Melt blended thermoplastic protein elastomer composites

Abstract

The present disclosure relates to thermoplastic protein elastomer compositions comprising a protein, at least one reactive thermoplastic elastomer, and at least one softener, and composites made from these compositions. Methods of making and using the thermoplastic protein elastomer composite material to produce engineered leather are also disclosed. In some embodiments, the protein is selected from the group consisting of soy protein, cellulase, corn protein, egg white albumin, and pea protein; and wherein the protein and the thermoplastic elastomer are not covalently bound together. In some embodiments, the protein and the thermoplastic elastomer are present in a co-continuous phase.

Description

Technical Field

[0001] The present disclosure relates to thermoplastic protein elastomer composites comprising a protein blended with a thermoplastic elastomer. In some embodiments, the thermoplastic protein elastomer composites can be used to prepare textile or fabric articles, such as textile or fabric articles typically prepared from natural leather. Background Art

[0002] Leather is a common product used in many industries, including: the furniture industry, where leather is often used as a furniture upholstery material; the apparel industry, where leather is used to make pants and jackets; the footwear industry, where leather is used to make casual and dress shoes; the luggage industry; the handbags and accessories industry; and the automotive industry. The global trade value of leather is high, and the demand for leather products continues to grow. Although leather seems to be everywhere, there are various costs, restrictions, and social issues associated with producing natural leather. First, natural leather is made from animal skins, so livestock must be raised and slaughtered. Raising livestock requires large amounts of feed, pasture, water, and fossil fuels, and can cause air and waterway pollution, such as through greenhouse gases such as methane. Leather production also raises social issues related to the treatment of animals. In recent years, the supply of traditional high-quality leather has also seen a considerable decline. For at least these reasons, it is desirable to find alternative ways to meet the demand for leather. Summary of the invention

[0003] The present disclosure provides thermoplastic protein elastomer composites suitable for various applications (including textile or fabric applications). In some embodiments, the thermoplastic protein elastomer composite comprises a protein and a thermoplastic elastomer covalently bound together. In some embodiments, the protein and the thermoplastic elastomer are not covalently bound together. In some embodiments, the protein and the thermoplastic elastomer are present in a co-continuous phase. The present disclosure also provides a method for preparing the thermoplastic protein elastomer composite and an article comprising the thermoplastic protein elastomer composite.

[0004] The first embodiment (1) of the present disclosure relates to a thermoplastic protein elastomer composite material, which comprises a protein containing at least one first reactive functional group, which has been reacted with a thermoplastic elastomer containing at least one second reactive functional group, wherein the protein is a protein other than collagen, gelatin or any combination thereof.

[0005] In the second embodiment (2), the protein and the thermoplastic elastomer according to the first embodiment (1) are covalently bound together by reaction of the first reactive functional group and the second reactive functional group.

[0006] In a third embodiment (3), the protein according to the first embodiment (1) or the second embodiment (2) is selected from the group consisting of soy protein, cellulase, zein, egg white albumin and pea protein.

[0007] In a fourth embodiment (4), the first reactive functional group according to any one of embodiments (1) to (3) is an amino group, a hydroxyl group or a carboxylic acid group.

[0008] In a fifth embodiment (5), the second reactive functional group according to any one of embodiments (1) to (4) is maleic anhydride, epoxy, silane or glycidyl.

[0009] In a sixth embodiment (6), the second reactive functional group according to the fifth embodiment (5) is an epoxy group.

[0010] In a seventh embodiment (7), the thermoplastic elastomer according to any one of embodiments (1) to (6) is selected from the group consisting of maleated polyethylene, maleated polypropylene, maleated styrene-ethylene-butylene-styrene block copolymer, maleated styrene-butadiene-styrene block copolymer, maleated styrene-ethylene-propylene-styrene block copolymer, maleated ethylene-propylene rubber, epoxidized natural rubber, methyl methacrylate grafted natural rubber, polyhydroxyalkanoate and polyurethane.

[0011] In an eighth embodiment (8), the thermoplastic elastomer according to any one of embodiments (1) to (6) is an epoxidized natural rubber.

[0012] In a ninth embodiment (9), the epoxidized natural rubber according to embodiment (8) comprises about 50% of epoxidized olefinic bonds.

[0013] In a tenth embodiment (10), the composite material according to any one of embodiments (1) to (9) is a film.

