). In some embodiments, the polycationic non-animal protein is a plant protein, such as pea protein, soy protein, canola protein, broad bean protein, etc. In some embodiments, the polyanionic polymer is pectin, gum arabic, carrageenan, sunflower protein, etc. In some embodiments, the polyelectrolyte complex is in the form of a solid precipitate, for example, it is formed by precipitating the composite polymer from an aqueous medium under acidic conditions. In some embodiments, the polyelectrolyte complex is a core-shell coacervate, wherein the shell portion comprises the polyelectrolyte complex.

[0008] In a second form, the present disclosure provides the use of polyanionic polymers for reducing one or more peculiar smells of polycationic non-animal proteins. In some embodiments, the use includes forming a polyelectrolyte complex between the polyanionic polymer and the polycationic non-animal protein. In some embodiments, the reduced peculiar smell includes nutty taste, cereal taste, beany taste, astringent taste, bitter taste, high acid taste, green plant taste, acidic taste or any combination thereof. In certain related forms, the present disclosure provides a method for reducing one or more peculiar smells of polycationic non-animal proteins, the method including forming a polyelectrolyte complex between the polyanionic polymer and the polycationic non-animal protein. In some embodiments, the polycationic non-animal protein is a plant protein, such as pea protein, soy protein, broad bean protein, etc. In some embodiments, the polyanionic polymer is pectin, gum arabic, sunflower protein, etc. In some embodiments, the polyelectrolyte complex is in the form of a solid precipitate, for example, it is formed by precipitating the composite polymer from an aqueous medium under acidic conditions.

[0009] In a third aspect, the present disclosure provides the use of polyanionic polymers for enhancing the mouthfeel of polycationic non-animal proteins or enhancing their texture. In some embodiments, enhancing texture includes improving the perceived thickness of an ingestible composition. In some embodiments, the use includes forming a polyelectrolyte complex between a polyanionic polymer and a polycationic non-animal protein. In certain related aspects, the present disclosure provides a method for enhancing the mouthfeel of polycationic non-animal proteins, the method including forming a polyelectrolyte complex between a polyanionic polymer and a polycationic non-animal protein. In some embodiments, the polycationic non-animal protein is a plant protein, such as pea protein, soy protein, broad bean protein, etc. In some embodiments, the polyanionic polymer is pectin, gum arabic, sunflower protein, etc. In some embodiments, the polyelectrolyte complex is in the form of a solid precipitate, for example, it is formed by precipitating the composite polymer from an aqueous medium under acidic conditions.

[0010] In a fourth aspect, the present disclosure provides an ingestible composition comprising the polyelectrolyte complex of the first aspect. In some embodiments, the ingestible composition comprises a sweetener, a sweetness enhancer, an umami tastant, an umami enhancer, a kokumi tastant, a bitterness blocker, a flavoring agent, or any combination thereof. In some embodiments, the ingestible composition comprises a fiber component.

[0011] In a fifth aspect, the present disclosure provides a flavored product comprising the ingestible composition of the fourth aspect. In some embodiments, the flavored product is a beverage product, such as a dairy product or a dairy analog product. In some other embodiments, the flavored product is a food product, such as a yogurt, or a meat analog product, such as a chicken analog product, a beef analog product, etc., or a seafood analog product, such as a shellfish analog product. In some embodiments, the flavored product is an animal feed product, such as a cat food or dog food product.

[0012] Further aspects and embodiments thereof are set forth in the following detailed description, drawings, abstract and claims. BRIEF DESCRIPTION OF THE DRAWINGS

[0013] The following figures are provided to illustrate various embodiments of the compositions and methods disclosed herein. The figures are provided for illustration purposes only and are not intended to describe any preferred compositions or preferred methods, nor as a source of any limitation on the scope of the claimed invention.

[0014] Figure 1 Three photomicrographs at 20 times magnification of the precipitate after stirring for 30 minutes, stirring for 1 hour, and stirring for 3 hours are shown.

[0015] Figure 2 Three photomicrographs at 20 times magnification of the precipitate after stirring for 30 minutes, stirring for 1 hour, and stirring for 3 hours are shown.

[0016] Figure 3 A 20X magnification micrograph is shown after the precipitate has fully formed.

[0017] Figure 4 Micrographs at 20X magnification after precipitate formation are shown.

[0018] Figure 5 A 40x magnification micrograph of the particles formed after spray drying is shown.

[0019] Figure 6 A 40x magnification micrograph of the particles formed after spray drying is shown.

[0020] Figure 7 A micrograph at 40 times magnification after precipitate formation is shown.

[0021] Figure 8 Micrographs at 40X magnification after microparticle formation and after enzyme inactivation are shown.

[0022] Fig. 9 Micrographs at 40 times magnification of the microparticles formed after the deactivation step are shown, case a on the left and case b on the right.

[0023] Fig.10 Micrographs taken after inactivation at 40X magnification are shown.

[0024] Fig.11 Micrographs at 40X magnification of the microparticles formed after inactivation for the four conditions are shown.

[0025] Fig.12 Micrographs of the complexes formed are shown: a) pea protein isolate / canola protein isolate; b) pea protein isolate / potato protein isolate; c) pea protein isolate / soluble wheat gluten.

[0026] Fig.13 Micrographs of the particles formed are shown, with the lower bar representing 50 microns.

[0027] Fig.14 Micrographs of the resulting emulsions are shown, with the lower bar representing 50 microns. DETAILED DESCRIPTION

[0028] The following detailed description sets forth various configurations and embodiments provided herein. This description will be read from the perspective of a person of ordinary skill in the relevant art. Therefore, information known to these persons of ordinary skill is not necessarily included.

[0029] definition

[0030] Unless otherwise provided herein, the following terms and phrases have the meanings indicated below. The present disclosure may employ other terms and phrases not expressly defined herein. Such other terms and phrases have the meanings they have in the context of the present disclosure for those of ordinary skill in the art. In some cases, a term or phrase may be defined in the singular or in the plural. In this case, it is to be understood that any term in the singular may include its plural form, and vice versa, unless expressly indicated to the contrary.

[0031] As used herein, "sweetener," "sweet flavoring," "sweet flavor entity," or "sweet compound" refers to a compound that elicits a detectable sweet flavor in a subject, such as a compound that activates a human T1R2 or T1R3 receptor in an in vitro screening process, or a compound that is reported as sweet by a sensory test of human subjects.

[0032] As used herein, "sweetener" or "sweet tastant" refers to a compound that elicits a detectable sweet flavor in a subject, such as a compound that activates human T1R2 or T1R3 receptors in an in vitro screening procedure, or a compound that is reported as savory by a sensory test of human subjects.

[0033] As used herein, "umami tastant" refers to a compound that elicits a detectable umami flavor in a subject, such as a compound that activates human T1R1 or T1R3 receptors in an in vitro screening procedure, or a compound that is reported as palatable by sensory testing in human subjects.

[0034] As used herein, "bitter tastant" refers to a compound that elicits a detectable bitter flavor in a subject, such as a compound that activates one or more human T2R receptors in an in vitro screening process, or a compound that is reported as palatable by sensory testing in human subjects.

[0035] As used herein, "polyanionic polymer" refers to a polymer containing multiple anionic functional groups in a polyelectrolyte complex. Such polyanionic polymers have a lower isoelectric point than polycationic polymers.

[0036] As used herein, "polycationic polymer" refers to a polymer having multiple cationic functional groups in a polyelectrolyte complex. "Polycationic protein" refers to a polymer wherein the polymer is a protein, such as a non-animal protein or a plant protein. Such polycationic polymers have a higher isoelectric point than polyanionic polymers.

[0037] As used herein, "polyelectrolyte complex" refers to an association complex formed between a polyanionic polymer and a polycationic polymer. Such an association complex can be precipitated as particles, such as microparticles, or used to form a part of the shell material of a core-shell microcapsule in the form of a coacervate.

[0038] As used herein, the singular forms "a," "an," and "the" include plural referents unless the context clearly dictates otherwise. For example, reference to "a substituent" encompasses a single substituent as well as two or more substituents, and so forth.

[0039] As used herein, "for example," "such as," "such as," or "including" are intended to introduce examples that further illustrate a more general subject matter. Unless otherwise expressly noted, such examples are provided merely to aid in understanding the embodiments shown in the present disclosure and are not meant to be limiting in any way. These phrases also do not indicate any kind of preference for the disclosed embodiments.

[0040] As used herein, "include," "comprising," "containing," and "comprised of" refer to an open group, meaning that the group may include other members in addition to those explicitly stated. For example, the phrase "comprising A" means that A must be present, but other members may also be present. The terms "including," "having," and "composed of" and their grammatical variants have the same meaning. In contrast, "consist of" or "composed of" or "composed of" refer to a closed group. For example, the phrase "consisting of A" means that only A is present.

[0041] As used herein, "optionally" means that the subsequently described event may or may not occur. In some embodiments, the optional event does not occur. In some other embodiments, the optional event does occur one or more times.

[0042] As used herein, "or" is to be given its broadest reasonable interpretation and is not limited to an "either / or" construction. Thus, the phrase "comprising A or B" means that A may be present and B may not be present, or B may be present and A may not be present, or both A and B may be present. Furthermore, for example, if A defines a group that may have multiple members (e.g., A 1 and A 2 ) of a class, one or more members of the class can exist at the same time.

[0043] Other terms are defined in other parts of this specification even if not included in this section.

[0044] Polyelectrolyte complex

[0045] In certain aspects, the present disclosure provides polyelectrolyte complexes comprising polycationic non-animal proteins and polyanionic polymers. In these complexes, the polycationic non-animal proteins and polyanionic polymers are associated with each other due to their opposite net charges.

[0046] Any suitable polycationic non-animal protein can be used, such as polycationic proteins derived from plants, algae and fungi. In some embodiments, the polycationic non-animal protein is a polycationic plant protein. Non-limiting examples of such plant proteins include pea protein, soy protein, broad bean protein and potato protein. In some embodiments, the polycationic non-animal protein is pea protein, soy protein or a combination thereof. In some embodiments, the polycationic non-animal protein is pea protein. In some embodiments, the polycationic non-animal protein is soy protein. In some embodiments, the polycationic non-animal protein is broad bean protein. In some embodiments, the polycationic non-animal protein is potato protein, such as potato protein comprising or mainly consisting of patatin (patatin, potato tuber specific protein).

[0047] In the polyelectrolyte complex disclosed herein, polycationic non-animal protein is associated with a polyanionic polymer. Any polyanionic protein suitable for consumption is acceptable. Non-limiting examples of such polymers include pectin, gum arabic, carrageenan, or certain plant proteins, such as sunflower protein and mung bean protein. In some embodiments, the polyanionic polymer is pectin. In some embodiments, the polyanionic polymer is gum arabic. In some embodiments, the polyanionic polymer is carrageenan. In such embodiments, any suitable carrageenan can be used, such as iota-carrageenan, kappa-carrageenan, lambda-carrageenan, or any combination thereof. In some embodiments, the polyanionic polymer is a plant protein. Note that plant proteins can be polyanions or polycations, depending on whether the pH is below its isoelectric point (polycation) or above its isoelectric point (polyanion). In some embodiments, the polyanionic polymer is sunflower protein. In some embodiments, the polyanionic polymer is mung bean protein. In some embodiments, the polyanionic polymer is pea protein. In some embodiments, the polyanionic polymer is a moong bean protein, such as a potato protein comprising or consisting essentially of potato glycoprotein.

[0048] As mentioned above, most proteins can act as either polyanionic polymers or polycationic non-animal proteins, depending on whether they are in an aqueous medium with a pH above or below their isoelectric point. Thus, depending on the pH at which the polyelectrolyte is formed, the polyanionic polymer or polycationic non-animal protein can be pea protein, soy protein, canola protein, hemp protein, potato protein, mung bean protein, sunflower protein, fava bean protein, wheat gluten, algae protein, etc.

[0049] The polycationic non-animal protein and the polyanionic polymer can be present in the polyelectrolyte complex in any suitable weight ratio. For example, in some embodiments, the weight ratio of the polycationic non-animal protein to the polyanionic polymer in the polyelectrolyte complex ranges from 1:10 to 10:1, or from 1:5 to 5:1. In some other embodiments, the weight ratio of the polycationic non-animal protein to the polyanionic polymer in the polyelectrolyte complex ranges from 1:1 to 10:1, or from 1:1 to 5:1.

[0050] The polyelectrolyte complex can be formed in any suitable manner. For example, in some embodiments, when the polyelectrolyte complex is a solid, the polyelectrolyte complex is a precipitate formed in an aqueous medium. This precipitation can be carried out at any suitable pH, but is generally carried out at a pH lower than the neutral charge point (and the lowest water solubility) of the two polymers. In some embodiments, the precipitate is formed when the pH range is 2.5 to 5.0, or 2.5 to 4.5, or 3.0 to 4.0. In this case, the resulting precipitate is a particle. Such particles can be ground and other processes to produce a more uniform particle size and reduce agglomeration and agglomeration.

[0051] These resulting particles generally have a zeta potential in aqueous media. In some embodiments, the particles of the polyelectrolyte complex have a zeta potential in the range of -30 mV to 30 mV, or -20 mV to 20 mV, or -10 mV to 10 mV in water.

[0052] In some embodiments, the particles comprise cross-linked polyanionic and polycationic polymers, for example, by introducing an enzyme (eg, transglutaminase) to cross-link the polymers.

[0053] Polycationic plant proteins have certain peculiar smells, such as beany, nutty, cereal, astringent, green plant, bitter, highly acidic or acidic, which many consumers consider unpleasant. Surprisingly, it was found that polyelectrolyte complexes containing these plant proteins do not exhibit such peculiar smells when eaten to the same extent as uncompounded plant proteins. Therefore, forming a polyelectrolyte complex (such as the above-mentioned complex) provides a suitable method for reducing the peculiar smell of polycationic plant proteins. Therefore, in some forms, the present disclosure provides the use of polyanionic polymers (according to any of the above-mentioned embodiments) to reduce one or more peculiar smells of polycationic non-animal proteins (according to any of the above-mentioned embodiments). In some embodiments, this use includes forming a polyelectrolyte complex between polycationic non-animal proteins and polyanionic polymers. In some related forms, the present disclosure provides a method for reducing one or more peculiar smells of polycationic non-animal proteins (according to any of the above-mentioned embodiments), the method including forming a polyelectrolyte complex between polycationic non-animal proteins (according to any of the above-mentioned embodiments) and polyanionic polymers. These off-flavors include nutty, grainy, beany, astringent, bitter, green, high acid, sour, and some vegetal and green notes. These notes include both aroma and flavor.

[0054] Polycationic plant proteins also tend to have a mouthfeel that many consumers do not like. For example, many consumers believe that such proteins have a certain powdery texture, which often causes products containing such proteins to feel dry or not juicy enough. Surprisingly, it was found that polyelectrolyte complexes containing these plant proteins showed a better mouthfeel than uncompounded plant proteins. In some cases, this is considered to be enhanced juiciness. Therefore, forming polyelectrolyte complexes, such as those described above, provides a suitable method for reducing the off-flavor of polycationic plant proteins. Therefore, in some forms, the present disclosure provides (according to any of the above-mentioned embodiments) polyanionic polymers for enhancing the mouthfeel or juiciness of polycationic non-animal proteins (according to any of the above-mentioned embodiments). In some embodiments, this use includes forming a polyelectrolyte complex between polycationic non-animal proteins and polyanionic polymers. In some related forms, the present disclosure provides a method for enhancing the mouthfeel or juiciness or perceived consistency of polycationic non-animal proteins (according to any of the above-mentioned embodiments), the method including forming a polyelectrolyte complex between polycationic non-animal proteins (according to any of the above-mentioned embodiments) and polyanionic polymers.

[0055] When the polyelectrolyte complex is added to an ingestible composition, it can be used at a concentration similar to that of the uncomplexed protein in such a composition. In other cases, lower amounts can be used, for example, when only a portion of the uncomplexed protein is replaced with the polyelectrolyte complex, or when the polyanionic polymer is also a protein.

[0056] Microparticle formation method

[0057] Microparticles comprising polyelectrolyte complexes can be formed in any suitable manner. In some embodiments, the first polymer and the second polymer are introduced into an aqueous medium, wherein the first polymer has a first isoelectric point, and the second polymer has a second isoelectric point, which is higher than the first isoelectric point. In some such embodiments, the pH of the aqueous medium is adjusted to a pH between the first isoelectric point and the second isoelectric point, so that the first polymer becomes a polyanionic polymer, and the second polymer becomes a polycationic polymer. In some embodiments, polyanionic polymers and polycationic polymers are associated in an aqueous medium, and precipitated to form microparticles. Such particles can be ground and other processes to produce a more uniform particle size and reduce agglomeration and agglomeration. In some other embodiments, the association of polyanionic polymers and polycationic polymers occurs in the presence of an enzyme (e.g., transglutaminase) and an optionally used oil (e.g., fatty acid glyceride). Suitable fatty acid glycerides include capric glyceride, caprylic glyceride, or any combination thereof.

[0058] Ingestible composition

[0059] In certain forms, the present disclosure provides an ingestible composition comprising a polyelectrolyte complex according to any embodiment described in the previous section. The polyelectrolyte complex can be present in the ingestible composition at any suitable concentration. For example, in some embodiments, the polyelectrolyte complex accounts for 10% to 99% by weight of the ingestible composition, or 20% to 95% by weight, or 30% to 95% by weight, based on the total dry weight of the ingestible composition.

[0060] The ingestible composition may contain other ingredients. These additional ingredients may be part of the ingestible composition.

[0061] Other Non-Animal Proteins

[0062] In certain embodiments, the ingestible composition comprises one or more other non-animal proteins in non-composite form. These other non-animal proteins include but are not limited to vegetable proteins, algae proteins, fungal proteins or combinations thereof. In some embodiments, other non-animal proteins are vegetable proteins. The non-limiting examples of such vegetable proteins include hemp plant proteins, almond proteins, cashew proteins, canola (rapeseed) proteins, chickpea proteins, wheat proteins, potato proteins, lupins, rice proteins, pea proteins, soy proteins, broad bean proteins, mung bean proteins, sunflower proteins, red lentil proteins, oat proteins or any combination thereof. These other non-animal proteins (when present) may account for any suitable proportion of the ingestible composition. For example, in some embodiments, based on the total dry weight of the ingestible composition, other non-animal proteins account for 1% to 50% by weight, or 1% to 40% by weight, or 1% to 30% by weight, or 1% to 20% by weight.

[0063] fiber

[0064] In some embodiments, the ingestible composition comprises one or more fibers. Such fibers are generally derived from plants and include soluble fibers and insoluble fibers.

[0065] As used herein, the term "soluble fiber" refers to a polysaccharide characterized as soluble by the official method of the Association of Official Analytical Chemists (AOAC) and described in Prosky et al., J. ASSOC. OFF. ANAL. CHEM., vol. 70 (5), pp. 1017-1023 (1988). Any suitable soluble fiber can be used, including but not limited to fruit fiber (e.g., citrus fiber), cereal fiber, psyllium husk fiber, natural soluble fiber, and synthetic soluble fiber. Natural fibers include soluble corn fiber, maltodextrin, gum arabic, and hydrolyzed guar gum. Synthetic soluble fibers include polydextrose, modified edible starch, and the like. Non-limiting examples of food-grade soluble fiber sources include inulin, corn fiber, barley fiber, corn germ, ground oat hulls, ground corn bran, a derivative of the wheat bran aleurone layer, flax meal, whole flax seed bran, winter barley flakes, ground oat groats, corn, pea fiber (e.g., Canadian yellow peas), Danish potatoes, konjac plant fiber (glucomannan), psyllium fiber from planago ovata seed husks, psyllium husks, liquid agave fiber, rice bran, oat sprout fiber, amaranth sprouts, lentil flour, grape seed fiber, apples, blueberries, cranberries, fig fiber, ciranda flour, carob flour, ground prune fiber, mango fiber, apple fiber, oranges, orange pulp, strawberries, carrageenan hydrocolloids, eucheuma , cottonnil, seaweed derivatives, cottonseed, soy, kiwi, acacia fiber, bamboo, chia seeds, potatoes, potato starch, pectin (carbohydrate) fiber, hydrolyzed guar gum, carrots, soy, edamame, chicory root, oats, wheat, tomatoes, polydextrose fiber, refined corn starch syrup, isomalto-oligosaccharide blend, soluble dextrin, citrus bioflavonoid blend, cracked nutritional yeast, lipophilic fiber, prune juice, larch derivatives, oligosaccharide fiber, cane sugar derivatives, short chain oligofructose, glucose synthetic polymers, polydextrose, pectin, polyanionic (polanion) compounds, cellulose fiber, cellulose fiber from hardwood plants, and carboxymethyl cellulose.