[0014] An eleventh embodiment (11) of the present disclosure is directed to a method for preparing a thermoplastic protein elastomer composite, the method comprising compounding a mixture comprising:

[0015] (a) a protein comprising a first functional group, wherein the protein is a protein other than collagen, gelatin, or any combination thereof;

[0016] (b) a reactive thermoplastic elastomer comprising a second functional group capable of reacting with the first functional group during compounding; and

[0017] (c) Softeners.

[0018] In a twelfth embodiment (12), the protein according to the eleventh embodiment (11) is selected from the group consisting of soy protein, cellulase, zein, egg white albumin and pea protein.

[0019] In a thirteenth embodiment (13), the softening agent according to the eleventh embodiment (11) or the twelfth embodiment (12) is a protein softening agent.

[0020] In a fourteenth embodiment (14), the protein softener according to the thirteenth embodiment (13) is alcohol.

[0021] In a fifteenth embodiment (15), the alcohol according to the fourteenth embodiment (14) is glycerol.

[0022] In a sixteenth embodiment (16), the method according to any one of embodiments (11) to (15) comprises mixing the protein and the softener to form a protein solution, and compounding the protein solution and the reactive thermoplastic elastomer to form the thermoplastic protein elastomer composite.

[0023] In a seventeenth embodiment (17), the mixture according to any one of embodiments (11) to (16) further comprises a catalyst configured to promote the reaction between the second functional group and the first functional group during compounding.

[0024] In an eighteenth embodiment (18), the method according to any one of embodiments (11) to (17) further comprises heat pressing the thermoplastic protein elastomer composite to form a thermoplastic protein composite film.

[0025] In a nineteenth embodiment (19), the method according to any one of embodiments (11) to (18) further comprises attaching the thermoplastic protein composite to a fabric.

[0026] The twentieth embodiment (20) of the present disclosure relates to an article comprising the composite material according to any one of embodiments (1) to (19).

[0027] The twenty-first embodiment (21) of the present disclosure relates to a thermoplastic protein elastomer composite material, which comprises a protein blended with a thermoplastic elastomer, wherein the protein is present in a first phase within the composite material and the thermoplastic elastomer is present in a second phase within the composite material, and wherein the first phase and the second phase are co-continuous.

[0028] In the twenty-second embodiment (22), about 50% to about 99% of the protein according to the twenty-first embodiment (21) is covalently bound to the thermoplastic elastomer.

[0029] In the twenty-third embodiment (23), about 20% to less than about 50% of the protein according to the twenty-first embodiment (21) is covalently bound to the thermoplastic elastomer.

[0030] In the twenty-fourth embodiment (24), the protein according to the twenty-first embodiment (21) is detectable in an amount to less than about 20% of the protein is covalently bound to the thermoplastic elastomer.

[0031] In the twenty-fifth embodiment (25), the protein according to the twenty-first embodiment (21) is not covalently bound to the thermoplastic elastomer.

[0032] In the twenty-sixth embodiment (26), the protein and the thermoplastic elastomer according to the twenty-first embodiment (21) are covalently bonded together by reaction of a first functional group on the protein and a second reactive functional group on the thermoplastic elastomer.

[0033] In the twenty-seventh embodiment (27), the protein according to any one of embodiments (21) to (26) is a protein other than collagen, gelatin, or any combination thereof.

[0034] In the twenty-eighth embodiment (28), the protein according to any one of embodiments (21) to (26) is selected from the group consisting of soy protein, cellulase and zein.

[0035] In the twenty-ninth embodiment (29), the thermoplastic elastomer according to any one of embodiments (21) to (28) is selected from the group consisting of maleated polyethylene, maleated polypropylene, maleated styrene-ethylene-butylene-styrene block copolymer, maleated styrene-butadiene-styrene block copolymer, maleated styrene-ethylene-propylene-styrene block copolymer, maleated ethylene-propylene rubber, epoxidized natural rubber, methyl methacrylate grafted natural rubber, polyhydroxyalkanoates and polyurethanes.

[0036] In a thirtieth embodiment (30), the thermoplastic elastomer according to any one of embodiments (21) to (28) is epoxidized natural rubber.

[0037] In the thirty-first embodiment (31), the epoxidized natural rubber according to the thirtieth embodiment (30) comprises about 50% epoxidized olefinic bonds.

[0038] In a thirty-second embodiment (32), the composite material according to any one of embodiments (21) to (31) is a film.