[0066] In some embodiments, the ingestible composition or protein additive composition may also include certain insoluble fibers, which may provide structure and texture to the ingestible composition. Any suitable insoluble fiber may be used. In some embodiments, the insoluble fiber is a plant-derived fiber. Non-limiting examples include nut fiber, cereal fiber, rice fiber, seed fiber, oat fiber, pea fiber, potato fiber, berry fiber, soy fiber, banana fiber, citrus fiber, apple fiber, and carrot fiber. In some embodiments, the insoluble fiber is pea fiber.

[0067] In some embodiments, the ingestible composition comprises pea fiber, citrus fiber, potato fiber, psyllium fiber, acacia fiber, inulin, konjac fiber, or any combination thereof.

[0068] Fiber can comprise any suitable proportion of the ingestible composition. For example, in some embodiments, based on the total dry weight of the ingestible composition, fiber comprises 1 wt % to 50 wt %, or 1 wt % to 40 wt %, or 1 wt % to 30 wt %, or 1 wt % to 20 wt %, or 3 wt % to 50 wt %, or 3 wt % to 40 wt %, or 3 wt % to 30 wt %, or 3 wt % to 20 wt %.

[0069] Flavorings, extracts, flavor and aroma modifiers

[0070] In some embodiments, the ingestible composition includes one or more flavorings, extracts, flavor modifiers, aroma modifiers, or any combination thereof.

[0071] Edible compositions disclosed herein include flavorings. Generally, flavorings can improve the mouthfeel and flavor of an ingestible composition or a flavored product obtained using the ingestible composition. Such improvements include reducing the bitterness of an ingestible composition or a flavored product obtained, reducing the astringency perception of an ingestible composition or a flavored product obtained, reducing the perception of the raw green taste tonality (e.g., pea flavor) of an ingestible composition or a flavored product obtained, reducing the perception of the grain tonality of an ingestible composition or a flavored product obtained, improving the creaminess of an ingestible composition or a flavored product obtained, improving the fatness of an ingestible composition or a flavored product obtained, improving the sweetness perception of an ingestible composition or a flavored product obtained, improving the savory (umami or rich taste) perception of an ingestible composition or a flavored product obtained, improving the mouthfeel or oral coating sense or perceived consistency of an ingestible composition or a flavored product obtained, improving the juiciness of an ingestible composition or a flavored product obtained, and improving the consistency perception of an ingestible composition or a flavored product obtained.

[0072] Any suitable flavoring agent can be used. In some embodiments, the flavoring agent comprises synthetic flavoring oils and flavoring aromatic substances or oils, oleoresins and extracts from plants, leaves, flowers, fruits, etc., and combinations thereof. Non-limiting examples of flavor oils include spearmint oil, cinnamon oil, sedge oil (methyl salicylate), peppermint oil, Japanese mint oil, clove oil, bay oil, anise oil, eucalyptus oil, thyme oil, cedar leaf oil, nutmeg oil, allspice, sage oil, mace, bitter almond oil, and cinnamon oil. Non-limiting examples of other flavors include natural and synthetic fruit flavors, such as vanilla, and citrus oils, including lemon, orange, lime, grapefruit, yazu, sudachi, and fruit essences, including apple, pear, peach, grape, blueberry, strawberry, raspberry, cherry, plum, pineapple, watermelon, apricot, banana, melon, apricot, plum, cherry, raspberry, blackberry, tropical fruits, mango, mangosteen, pomegranate, papaya, etc. Other potential flavors include milk flavors, butter flavors, cheese flavors, cream flavors, and yogurt flavors; vanilla flavors; tea or coffee flavors, such as green tea flavors, oolong tea flavors, tea flavors, cocoa flavors, chocolate flavors, and coffee flavors; mint flavors, such as peppermint flavors, spearmint flavors, and Japanese mint flavors; spice flavors, such as asafoetida flavors, ajwain flavors, anise flavors, angelica flavors, fennel flavors, allspice flavors, cinnamon flavors, chamomile flavors, mustard flavors, cardamom flavors, coriander flavors, cumin flavors, clove flavors, pepper flavors, cilantro flavors, sassafras flavors, and cumin flavors. Flavoring agent, salty flavoring agent, Sichuan pepper flavoring agent, basil flavoring agent, juniper berry flavoring agent, ginger flavoring agent, star anise flavoring agent, horseradish flavoring agent, thyme flavoring agent, tarragon flavoring agent, dill flavoring agent, vegetable pepper flavoring agent, nutmeg flavoring agent, basil flavoring agent, marjoram flavoring agent, rosemary flavoring agent, bay leaf flavoring agent and wasabi (Japanese horseradish) flavoring agent; Wine flavoring agent, such as red wine flavoring agent, whiskey flavoring agent, brandy flavoring agent, rum flavoring agent, gin flavoring agent and liqueur flavoring agent; Flower flavoring agent; And vegetable flavoring agent, such as onion flavoring agent, garlic flavoring agent, cabbage flavoring agent, carrot flavoring agent, celery flavoring agent, mushroom flavoring agent and tomato flavoring agent. These flavoring agents can be used in liquid or solid form, and can be used alone or in combination. In dairy or dairy analog products, the most commonly used flavoring agents are agents that impart flavors such as vanilla, French vanilla, chocolate, banana, lemon, hazelnut, coconut, almond, strawberry, mocha, coffee, tea, chai, cinnamon, caramel, cream, brown sugar, toffee, pecan, butter pecan, toffee, Irish cream, white chocolate, raspberry, pumpkin pie spice, spearmint or any combination thereof.

[0073] In some embodiments, the flavoring agent is a flavoring agent that provides a meaty or savory note, including flavorings or notes of beef, lamb, bison, smoked, pork, bacon, ham, sausage, chicken, turkey, goose, duck, mushroom, celery, tomato, onion, garlic, carrot, leek, fish, shellfish, soy, miso, etc. In some further embodiments, the flavoring agent comprises one or more lactones that impart a creamy flavor to the ingestible composition.

[0074] In some embodiments, the flavoring comprises a yeast extract, such as a yeast lysate. Such an extract can be obtained from any suitable yeast strain, wherein such an extract is suitable for human consumption. Non-limiting examples of such yeasts include: yeasts of the genus Saccharomyces, such as Saccharomyces cerevisiae or Saccharomyces pastorianus; yeasts of the genus Candida, such as Candida utilis; yeasts of the genus Kluyveromyces, such as Kluyveromyces lactis or Kluyveromyces marxianus; yeasts of the genus Pichia, such as Pichia pastoris; yeasts of the genus Debaryomyces, such as Debaryomyces hansenii; and yeasts of the genus Zygosaccharomyces, such as Zygosaccharomyces mellis. In some embodiments, the yeast is yeast collected after brewing beer, sake, etc. In some embodiments, the yeast is yeast that is dried after collection (dried yeast).

[0075] Such extracts can be produced by any suitable means. In general, yeast extracts or lysates are prepared by extracting the contents of yeast cells from cell wall materials. In many cases, the digestive enzymes in the cells (or other enzymes added to the composition) decompose the proteins and polynucleotides in the yeast into amino acids, oligopeptides (e.g., 2 to 10 peptides), nucleotides, oligonucleotides (2 to 10 nucleotides) and mixtures thereof. Yeast lysates can be prepared by cracking yeast. For example, in some embodiments, the cultured yeast is crushed or cracked by enzymolysis, self-digestion, alkali extraction, hot water extraction, acid decomposition, ultrasonic crushing, homogenizer crushing, freezing and thawing, etc. (two or more of which can be used in combination), thereby obtaining yeast lysates. Yeast can be cultured according to conventional methods. In some embodiments, the cultured yeast is heat treated and then treated with a lysing enzyme to obtain an enzyme lysate. The conditions of the heat treatment are, for example, 80°C to 90°C for 5 to 30 minutes. As a lysing enzyme for enzymolysis, various enzymes can be used as long as the cell wall of the yeast can be cracked. The reaction conditions can be set to be optimal or suitable for the lytic enzyme used, and specific examples thereof may include a temperature of 50 to 60° C. and a pH of 7.0 to 8.0. The reaction time is also not particularly limited, and may be, for example, 3 to 5 hours.

[0076] Compositions comprising yeast lysate can be obtained from a variety of commercial sources. For example, in some embodiments, yeast lysate is provided by a flavoring additive sold under the name MODUMAX (DSM Food Specialties BV, Delft, The Netherlands).

[0077] In certain embodiments, the flavoring agent further comprises one or more additional flavor-modifying compounds, such as compounds that enhance sweetness (e.g., phloretin, naringenin, glucosylated steviol glycosides, etc.), compounds that block bitterness, compounds that enhance umami, compounds that enhance kokumi, compounds that reduce sour or licorice taste, compounds that enhance saltiness, compounds that enhance cooling effects, compounds that enhance mouthfeel, or any combination of the foregoing.

[0078] In some embodiments, the ingestible composition includes a sweetener. The sweetener can be present in any suitable concentration, depending on factors such as the potency of the sweetener as a sweetener, its solubility, and the like.

[0079] In general, the ingestible composition disclosed herein may include any suitable sweetener or a combination of multiple sweeteners. In some embodiments, the sweetener is a common sugar sweetener, such as sucrose, fructose, glucose, and a sweetener composition comprising natural sugars such as corn syrup (including high fructose corn syrup) or other syrups or sweetener concentrates derived from natural fruit and vegetable sources. In some embodiments, the sweetener is sucrose, fructose or a combination thereof. In some embodiments, the sweetener is sucrose. In some other embodiments, the sweetener is selected from rare natural sugars, including D-allose, D-psicose, L-ribose, D-tagatose, L-glucose, L-fucose, L-arabinose, D-turanose and D-white bacteria disaccharide. In some embodiments, the sweetener is selected from semi-synthetic "sugar alcohol" sweeteners, such as erythritol, isomalt, lactitol, mannitol, sorbitol, xylitol, maltodextrin etc. In some embodiments, the sweetener is selected from artificial sweeteners, such as aspartame, saccharin, acesulfame potassium, cyclamates, sucralose and alitame. In some embodiments, the sweetener is selected from the group consisting of cyclamic acid, mogroside, tagatose, maltose, galactose, mannose, sucrose, fructose, lactose, allulose, neotame and other aspartame derivatives, glucose, D-tryptophan, glycine, maltitol, lactitol, isomalt, hydrogenated glucose syrup (HGS), hydrogenated starch hydrolysate (HSH), stevioside, rebaudioside A, other sweet steviosides, chemically modified steviol glycosides (such as glucosylated steviol glycosides), other mogrosides, chemically modified mogrosides (such as glucosylated mogrosides), guanidine sweeteners (carrelame) and other guanidine sweeteners. In some embodiments, sweetener is a combination of two or more sweeteners set forth in this paragraph. In some embodiments, sweetener can be a combination of two, three, four or five sweeteners disclosed herein. In some embodiments, sweetener can be sugar. In some embodiments, sweetener can be a combination of one or more sugars and other natural and artificial sweeteners. In some embodiments, sweetener is sugar. In some embodiments, sugar is cane sugar. In some embodiments, sugar is beet sugar. In some embodiments, sugar can be sucrose, fructose, glucose or a combination thereof. In some embodiments, sugar can be sucrose. In some embodiments, sugar can be a combination of fructose and glucose.

[0080] In some embodiments, sweeteners may also include, for example, sweetener compositions comprising one or more natural or synthetic carbohydrates, such as corn syrup, high fructose corn syrup, high maltose corn syrup, glucose syrup, sucralose syrup, hydrogenated glucose syrup (HGS), hydrogenated starch hydrolysate (HSH), or other syrups or sweetener concentrates from natural fruit and vegetable sources, or semi-synthetic "sugar alcohol" sweeteners, such as polyols. In some embodiments, non-limiting examples of polyols include erythritol, maltitol, mannitol, sorbitol, lactitol, xylitol, isomalt, propylene glycol, glycerol (glycerine), threitol, galactitol, palatinose, reduced isomaltooligosaccharides, reduced xylo-oligosaccharides, reduced gentio-oligosaccharides, reduced maltose syrup, reduced glucose syrup, isomaltulose, maltodextrin, etc., as well as sugar alcohols or any other carbohydrates or combinations thereof that can be reduced without adversely affecting the taste.

[0081] The sweetener may be a natural or synthetic sweetener, including, but not limited to, agave inulin, agave nectar, agave syrup, amazake, brazzein, brown rice syrup, coconut crystals, coconut sugar, coconut syrup, date sugar, fructans (also known as inulin fiber, fructooligosaccharides or oligofructose), green stevia powder, stevia rebaudiana, rebaudioside A, rebaudioside B, rebaudioside C, rebaudioside D, rebaudioside E, rebaudioside F, rebaudioside I, rebaudioside H, rebaudioside L, rebaudioside K, rebaudioside J, rebaudioside N, rebaudioside O, rebaudioside M and other steviol-based glycosides, stevioside, stevioside extract, honey, Jerusalem artichoke, artichoke syrup, licorice root, monk fruit (fruit, powder or extract), lucuma (fruit, powder or extract), maple sap (including, for example, sap extracted from sugar maple (Acer saccharum), black maple (Acer nigrum), American red maple (Acer rubrum), silver maple (Acersaccharinum), Norway maple (Acer platanoides), ash maple (Acer negundo), bigleaf maple (Acer macrophyllum), roughtooth maple (Acer grandidentatum), Rocky Mountain maple (Acer glabrum), monochromatic maple (Acer mono), maple syrup, maple sugar, walnut sap (including, for example, sap extracted from white walnut (Juglans cinerea), black walnut (Juglans nigra), ghost walnut (Juglans ailatifolia), walnut (Juglans regia), birch sap (including, for example, sap extracted from paper birch (Betula papyrifera, yellow birch (Betula alleghaniensis), mountain birch (Betula lenta), river birch (Betula nigra), gray birch (Betula populifolia), weeping birch (Betula pendula), sycamore sap (e.g., sap extracted from Platanus occidentalis), ironwood sap (e.g., sap extracted from Ostrya virginiana), unrefined cane sugar (mascobado), molasses (e.g., blackstrap molasses), molasses sugar, monatin, monellin, cane sugar (e.g.,sugar (also known as natural sugar, unrefined sucrose or table sugar), palm sugar, panocha, piloncillo, rapadura, raw sugar, rice syrup, sorghum, sorghum syrup, tapioca syrup (also known as tapioca syrup), thaumatin, yacon root), maltose syrup, barley malt syrup, barley malt powder, beet sugar, cane sugar, crystallized fruit juice crystals, caramel, carbitol, carob syrup, castor sugar, hydrogenated starch hydrolates, hydrolyzed canned fruit juice, hydrolyzed starch, invert sugar, anethole, arabinogalactan, concentrated grape juice (arrope), syrup, P-4000, acesulfame potassium (also known as acesulfame potassium or ace-K), alitame (also known as aclame), advantame, aspartame, baiyunosdie, neotame, benzamide derivatives, bernadame, canderel, guanidine sweeteners (carrelame) and other guanidine sweeteners, vegetable fiber, corn sugar, coupling sugar, curculin, cyclamates, cyclocaryoside I ( I), demerara, dextran, dextrin, diastatic maltmalt), dulcin, sucrol, valzin, dulcoside A, dulcoside B, emulin, enoxolone, maltodextrin, saccharin, estragole, ethyl maltol, glucin, gluconic acid, gluconic acid lactone, glucosamine, glucuronic acid, glycerol, glycine, glycyphillin, glycyrrhizin, glycyrrhetinic acid monoglucuronide, golden sugar, brown sugar, golden syrup, granulated sugar, gynostemma pentaphyllum, hernandulcin, isomerized liquid sugar, jallab, chicory root dietary fiber, kynurenine derivatives (including N'-formyl-kynurenine, N'-acetyl-kynurenine, amino acid, 6-chloro-kynurenine), galactitol, litesse, ligicane, lycasin, lugduname, guanidine, falernum, mabinin I, mabinin II, maltol, maltisorb, maltodextrin, maltotriol, mannosamine, micraculin, mizuame, mogrosides (including, for example, mogroside IV, mogroside V and neomogroside), mukurozioside, nanosaccharides, sugar), naringin dihydrochalcone, neohesperidin dihydrochalcone, nib sugar, nib oligosaccharide, norbu, almond syrup, osladin, pekmez, pentadin, periandrin I, perillaldehyde, perillartine, petphyllum, phenylalanine, phloisosideside I, phloretin, phlorodizin, phyllodulcin, polyglycitol syrup, polypodoside A, pterocaryoside A, pterocaryoside B, rebiana, refined syrup, rub syrup, rubusoside, selligueain A), shugr, simenoside I, siraitia grosvenorii, soy oligosaccharides, Splenda, SRIoximeV, steviol glycosides, steviol biosides, stevioside, strogins 1, 2 and 4, sucrose, sucrononate, sugar, sodium p-nitrophenylureidopropionate (suosan), phloridzin, super aspartame, tetrasaccharide, threitol, treacle, trilobtain, tryptophan and derivatives (6-trifluoromethyl-tryptophan, 6-chloro-D-tryptophan), vanilla sugar, heptyl heptol, birch syrup, aspartame-acesulfame, assugrin, and combinations or blends of any two or more thereof.

[0082] In other embodiments, the sweetener can be a chemically or enzymatically modified natural high-potency sweetener. Modified natural high-potency sweeteners include glycosylated natural high-potency sweeteners, such as glucosyl, galactosyl or fructosyl derivatives containing 1 to 50 glycoside residues. Glycosylated natural high-potency sweeteners can be prepared by enzymatic transglycosylation reactions catalyzed by various enzymes with transglycosylation activity. In some embodiments, the modified sweetener can be substituted or unsubstituted.

[0083] In some embodiments, the flavoring agent comprises one or more sweetness enhancing compounds. Such sweetness enhancing compounds include, but are not limited to, naturally derived compounds such as hesperidin dihydrochalcone, hesperidin dihydrochalcone-4'-O'glucoside, neohesperidin dihydrochalcone, brazein, hesperidin, chlorophyll, naringenin, naringin, phloretin, glucosylated steviol glycosides, (2R, 3R)-3-acetoxy-5,7,4'-trihydroxyflavanone, (2R, 3R)-3-acetoxy-5,7,3 '-trihydroxy-4'-methoxyflavanone, sweet leaf rubusoside, eriodictyol, homoeriodictyol or synthetic compounds, such as U.S. Patent Nos. 8,541,421, 8,815,956, 9,834,544, 8,592,592, 8,877,922, 9,000,054, and 9,000,051, and compounds described in U.S. Patent Application Publication No. 2017 / 0119032. As used herein, the term "glucosylated steviol glycoside" refers to the product of enzymatic glucosylation of natural steviol glycoside compounds. Glucosylation usually occurs through glycosidic bonds, such as α-1,2 bonds, α-1,4 bonds, α-1.6 bonds, β-1,2 bonds, β-1,4 bonds, β-1,6 bonds, etc. In some embodiments of any of the preceding embodiments, the edible composition comprises 3-((4-amino-2,2-dioxo-1H-benzo[c][1,2,6]thiadiazin-5-yl)oxy)-2,2-dimethyl-N-propyl-propionamide or N-(1-((4-amino-2,2-dioxo-1H-benzo[c][1,2,6]thiadiazin-5-yl)oxy)-2-methyl-propan-2-yl)-isonicotinamide.

[0084] In some further embodiments, the flavoring agent comprises one or more umami enhancing compounds. Such umami enhancing compounds include but are not limited to naturally derived compounds or synthetic compounds, such as any compound described in U.S. Patent Nos. 8,735,081, 8,124,121 and 8,968,708. In some embodiments, the umami enhancing compound is (2R, 4R) -1,2,4- trihydroxy - 17 carbon -16-ene, (2R, 4R) -1,2,4- trihydroxy - 17 carbon -16- yne, or a mixture thereof. In some embodiments, the umami enhancing compound is (3R, 5S) -1- (4-hydroxy -3- methoxyphenyl) decane -3,5- diol diacetate. In some embodiments, the umami enhancing compound is N- (heptane -4- base) benzo - [d] [1,3] dioxole -5- carboxamide.

[0085] In some embodiments, the ingestible composition comprises one or more compounds commonly used in savory products. Such flavoring agents include glutamate (e.g., MSG), arginine, avocadoene, aguacin, purine ribonucleotides (e.g., inosine monophosphate (IMP), guanosine monophosphate (GMP), hypoxanthine, inosine), yeast extract (as described above), fermented food products, cheese, garlic or its extract, γ-glutamyl-containing polypeptides, γ-glutamyl-containing oligopeptides (e.g., γ-glutamyl-containing tripeptides); flavor modification compositions (e.g., cinnamic acid amide or derivatives thereof), nucleotides, oligonucleotides, plant extracts, food extracts, or any combination thereof.