[0039] In the thirty-third embodiment (33), at a temperature between about 50°C and about 180°C, the first phase according to any one of embodiments (21) to (32) has a first complex viscosity at a certain angular frequency, and the second phase according to any one of embodiments (21) to (32) has a second complex viscosity at the angular frequency, further wherein the first complex viscosity is no more than one order of magnitude greater than the second complex viscosity, and wherein the first complex viscosity is no more than one order of magnitude less than the second complex viscosity.

[0040] The thirty-fourth embodiment (34) of the present disclosure is directed to a method for preparing a thermoplastic protein elastomer composite, the method comprising compounding a mixture comprising:

[0041] (a) Protein;

[0042] (b) thermoplastic elastomers; and

[0043] (c) a softener, wherein, after compounding, the protein is present in a first phase within the composite and the thermoplastic elastomer is present in a second phase within the composite, and wherein the first phase and the second phase are co-continuous.

[0044] In the thirty-fifth embodiment (35), the protein according to the thirty-fourth embodiment (34) is a protein other than collagen, gelatin, or any combination thereof.

[0045] In the thirty-sixth embodiment (36), the protein according to the thirty-fourth embodiment (34) is selected from the group consisting of soy protein, cellulase and zein.

[0046] In the thirty-seventh embodiment (37), the softening agent according to any one of embodiments (34) to (36) is an alcohol.

[0047] In the thirty-eighth embodiment (38), the alcohol according to the thirty-seventh embodiment (37) is glycerol.

[0048] In the thirty-ninth embodiment (39), the method according to any one of embodiments (34) to (38) further comprises mixing the protein and the softener to form a protein solution, and compounding the protein solution and the thermoplastic elastomer to form the thermoplastic protein elastomer composite.

[0049] In a fortieth embodiment (40), the method according to any one of embodiments (34) to (39) further comprises heat pressing the thermoplastic protein elastomer composite to form a thermoplastic protein composite film.

[0050] In a forty-first embodiment (41), the method according to any one of embodiments (34) to (40) further comprises attaching the thermoplastic protein composite to a fabric.

[0051] In the forty-second embodiment (42), at a temperature between about 50°C and about 180°C, the first phase according to any one of embodiments (34) to (41) has a first complex viscosity at a certain angular frequency, and the second phase according to any one of embodiments (34) to (41) has a second complex viscosity at the angular frequency, further wherein the first complex viscosity is no more than one order of magnitude greater than the second complex viscosity, and wherein the first complex viscosity is no more than one order of magnitude less than the second complex viscosity.

[0052] In the forty-third embodiment (43), after compounding, about 50% to about 99% of the protein according to any one of embodiments (34) to (42) is covalently bound to the thermoplastic elastomer.

[0053] In the forty-fourth embodiment (44), after compounding, from about 20% to less than about 50% of the protein according to any one of embodiments (34) to (42) is covalently bound to the thermoplastic elastomer.

[0054] In the forty-fifth embodiment (45), after compounding, a detectable amount of the protein according to any one of embodiments (34) to (42) to less than about 20% of the protein is covalently bound to the thermoplastic elastomer.

[0055] In the forty-sixth embodiment (46), after compounding, the protein according to any one of embodiments (34) to (42) is not covalently bound to the thermoplastic elastomer.

[0056] In the forty-seventh embodiment (47), after compounding, the protein and the thermoplastic elastomer according to any one of embodiments (34) to (42) are covalently bound together by reaction of a first functional group on the protein and a second reactive functional group on the thermoplastic elastomer.

[0057] A forty-eighth embodiment (48) of the present disclosure relates to an article comprising the composite material according to any one of embodiments (21) to (47).

[0058] In the forty-ninth embodiment (49), the percentage of protein covalently bound to the thermoplastic elastomer according to any one of embodiments (22) to (24) is measured in mol %.

[0059] In a fiftieth embodiment (50), the percentage of protein covalently bound to the thermoplastic elastomer according to any one of embodiments (22) to (24) is measured in weight %.

[0060] In the fifty-first embodiment (51), the percentage of protein covalently bound to the thermoplastic elastomer according to any one of embodiments (43) to (45) is measured in mol %.

[0061] In the fifty-second embodiment (52), the percentage of protein covalently bound to the thermoplastic elastomer according to any one of embodiments (43) to (45) is measured in weight %. BRIEF DESCRIPTION OF THE DRAWINGS

[0062] Figure 1 is a graph of the complex viscosities of epoxidized natural rubber-50 and two protein solutions measured at 100°C.