[0086] In some further embodiments, the flavoring agent comprises one or more cooling enhancing compounds. Such cooling enhancing compounds include, but are not limited to, naturally derived compounds, such as menthol or its analogs, or synthetic compounds, such as any of the compounds described in U.S. Pat. Nos. 9,394,287 and 10,421,727.

[0087] In some further embodiments, the flavoring agent comprises one or more bitter blocking compounds. Such bitter blocking compounds include, but are not limited to, naturally derived compounds, such as menthol or its analogs, or synthetic compounds, such as any compound described in U.S. Patent Nos. 8,076,491, 8,445,692, and 9,247,759 or PCT Publication No. WO 2020 / 033669. In some embodiments, the bitter blocking compound is 3-(1-((3,5-dimethylisoxazol-4-yl)-methyl)-1H-pyrazol-4-yl)-1-(3-hydroxybenzyl)-imidazoline-2,4-dione.

[0088] In some further embodiments, the flavoring agent comprises one or more sour taste adjusting compounds.

[0089] In some further embodiments, the flavoring agent comprises one or more mouthfeel-modifying or mouthfeel-enhancing compounds including, but not limited to, polymethoxylated flavones, tannins, cellulosic materials, bamboo powder, and the like.

[0090] In some further embodiments, the flavoring agent comprises one or more flavor masking compounds. Such flavor masking compounds include, but are not limited to, cellulosic materials, materials extracted from fungi, materials extracted from plants, citric acid, carbonic acid (or carbonates), and the like.

[0091] In some embodiments, the above-described flavor-modifying compounds are included to improve other tastants that may be present in the edible composition itself or that may be included in a flavored product employing such a composition. Such tastants include sweeteners, umami tastants, kokumi tastants, bitter tastants, sour tastants, and the like.

[0092] In some embodiments, the ingestible comprises one or more metal salts or metal complexes, such as iron salts or iron complexes. Such compounds may include any edible metal salt or complex, such as salts or complexes of calcium, magnesium, sodium, potassium, iron, cobalt, copper, zinc, manganese, molybdenum, and selenium. In some embodiments, the iron compound is an iron salt or an iron complex. In some specific embodiments, the metal compound is ferrous (Fe 2+ ) salt or ferrous iron (Fe 2+ ) complex. In some embodiments, the metal compound is ferrous (Fe 2+ ) salts, such as ferrous sulfate, ferrous lactate, ferrous fumarate, ferrous gluconate, ferrous succinate, ferrous chloride, ferrous oxalate, ferrous nitrate, ferrous citrate, ferrous ascorbate, ferric citrate, ferric phosphate, or any combination thereof. In some other embodiments, the metal compound is iron (Fe 3+ ) salt or iron (Fe 3+ ) complex, such as ferric pyrophosphate. In some embodiments, the iron compound is ferrous lactate, ferrous sulfate, or any combination thereof.

[0093] In some embodiments, the iron compound is a heme-containing protein. As used herein, the term "heme-containing protein" includes any polypeptide covalently or non-covalently bound to a heme moiety. In some embodiments, the heme-containing polypeptide is a globin, and may include a globin fold, which contains a series of seven to nine alpha helices. Globin-type proteins can be of any class (e.g., class I, class II, or class III), and in some embodiments, can transport or store oxygen. For example, a heme-containing protein can be a non-symbiotic type of hemoglobin or leghemoglobin. A heme-containing polypeptide can be a monomer, such as a single polypeptide chain, or can be a dimer, trimer, tetramer, and / or higher oligomer. Oxidized Fe of heme-containing proteins 2+ The lifetime of the state can be similar to that of myoglobin, or can exceed the lifetime of myoglobin by 10%, or 20%, or 30%, or 40%, or 50%, or even 100% or more under the conditions of manufacturing, storing, processing or preparing a consumable product of a heme-containing protein for consumption.

[0094] Non-limiting examples of heme-containing proteins include androglobin, cytoglobin, globin E, globin X, globin Y, hemoglobin, myoglobin, erythroglobin, β-hemoglobin, α-hemoglobin, protoglobin, cyanoglobin, cytoglobin, histoglobin, neuroglobin, chlorocruorin, truncated hemoglobin (e.g., HbN or HbO), truncated 2 / 2 globin, hemoglobin 3 (e.g., Glb3), cytochrome, or peroxidase.

[0095] Heme-containing proteins can be used in the edible compositions described herein and can be from mammals (e.g., farm animals such as cattle, goats, sheep, pigs, cattle, or rabbits), birds, plants, algae, fungi (e.g., yeast or filamentous fungi), ciliates, or bacteria. For example, heme-containing proteins can be from mammals, such as farm animals (e.g., cattle, goats, sheep, pigs, fish, cattle, or rabbits), or birds, such as turkeys or chickens. The heme-containing protein may be derived from a plant such as Nicotiana tabacum or Nicotiana sylvestris (nicotiana); corn (Zea mays), Arabidopsis thaliana, legumes such as soybeans (Glycine max), chickpeas (Cicerarietinum) (chickpeas or chickpeas), pea (Pisum sativum) varieties such as garden peas or sugar snap peas, common legumes (Phaseolus vulgaris) varieties such as green beans, black beans, navy beans, northern beans or pinto beans, cowpea (Vigna unguiculata) varieties, mung beans (Vigna radiata), lupinus (Lupinus albus) or alfalfa (Medicago sativa); Brassica napus (canola); Triticum spp. sps) (wheat, including wheat berries and spelt); Gossypium hirsutum (cotton); Oryza sativa (rice); Zizania sps. (wild rice); Helianthus annuus (sunflower); Betavulgaris (sugar beet); Pennisetum glaucum (pearl millet); Chenopodium sp.; Sesamum sp.; Linum usitatissimum (flax); or Hordeum vulgare (barley).Heme-containing proteins can be isolated from fungi, such as Saccharomyces cerevisiae, Pichia pastoris, Magnaporthe oryzae, Fusarium graminearum, Aspergillus oryzae, Trichoderma reesei, Myceliopthera thermophile, Kluyveramyces lactis, or Fusarium oxysporum. Heme-containing proteins can be isolated from Escherichia coli, Bacillus subtilis, Bacillus licheniformis, Bacillus megaterium, Synechocistis sp., Aquifex aeolicus, Methylacidiphiluminfernorum, or thermophilic bacteria, such as Thermophilus spp. The sequences and structures of many heme-containing proteins are known. See, for example, Reedy et al., Nucleic Acids Research, 2008, Vol. 36, Database issue D307-D313 and the heme protein database available on the Internet at http: / / hemeprotein.info / heme.php.

[0096] In some embodiments, the non-symbiotic hemoglobin can be from any plant. In some embodiments, the non-symbiotic hemoglobin can be from a plant selected from the group consisting of soybean, sprouted soybean, alfalfa, golden flax, black bean, black-eyed pea, northern bean, tobacco, pea, chickpea, mung bean, cowpea, pinto bean, pea pod, quinoa, sesame, sunflower, wheat kernel, spelt, barley, wild rice and rice.

[0097] In some embodiments, the heme-containing protein is leghemoglobin, such as soy, pea, or cowpea leghemoglobin.

[0098] Heme-containing proteins or other proteins can also be recombinantly produced using polypeptide expression techniques (e.g., heterologous expression techniques using bacterial cells, insect cells, fungal cells (such as yeast), plant cells (such as tobacco, soybean or Arabidopsis), or mammalian cells). For example, leghemoglobin can be recombinantly produced in Escherichia coli or Pichia pastoris. In some cases, heme-containing proteins can be synthetically produced using standard polypeptide synthesis techniques (such as liquid phase polypeptide synthesis techniques or solid phase polypeptide synthesis techniques). In some cases, heme-containing proteins can be produced using in vitro transcription-translation techniques.

[0099] The heme-containing protein or iron salt can be used at any suitable concentration. Examples are listed in PCT Publication No. WO2015 / 153666, which is incorporated herein by reference.

[0100] The iron compound may comprise any suitable weight of the ingestible particle. In some embodiments, the iron compound comprises 0.1 wt % to 10 wt %, or 0.2 wt % to 5 wt %, or 0.5 wt % to 3 wt % of the ingestible composition, based on the total dry weight of the ingestible composition.

[0101] Other additives

[0102] In some embodiments, the ingestible composition includes various other additives, such as emulsifiers, bulking agents, thickening agents, and the like.

[0103] For example, in some embodiments, the ingestible composition includes an emulsifier. Any suitable emulsifier can be used. For example, in some non-limiting embodiments, the emulsifier includes lecithin, monoglyceride, diglyceride, polysorbate, vegetable oil, etc. In some embodiments, the emulsifier includes lecithin. The example of emulsifier can be found in McCutcheon's Emulsifiers & Detergents or Industrial Surfactants Handbook. The emulsifier can be present in any suitable concentration, such as when incorporated into a flavored product, the concentration can be adjusted to form a stable emulsion of other components in the edible composition.

[0104] In some cases, it may be necessary to include additives that help adjust the viscosity of the ingestible composition (for example, when the ingestible composition is introduced into water or includes water). Various salts and acids can be used to perform such adjustments. In some embodiments, the edible composition or the resulting flavored product comprises one or more salts. Non-limiting examples of suitable salts include magnesium sulfate, sodium chloride, sodium sulfate, calcium chloride, calcium sulfate, potassium sulfate, potassium chloride, potassium sorbate, potassium phosphate, potassium monophosphate, zinc chloride, zinc sulfate, or any mixture thereof. In some embodiments, the edible composition or the resulting flavored product also comprises one or more acids, which can be used alone or in combination with the aforementioned salts. Non-limiting examples of suitable acids include citric acid, lactic acid, acetic acid, tartaric acid, succinic acid, ascorbic acid, maleic acid, phosphoric acid, potassium dihydrogen phosphate, gluconic acid, gluconolactone, glucuronic acid, glycyrrhetinic acid, folic acid, pantothenic acid, or a mixture thereof.