[0063] Figure 2 is a graph of the complex viscosities of epoxidized natural rubber-50 and two protein solutions measured at 120°C. DETAILED DESCRIPTION

[0064] definition

[0065] As used herein, "a", "an" and "the" include plural referents unless the context clearly indicates otherwise. The terms "a" or "an" and the terms "one / kind or more / kind" and "at least one / kind" can be used interchangeably herein.

[0066] As used in the claims, "comprising" is an open transition phrase. The list of elements following the transition phrase "comprising" is a non-exclusive list such that elements other than those specifically listed in the list may be present. As used in the claims, "consisting essentially of" or "consisting essentially of" limits the composition of materials to the specified materials and materials that do not materially affect the basic and novel properties of the material. As used in the claims, "consisting of" or "consisting entirely of" limits the composition of materials to the specified materials and excludes any materials not specified.

[0067] When quoting the numerical range including the upper limit and the lower limit herein, unless otherwise specified in a particular case, the range is intended to include its endpoints, and all integers and fractions within the range. When limiting the range, it is not intended that the scope of the claims be limited to the specific values ​​cited. In addition, when equivalents, concentrations or other values ​​or parameters are given with a list of ranges, one or more preferred ranges or preferred upper limits and preferred lower limits, it should be understood as specifically disclosing all ranges formed by any paired upper range limit or preferred value and any lower range limit or preferred value, regardless of whether such pairs are disclosed individually. Finally, when the term "about" is used to describe the endpoint of a value or range, the disclosure should be understood to include the specific value or endpoints mentioned. Regardless of whether the endpoint of a numerical value or range is described as "about", the endpoint of a numerical value or range is intended to include two embodiments: one is modified by "about", and one is not modified by "about".

[0068] As used herein, the term "about" refers to a value within the range of ±10% of the stated value. For example, about 3 kPa may include any value between 2.7 kPa and 3.3 kPa. That is, if a percentage is listed and the value of the percentage cannot be higher than 100%, such as 100 weight % or 99 weight %, then "about" does not modify the percentage to include values ​​higher than 100%.

[0069] As used herein, the term "substantially free" means that a component is present in a detectable amount of no more than about 0.1% by weight.

[0070] As used herein, the term "thermoplastic elastomer" refers to a polymer that (1) has the ability to be stretched beyond its original length and substantially retract to its original length when released; and (2) softens when exposed to heat and substantially returns to its original state when cooled to room temperature. In some embodiments, the thermoplastic elastomer is not crosslinked, and is otherwise free of crosslinks.

[0071] As used herein, the term "maleated" refers to a polymer wherein one or more maleic anhydride groups have been grafted onto the polymer backbone.

[0072] As used herein, the term "epoxidized" refers to a polymer in which one or more double bonds in the polymer backbone have been converted to an epoxide.

[0073] As used herein, the term "softener" refers to a substance or material that is incorporated into another material (usually a plastic or elastomer) to increase its flexibility, processability, or flowability.

[0074] As used herein, a protein described as being "covalently bound to" a thermoplastic elastomer means that the protein is directly bound to the thermoplastic elastomer via a covalent bond. For example, it is believed that hydroxyl and / or amino groups in the protein can react with anhydrides, epoxides, or other reactive functional groups present on the thermoplastic elastomer to form covalent bonds that connect the protein to the polymer. In some embodiments, a cross-linking agent can be used to form the covalent bonds. If a cross-linking agent is used, the nature of the bonding, i.e., the number of atoms separating the protein from the backbone of the polymer and the nature of the covalent bonds (i.e., carbon-oxygen, carbon-nitrogen, etc.), will vary depending on the location and nature of the functional groups present on a given thermoplastic elastomer and a particular cross-linking agent.

[0075] As used herein, the term "thermoplastic protein elastomer composite" refers to the product formed after blending, heating and cooling a thermoplastic protein elastomer composition. In some embodiments, the thermoplastic protein elastomer composite refers to the product formed after the reaction of a protein and a thermoplastic elastomer.