[0105] In certain embodiments, the ingestible compositions may include any additional ingredients or combinations of ingredients commonly used in food and beverage products, including, but not limited to:

[0106] Acids, including, for example, citric acid, phosphoric acid, ascorbic acid, sodium bisulfate, lactic acid, or tartaric acid;

[0107] bitter ingredients, including, for example, caffeine, quinine, green tea, catechins, polyphenols, robusta green coffee bean extract, green coffee bean extract, potassium chloride, menthol, or proteins (e.g., proteins and protein isolates from plants, algae, or fungi);

[0108] Coloring agents, including, for example, caramel, red #40, yellow #5, yellow #6, blue #1, red #3, purple carrot, black carrot juice, purple sweet potato, vegetable juice, fruit juice, beta-carotene, turmeric curcumin, or titanium dioxide;

[0109] preservatives, including, for example, sodium benzoate, potassium benzoate, potassium sorbate, sodium metabisulfite, sorbic acid, or benzoic acid;

[0110] Antioxidants including, for example, ascorbic acid, calcium disodium EDTA, alpha-tocopherol, mixed tocopherols, rosemary extract, grape seed extract, resveratrol, or sodium hexametaphosphate;

[0111] Vitamins or functional ingredients, including, for example, resveratrol, Co-Q10, omega 3 fatty acids, theanine, choline chloride (Citcoline), inositol, inulin (chicory root), taurine, ginseng extract, guarana extract, ginger extract, L-phenylalanine, L-carnitine, L-tartrate, D-glucuronolactone, inositol, bioflavonoids, echinacea, Ginkgo Biloba, yerba mate, flaxseed oil, Garcinia cambogia peel extract, white tea extract, ribose, milk thistle, thistle extract, grape seed extract, pyridoxine hydrochloride (vitamin B6), cyanocobalamin (vitamin B12), niacinamide (vitamin B3), biotin, calcium lactate, calcium pantothenate (pantothenic acid), calcium phosphate, calcium carbonate, chromium chloride, chromium polynicotinate, cupric sulfate, folic acid, ferric pyrophosphate, iron, magnesium lactate, magnesium carbonate, magnesium sulfate, monopotassium phosphate, monosodium phosphate, phosphorus, potassium iodide, potassium phosphate, riboflavin, sodium sulfate, sodium gluconate, sodium polyphosphate, sodium bicarbonate, thiamine mononitrate, vitamin D3, vitamin A palmitate, zinc gluconate, zinc lactate, or zinc sulfate;

[0112] Clouding agents, including, for example, ester gums, brominated vegetable oil (BVO), or sucrose acetate isobutyrate (SAIB);

[0113] buffers, including, for example, sodium citrate, potassium citrate, or saline;

[0114] Propylene glycol, ethanol, glycerin, gum arabic (acacia), modified corn starch, silicon dioxide, magnesium carbonate, or tricalcium phosphate; or

[0115] Starch and stabilizers, including, for example, polysorbate 60, polysorbate 80, medium chain triglycerides, and the like.

[0116] In some embodiments, component (a) may further include galacto-oligosaccharides, fructo-oligosaccharides, gum arabic fiber, soluble pea fiber, soluble wheat fiber, arabinoxylan, isomaltooligosaccharides, xylo-oligosaccharides, and the like.

[0117] The edible composition may contain a variety of ingredients, such as those typically included in meat analog products.

[0118] For example, in some embodiments, the edible composition comprises a flavored water-in-oil emulsion according to any embodiment described in PCT Publication No. WO 2020 / 260628, which is incorporated herein by reference.

[0119] In some embodiments, the edible composition comprises an encapsulated flavor composition according to any embodiment described in PCT Publication No. WO 2021 / 104846, which is incorporated herein by reference.

[0120] In some embodiments, the ingestible composition further comprises a carrier and optionally at least one adjuvant. The term "carrier" refers to a generally inactive auxiliary substance, such as a solvent, a binder, an extender, or other inert medium, which is used in combination with the compounds of the present invention and one or more optional adjuvants to form a formulation. For example, water or starch can be a carrier of a flavored product. In some embodiments, the carrier is the same as the dilution medium used to reconstitute the flavored product; while in other embodiments, the carrier is different from the dilution medium. As used herein, the term "carrier" includes, but is not limited to, edible acceptable carriers.

[0121] The term "adjuvant" means an additive that supplements, stabilizes, maintains or enhances the expected function or efficacy of an active ingredient such as the compounds of the present invention. In one embodiment, at least one adjuvant comprises one or more flavoring agents. Flavoring agents can have any flavor known to those skilled in the art or consumers, such as chocolate, coffee, tea, mocha, French vanilla, peanut butter, Indian milk tea, or the flavor of a combination thereof. In another embodiment, at least one adjuvant comprises one or more sweeteners. One or more sweeteners can be any sweetener described in the present application. In another embodiment, the at least one adjuvant comprises one or more ingredients selected from the group consisting of: emulsifiers, stabilizers, antimicrobial preservatives, antioxidants, vitamins, minerals, fats, starches, protein concentrates and isolates, salts, and combinations thereof. Examples of emulsifiers, stabilizers, antimicrobial preservatives, antioxidants, vitamins, minerals, fats, starches, protein concentrates and isolates and salts are described in U.S. Patent No. 6,468,576, the entire contents of which are incorporated herein by reference for all purposes.

[0122] The ingestible composition may further comprise a freezing point depression agent, a nucleating agent or both as the at least one adjuvant. A freezing point depression agent is an acceptable compound or agent for ingestion, which can reduce the freezing point of a liquid or solvent to which the compound or agent is added. That is, the freezing point of a liquid or solution containing a freezing point depression agent is lower than the freezing point of a liquid or solvent without a freezing point depression agent. In addition to reducing the initial freezing point, a freezing point depression agent can also reduce the water activity of a flavored product. Examples of freezing point depression agents include, but are not limited to, carbohydrates, oils, ethanol, polyols such as glycerol, and combinations thereof. A nucleating agent represents an acceptable compound or agent for ingestion that can promote nucleation. The presence of a nucleating agent in a flavored product can improve the mouthfeel of slush, and helps maintain the physical properties and performance of slush at freezing temperatures by increasing the number of required ice crystal centers. Examples of nucleating agents include, but are not limited to, calcium silicate, calcium carbonate, titanium dioxide, and combinations thereof.

[0123] In some embodiments, the ingestible composition is formulated to have a low water activity to extend shelf life. Water activity is the ratio of the vapor pressure of water in the formulation to the vapor pressure of pure water at the same temperature. In one embodiment, the water activity of the ingestible composition is less than about 0.85. In another embodiment, the water activity of the ingestible composition is less than about 0.80. In another embodiment, the water activity of the ingestible composition is less than about 0.75.

[0124] Preparation method

[0125] Ingestible compositions disclosed herein can be made by any suitable method, such as methods commonly used to make products containing fiber blends. Such methods include dry mixing, granulation, encapsulation, spray drying, etc. In some embodiments, the ingestible composition is prepared by spray drying, wherein the protein composition is mixed with a liquid medium, and the liquid medium is removed by drying in the spray process. Spray drying processes are well known in the field of preparing edible products. Any suitable spray drying process can be used, and the components used in the ingestible composition are optimized. In some embodiments, the ingestible composition is prepared by extrusion, wherein the protein composition is mixed with other materials and formed into shaped articles by extrusion. Extrusion processes are well known in the field of preparing edible products. Any suitable extrusion process or equipment can be used, and the components used in the ingestible composition are optimized.

[0126] Flavored products

[0127] In certain forms, the present disclosure provides a flavored product comprising an ingestible composition according to any of the above embodiments. In some embodiments, the flavored product is a food product, such as a meat analog product, such as a non-animal ground beef replica. In some other embodiments, the flavored product is an animal feed product, such as pet food. In such flavored products, in some embodiments, the edible composition can be used in combination with an animal product to reduce the level of animal fat or animal products in the edible product. In other embodiments, the flavored product does not contain an animal product, so the edible composition is used to make an analog or replica of a meat product, such as ground beef patties.

[0128] In some other embodiments, the flavored product is a meat substitute product (or meat analog), such as a product designed to imitate a product traditionally made from red meat. For example, the flavored product can be a meat analog dough, such as the dough described in PCT Publication No. WO 2015 / 153666. Such a flavored product can be designed to simulate a beef product, such as ground beef (for making burgers) or beef cuts for adding to soups, prepared meals, etc. The flavored product can also be designed to simulate other meats, such as chicken, turkey, pork, goat, lamb, venison, and bison, or seafood, such as fish or shellfish (crab, scallops, shrimp, squid, etc.) in cut or chopped form.

[0129] Example

[0130] To further illustrate the present invention, the following examples are included. Of course, these examples should not be construed as specifically limiting the present invention. Variations of these embodiments within the scope of the claims are within the capabilities of those skilled in the art and are considered to fall within the scope of the present invention as described and claimed herein. The reader will recognize that a skilled artisan and a person skilled in the art having grasped this disclosure will be able to prepare and use the present invention without exhaustive examples.

[0131] Example 1 - Pea protein and pectin complex

[0132] Pea protein isolate was added to demineralized water at a concentration of 5% (w / w) to a soluble protein content of 1.28% (w / w) and a pH of 3.5 in the supernatant. The composition was hydrated for 2 hours under stirring at 400 rpm. Low methoxyl (LM) pectin was added to demineralized water at a concentration of 0.5% (w / w) and stirred at 400 rpm for 2 hours. After hydration for 2 hours, the protein solution was adjusted to a pH of 3.5 with anhydrous citric acid and kept balanced for 30 minutes. The entire solution was transferred to a centrifuge tube and centrifuged at 4000 rpm for 15 minutes. The supernatant was removed and set aside to form a precipitate. The pectin solution was adjusted to a pH of 3.5 with 0.1M HCl and allowed to stand for 30 minutes to balance.

[0133] The precipitate was formed at a pH of 3.5, a weight ratio of 2.6:1 (vegetable protein / pectin) and a total biopolymer concentration of 0.37 wt% (0.27 wt% pea protein and 0.1 wt% LM pectin). At this ratio, the precipitate Zeta potential was measured to be -6.5 mV. Figure 1 The precipitate formation at 30 minutes, 1 hour and 3 hours is shown, measured in units of 30 μm. The maximum particle size of the precipitate measured was approximately 30 μm.

[0134] The precipitate was recovered and subjected to sensory evaluation for its off-flavor masking potential. Five panelists tested the precipitate in solution and compared it to a reference sample of 0.27% (w / w) pea protein solution in demineralized water adjusted to pH 3.5 with anhydrous citric acid. The sensory panelists noted that the intensity of off-flavor descriptors such as nutty, cereal and beany was less pronounced in the precipitate.

[0135] Example 2 - Pea protein and gum arabic

[0136] The pea protein / gum arabic precipitate was formed at pH 3.5 and a weight ratio of 3.6:1. The total biopolymer concentration was 1.15 wt% (0.9 wt% pea protein isolate / 0.25 wt% gum arabic). The pea protein composition was formed in the same manner as described in Example 1. The gum arabic matrix composition contained 2.25 wt% gum arabic in demineralized water. The pH was adjusted to pH 3.5 using 0.1 M HCl. The pea protein composition and the gum arabic composition were mixed in the above proportions and then stirred for 2 hours.

[0137] Figure 2 Precipitate formation at 30 minutes, 1 hour and 3 hours is shown, measured in 30 μm units.

[0138] The precipitate was recovered and subjected to sensory evaluation for its off-flavor masking potential. Five panelists tested the precipitate in solution and compared it to a reference sample of 0.9% (w / w) pea protein solution in demineralized water adjusted to pH 3.5 with anhydrous citric acid. The sensory panelists noted that the intensity of off-flavor descriptors such as astringency and sourness exhibited by the precipitate was less pronounced.

[0139] Example 3 - Pea protein and carrageenan

[0140] A pea protein / carrageenan precipitate was prepared using a similar method as in Examples 1 and 2. A 5% (w / w) pea protein isolate was adjusted to pH 3 with HCl, and a 1% (w / w) carrageenan (SATIAGUM, Cargill, Wayzata, MN) solution was adjusted to pH 3 with HCl. The supernatant containing soluble protein was mixed with the carrageenan solution in a ratio of 2.8:1 and completed with demineralized water at pH 3. The mixture was stirred for 2 hours. The average Zeta potential of the precipitate formed was -2.9 mV. The complexation yield was calculated to be 68%. Figure 3 The precipitate formed is shown, measuring 15 μm.

[0141] Example 4 - Pea protein, gum arabic and carrageenan

[0142] The following solutions were prepared: (a) a 5% (w / w) pea protein isolate solution was adjusted to pH 3 with HCl, (b) a 1% (w / w) carrageenan (SATIAGUM, Cargill, Wayzata, MN) was adjusted to pH 3 with HCl, and (c) a 2.5 wt% gum arabic solution was adjusted to pH 3 with HCl. The carrageenan and gum arabic solutions were first diluted and mixed together, with the concentration of the carrageenan solution being 0.1 wt% and the concentration of the gum arabic solution being 0.21 wt%. The mixture was stirred at 400 rpm for 15 minutes. Subsequently, the pea protein solution was slowly added with further stirring and was made up to 100% with demineralized water at pH 3. The solution was stirred for 2 hours. The weight ratio of pea protein, gum arabic and carrageenan was 9.7:2.1:1. The complexation yield was calculated to be 50%, and the average Zeta potential of the precipitate formed was 5.45 mV. All precipitates showed stability over a wide pH range (ie, from 3.5 to 6.6). Figure 4 The precipitate formed is shown, measuring 15 μm.

[0143] Example 5 - Pea protein and gum arabic and spray drying

[0144] Two solutions were prepared: (a) 5% (w / w) pea protein isolate and 1.3% (w / w) gum arabic solution. After hydration of the pea protein solution, the pH of both solutions was adjusted to pH 3.6. Pea protein isolate is positively charged and interacts rapidly with anionic gum arabic. The protein solution was centrifuged and only the supernatant was used to determine the soluble protein content of 1.75% (w / w). The mixing ratio was 3:1 pea protein / gum arabic weight ratio. The total biopolymer concentration was approximately 1.4% (w / w) before the addition of the carrier (maltodextrin 18DE, added at a total concentration of 25% (w / w)). The total mixture was stirred for 2 hours and stored in a refrigerator overnight. The mixture was spray dried the next day using standard spray drying techniques. The formed coacervate was retained during the spray drying process, as shown in Figure 5 shown.

[0145] Example 6 - Pea protein and sunflower protein

[0146] A 5% (w / w) pea protein isolate solution and a 2% (w / w) sunflower protein solution were prepared and left to hydrate overnight. The pH of both solutions was adjusted to pH 3.5 and the supernatant was removed after centrifugation at 4000 rpm for 15 minutes. The solutions were mixed in a 2:1 sunflower protein / pea protein weight ratio and stirred for 2 hours to form a precipitate. Once the precipitate was formed, a carrier was introduced. The carrier was maltodextrin 18DE, which was added and the total amount. After stirring for two hours, the mixture was spray dried. The precipitate formed was retained during the drying process, as Figure 6 shown.

[0147] Example 7 - Pea Protein and Canola Protein

[0148] A 5% (w / w) solution of pea protein isolate was prepared, stirred for 2 hours, and then placed in a refrigerator to hydrate overnight. A 2% (w / w) solution of canola protein was prepared, stirred for 2 hours, and then placed in a refrigerator to hydrate overnight. The samples were allowed to stand at their natural pH, which was approximately pH 7.3 for pea protein isolate and pH 6.3 for canola protein. The samples were centrifuged (@4500rpm for 15 minutes) and the supernatant was removed (2.6% soluble protein for pea protein isolate, -25mV, 1.8% soluble protein for canola protein, +4mV). The samples were then mixed in a ratio of 1.4:1, with a final total biopolymer concentration of approximately 2% (w / w). A precipitate formed immediately. The samples were stirred overnight and then analyzed by microscopy.

[0149] Example 8 - Algae protein and wheat gluten

[0150] A 5% (w / w) solution of chlorella algae protein was prepared, stirred for 2 hours, and then placed in a refrigerator to hydrate overnight. A 2% (w / w) solution of wheat gluten was prepared, stirred for 2 hours, and then placed in a refrigerator to hydrate overnight. The samples were allowed to stand at their natural pH, which was approximately pH 5.6 for chlorella protein and approximately pH 4.9 for wheat gluten. The Zeta potential of chlorella protein at natural pH was -11mV, and the Zeta potential of wheat gluten was +9mV. The samples were centrifuged (@4500rpm for 15 minutes) and the supernatant was removed. The soluble protein in the chlorella protein sample was 0.7% (w / w), while the soluble protein in wheat gluten was 1.6% (w / w). The samples were then mixed at a ratio of 2.2:1, with a final total biopolymer concentration of approximately 0.76% (w / w). A precipitate formed quickly. Figure 7 Micrographs of the precipitates are shown.

[0151] Example 9 - Wheat protein and potato gluten

[0152] A wheat protein solution with a protein content of 2% is emulsified with a 10-fold amount of oil (caprylic / caprylic triglyceride). The potato protein supernatant is added under stirring to a total biopolymer concentration of 0.8% (R=1). The entire process is carried out at about pH 5.5. After stirring for 2 hours, transglutaminase (40 U / g protein) is added. The dispersion is heated to 40°C and stirred for 2 hours, and then stirring is continued at room temperature overnight. The enzyme is inactivated at 80°C for at least 30 minutes. The wheat protein is adsorbed on the surface of the particle membrane, which is rigid and retracts after squeezing. Figure 8 Micrographs of microparticles after enzyme inactivation are shown.

[0153] The same protocol as above was used except that the oil concentration was reduced to 1% (case a) and 1.66% (case b). Fig. 9 Micrographs of the microparticles formed after the deactivation step are shown at 40X magnification, case a on the left and case b on the right.

[0154] The two proteins were mixed at pH 2 to avoid electrostatic interactions; the emulsion with the second protein was then adjusted stepwise to a final pH of 5.35 and stirred at room temperature for 2 hours. Tgase (transglutaminase) was added and the temperature was kept at 40°C for 3 hours, followed by inactivation at 80°C for 30 minutes. Fig.10 Micrographs taken after inactivation at 40X magnification are shown.

[0155] Example 10 - Canola and potato protein

[0156] Potato protein was used to emulsify oil (caprylic / caprylic glycerides) at a final concentration of 10%. Rapeseed protein concentrate was then added to give a total final protein concentration of 4%, with a relative weight ratio of R 低芥酸菜籽 / 马铃薯 =3 (case a), 2 (case b), 1 (case c), 0.5 (case d). The mixture was stirred at room temperature, then Tgase was added and the temperature was kept at 40°C for 3 hours. The enzyme was then inactivated at 80°C for 30 minutes. Fig.11 Micrographs at 40X magnification of the microparticles formed after inactivation for the four cases are shown.

[0157] Example 11 - Sensory Testing

[0158] A vegetable protein solution of 5% pea protein isolate was prepared in demineralized water. A second vegetable protein solution was prepared, wherein the second protein was selected from vegetable protein isolates (e.g., canola and potato protein) and / or protein concentrates (e.g., soluble wheat protein) at a concentration of 2%. The solution was hydrated at room temperature for 2 hours. The pH values ​​of pea protein isolate and canola protein isolate were adjusted to 6 with 1M and 0.1M food grade HCl, respectively, and potato and wheat protein were adjusted to pH 6 with NaOH. The solution was kept under magnetic stirring for 2 hours. The total solution was centrifuged at 4500rpm for 15 minutes, and then the supernatant was removed and analyzed gravimetrically by TGA. The ionic charge was measured by Zetasizer (Malvern). Pea protein isolate, canola protein isolate, potato protein isolate, and wheat protein contained 1.61%, 1.89%, 1.19%, and 1.18% soluble protein fractions, respectively. Pea protein isolate was positively charged, while the second protein was negatively charged. Pea protein isolate was complexed with canola or potato protein isolate in a 1:1 ratio and with a combination of wheat proteins in a 1:2 ratio. The solutions were blended to achieve maximum total biopolymer concentration and then stirred for 30 minutes. Fig.12 Micrographs of the complexes formed are shown: a) pea protein isolate / canola protein isolate; b) pea protein isolate / potato protein isolate; c) pea protein isolate / soluble wheat gluten).

[0159] Half of each solution was kept in this state and the other half was pasteurized at 92°C for 10 minutes. The solution was placed in a refrigerator overnight along with the two protein isolate supernatants.

[0160] Sensory evaluation was performed on clean slurries (0.25% pea protein isolate and 0.25% second protein) diluted to 0.5% of total biopolymer. Cleaning was performed by discarding the supernatant of the complex solution and re-diluting the complex by adding demineralized water. The pea protein isolate supernatant was diluted to 0.25% as a reference sample to evaluate the odor masking effect of the formed complex. Table 1 shows the results of the sensory evaluation, where approximately 20 panelists evaluated each quality on a scale of 0 to 10, with 10 indicating the highest intensity. Sensory evaluation of mixtures and individual ingredients. The reference was a 0.25% pea protein isolate solution; the complex formed by pea protein isolate complexed with a second plant protein, with a total biopolymer concentration of 0.5% (based on a theoretical pea protein isolate concentration of 0.25%).

[0161] Table 1

[0162] Peas (reference) Pea / Wheat Peas / Potatoes Peas / Canola Overall strength 4.9 5.1 4.9 5.6 Whole grain flavor 5.6 4.2 2.4 3.0 Green plant tone 2.6 2.2 1.9 2.3 sour 1.1 0.8 1.2 2.1 bitterness 2.9 3.8 3.2 3.8 Astringency 2.3 3.0 5.3 4.3 Sweetness 0.9 1.3 1.1 2.0 Consistency 2.3 3.8 3.1 4.1 Mouth coating 3.0 3.7 3.4 3.7

[0163] It was observed that the intensity of perceived negative descriptors of pea protein such as “whole grain” and “green vegetable” was reduced in the composite compared to the reference sample. The composite enhanced the “thickness” textural attribute of the samples evaluated and was therefore shown to have an impact on texture.

[0164] Example 12 - Sensory Testing

[0165] A complex of pea protein and canola protein was prepared for evaluation by approximately 20 panelists. Sample preparation was the same as in Example 11. For sensory evaluation, the reference solutions were pasteurized pea protein isolate supernatant diluted to a final concentration of 0.5% and 0.25%, respectively, non-pasteurized pea protein and canola protein isolate supernatant at a concentration of 0.5%, and the complex in slurry or cleaned form. Cleaning consisted of discarding excess protein in the formed complex supernatant and then re-diluting with demineralized water to the target final concentration.

[0166] The nine descriptors were rated on an intensity scale of 0 to 10 (not strong to very strong). Table 2 summarizes the results.

[0167] Table 2

[0168]

[0169] These results show how the formulations can reduce the intensity of the descriptors “whole grain” and “green vegetables” while enhancing textural attributes such as “mouthfeel” and “body”.

[0170] Example 13 - Emulsion

[0171] A 2% w / w potato protein isolate solution was prepared and the oil-based flavor composition was emulsified with the protein solution using a rotor / stator homogenizer at 10,000 rpm. Wheat protein supernatant (as described in Example 11) was added under magnetic stirring to a total biopolymer concentration of 0.8% (R=1). The process was performed at a pH of around 5.5. The emulsion was then stirred for two hours and placed in a refrigerator. It was observed that the wheat protein adsorbed on the surface of the particle film, enhancing the rigidity of the droplet film. Similar examples were prepared using an oil flavor composition instead of a flavor composition.

[0172] 2% potato protein isolate was used to emulsify a final oil concentration of 10% (caprylic / caprylic glycerides). 2% canola protein isolate solution was added to give a total final protein concentration of 4%, with a mass ratio of R 低芥酸菜籽 / 马铃薯 The ratios R = 3, 2, 1 and 0.5 were used. Canola protein concentrate was absorbed onto an oil film emulsified with potato protein isolate. The protein ratio affects the properties of the film. For the combinations used here, the ratios R = 3 and R = 2 resulted in films with increased rigidity, as determined by visual assessment of the deformation behavior of the film by compressing it between two glass slides using a bright field microscope. Thus, the ratio can be used to fine-tune the properties of the film to obtain a softer or stiffer film. Fig.13 A micrograph of the particles formed is shown, with the lower bar representing 50 microns.

[0173] Example 14 - Protein / Protein Paste for Masking Off-Taste

[0174] Both pea protein and canola protein isolate have opposite charges at their natural pH values ​​(7.5 and pH 6, respectively), and thus can be advantageously exploited here. Pea protein isolate and canola protein isolate powders were mixed in a kitchen blender, assuming solubility of 1 g for 5 g and 1 g for 1 g, respectively. Water was slowly added to the dry mixture; the blend was kneaded for 30 minutes. The final product was a moist paste with a protein / water content of 40 / 60 or 50 / 50. Protein interactions were visually assessed by microscopy. The resulting paste was extruded. It is believed that favorable protein / protein interactions block binding sites that lead to noticeable off-flavors, thereby reducing negative perceptual descriptors such as "whole grain" and "green vegetable". The particle size of the resulting structure was up to 50 microns.

[0175] Example 15 - Spray-dried composites and dairy analogs

[0176] The complex was formed as described in Example 11 and spray dried using maltodextrin as a carrier (at a concentration of about 20%). The spray dried powder i) was blended with pea protein isolate powder at R=1 before extrusion, or used entirely for high moisture extrusion. The final product had reduced off-flavor compared to extrudates produced purely with pea protein isolate; ii) could be used as a base for fermented dairy analog products with reduced off-flavor; iii) diluted with water to a final protein concentration of 3% or 6%, and the spray dried particles were stabilized with a clean label colloidal stabilizer.

[0177] Example 16 - Gel droplets and improved mouthfeel of plant-based burgers

[0178] Prepare 5% solutions of pea protein isolate and sunflower protein. Stir the solution for 2 hours to allow complete hydration. Subsequently, adjust the pH to pH 3 with food grade HCl; stir the solution for another 2 hours. Centrifuge the protein solution at 4500 rpm for 15 minutes and remove the supernatant. Simultaneously prepare a carrageenan solution at a final concentration of 1%. The carrageenan can be kappa or iota or a mixture of both, preferably iota. Kappa-carrageenan improves gel strength, while iota-carrageenan improves flexibility.

[0179] To prepare the gel droplets, the carrageenan solution is added to the pea protein isolate supernatant (step A) using a pipette under stirring. The formed droplets are stirred at room temperature for 15 minutes to form a stable droplet film. The second protein solution is added and then stirred for 15 minutes. Transglutaminase is added to the solution. Activation and deactivation are carried out at 40°C for 2 hours and at 80°C for 30 minutes, respectively. The gel droplets are sieved and transferred to demineralized water, where they retain their shape and stiffness. The prototype produced can be added to meat simulated beef patties to enhance the taste. The droplets are characterized by a particle size of about 5 mm and are therefore visible to the naked eye.

[0180] Alternatively, step A (addition of the carrageenan solution) can be performed using a variety of metering techniques, including (i) metering by a syringe pump through a capillary connected to a tube and a syringe; (ii) using a granulation / injection device, or (iii) using a nozzle if smaller droplets are desired. Smaller droplets can be produced by metering the carrageenan solution from a smaller diameter orifice, and larger droplets can be produced using a larger diameter orifice.

[0181] Example 17 - Cross-linking

[0182] An emulsion was prepared according to Example 13. After completing all the steps described in Example 13, transglutaminase was added for crosslinking at a concentration of 0.3% w / w (per total mass of liquid). The dispersion was heated to 40°C and stirred for 2 hours and continued to stir overnight at room temperature. The enzyme was inactivated at 80°C for at least 30 minutes. The result was a soft gelatin capsule slurry with a crosslinked protein / protein film. Fig.14 A micrograph of the emulsion formed is shown, with the lower bar representing 50 microns.

[0183] Example 18 - Soft Capsule Processing

[0184] In order to obtain dry powders of the formulations described in Examples 13 and 14, the emulsion in Example 13 and the soft capsules in Example 17 were further processed by spray drying using a laboratory-scale spray dryer. Maltodextrin with a dextrose equivalent of DE18 was added to 20% w / w in the aqueous phase, and the emulsion obtained in Example 13 or the soft capsules in Example 17 were processed into powder form. (Spray drying parameters: flow rate 100 ml / hour, air temperature set to 190 degrees Celsius).

[0185] Example 19 - Combination of cross-linked and non-cross-linked

[0186] By mixing the emulsion prepared in Example 13 and the crosslinked soft capsule slurry in Example 17, a combined system comprising a mixture of non-crosslinked emulsion droplets and crosslinked soft capsules can be obtained. Such a mixture may be beneficial if it is desired to deliver flavors or other oil-based actives on different time scales, where the non-crosslinked oil droplets allow for immediate release, while the crosslinked soft capsule droplets provide extended release. Alternatively, different oil-based flavor compositions can be used for the non-crosslinked and crosslinked emulsions.

[0187] The combined system can also be spray-dried; the combined dry system can also be obtained by preparing and drying a separate dry emulsion and a dry slurry for soft capsules, respectively, and then blending the mixture into powders.

[0188] It should be understood that for any combination described in this example, the emulsion or the slurry of the softgel capsule can contain the same flavor or fragrance composition, or they can each contain a different flavor or fragrance composition.

Claims

1. A polyelectrolyte complex comprising a polycationic non-animal protein and a polyanionic polymer, wherein the polycationic non-animal protein and the polyanionic polymer are bound by electrostatic attraction. 2 . The polyelectrolyte complex according to claim 1 , wherein the polycationic non-animal protein is a polycationic plant protein, such as pea protein, soy protein, broad bean protein, potato protein, etc. 3 . The polyelectrolyte complex according to claim 1 , wherein the polycationic non-animal protein is pea protein, soy protein or a combination thereof. 4 . The polyelectrolyte complex according to claim 1 , wherein the polyanionic polymer comprises pectin, gum arabic, carrageenan or any combination thereof.

5. The polyelectrolyte complex according to any one of claims 1 to 4, wherein the polyanionic polymer is a plant protein, such as sunflower protein, potato protein, etc. The polyelectrolyte complex according to any one of claims 1 to 5, wherein the polyelectrolyte complex is in the form of particles.

7. The polyelectrolyte complex according to claim 6, wherein the particles are formed by precipitation from an aqueous medium.

8. The polyelectrolyte complex according to claim 6, wherein the particles are formed by removing the aqueous medium, such as by spray drying.

9. An ingestible composition comprising the polyelectrolyte complex of any one of claims 1 to 8.

10. The ingestible composition of claim 9, wherein the polyelectrolyte complex comprises 1 wt% to 80 wt% of the ingestible composition based on the total dry weight of the ingestible composition.

11. An ingestible composition according to claim 9 or 10, further comprising plant fibres.

12. A flavored product comprising the ingestible composition of any one of claims 9 to 11.

13. The flavored product according to claim 12, wherein the flavored product is a dairy analog or a meat analog.

14. Use of a polyanionic polymer for reducing one or more off-flavors of a polycationic non-animal protein, the use comprising forming a polyelectrolyte complex between the polycationic non-animal protein and the polyanionic polymer.

15. Use of a polyanionic polymer for enhancing the mouthfeel or perceived juiciness or perceived thickness of a polycationic non-animal protein, said use comprising forming a polyelectrolyte complex between the polycationic non-animal protein and the polyanionic polymer.

16. A method of reducing one or more off-flavors of a polycationic non-animal protein, the method comprising forming a polyelectrolyte complex between the polycationic non-animal protein and a polyanionic polymer.

17. A method of enhancing the mouthfeel or perceived juiciness or perceived thickness of a polycationic non-animal protein, the method comprising forming a polyelectrolyte complex between the polycationic non-animal protein and a polyanionic polymer.

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