[0076] As used herein, when discussing two or more phases in a material, the term "co-continuous" is used to refer to two or more phases that are uniformly mixed within each other. In a co-continuous blend of two or more phases, neither the first phase nor the second phase is a dispersed phase that is completely encapsulated by the other phase. In contrast, in a co-continuous blend, the two or more phases are morphologically similar and interpenetrating. Typically, the two or more phases are elongated interpenetrating phases.

[0077] The present disclosure provides a thermoplastic protein elastomer composition, a thermoplastic protein elastomer composite material, and a method for preparing a thermoplastic protein elastomer composite material, which has a natural leather-like appearance and feel and mechanical properties. The thermoplastic protein elastomer composite material can have tactile properties, aesthetic properties, mechanical / performance properties, manufacturability properties, and / or thermal properties, etc., similar to natural leather.

[0078] Mechanical / performance properties that may be similar to natural leather include, but are not limited to, tensile strength, tear strength, elongation at break, abrasion resistance, internal cohesion, water resistance, and the ability to retain color when rubbed (color fastness). Tactile properties that may be similar to natural leather include, but are not limited to, softness, stiffness, coefficient of friction, and compression modulus. Aesthetic properties that may be similar to natural leather include, but are not limited to, dyeability, embossing, aging, color, color depth, and color pattern. Manufacturing properties that may be similar to natural leather include, but are not limited to, the ability to be stitched, cut, ground, and split. Thermal properties that may be similar to natural leather include, but are not limited to, heat resistance and resistance to hardening or softening over a significantly wide temperature range (e.g., 25°C to 100°C).

[0079] Thermoplastic protein elastomer composition

[0080] The present disclosure provides thermoplastic protein elastomer compositions. These compositions are suitable for preparing thermoplastic protein elastomer composites after treatment under appropriate conditions described elsewhere herein. For example, and in some embodiments, subjecting the thermoplastic protein elastomer composition to heat provides a thermoplastic protein elastomer composite.

[0081] In one embodiment, the present disclosure provides a thermoplastic protein elastomer composition comprising:

[0082] (a) Protein;

[0083] (b) reactive thermoplastic elastomers; and

[0084] (c) Softeners.

[0085] In some embodiments, the thermoplastic protein elastomer composition further comprises at least one non-reactive thermoplastic elastomer.

[0086] protein

[0087] In some embodiments, the protein may be soy protein. In some embodiments, the protein may be soy protein isolate. In some embodiments, the protein may be collagen. In some embodiments, the protein may be gelatin. In some embodiments, the protein may be pea protein. In some embodiments, the protein may be egg white albumin. In some embodiments, the protein may be zein. In some embodiments, the protein may be an enzyme. In some embodiments, the protein may be a cellulase.

[0088] Although many types of proteins are contemplated for use in the composite materials described herein, including, for example, collagen and gelatin, it should be understood that for all embodiments disclosed herein, the protein may be a protein other than collagen and / or gelatin. Thus, in some embodiments, the protein may be a protein other than collagen, gelatin, or any combination thereof. In some embodiments, the composite material may be free of or substantially free of collagen. In some embodiments, the composite material may be free of or substantially free of gelatin. In some embodiments, the composite material may be free of or substantially free of collagen and gelatin.

[0089] In some embodiments, the molecular weight of the protein may be from about 10 kDa to about 1000 kDa. In some embodiments, the molecular weight of the protein may be from about 10 kDa to about 1000 kDa, from about 10 kDa to about 500 kDa, from about 10 kDa to about 400 kDa, from about 10 kDa to about 300 kDa, from about 10 kDa to about 200 kDa, from about 10 kDa to about 100 kDa, from about 10 kDa to about 50 kDa, from about 50 kDa to about 1000 kDa, from about 50 kDa to about 500 kDa, from about 50 kDa to about 400 kDa, from about 50 kDa to about 300 kDa, from about 50 kDa to about 200 kDa, from about 50 kDa to about 100 kDa, from about 100 kDa to about 1000 kDa. , about 100 kDa to about 500 kDa, about 100 kDa to about 400 kDa, about 100 kDa to about 300 kDa, about 100 kDa to about 200 kDa, about 200 kDa to about 1000 kDa, about 200 kDa to about 500 kDa, about 200 kDa to about 400 kDa, about 200 kDa to about 300 kDa, about 300 kDa to about 1000 kDa, about 300 kDa to about 500 kDa, about 300 kDa to about 400 kDa, about 400 kDa to about 1000 kDa, about 400 kDa to about 500 kDa, or about 500 kDa to about 1000 kDa.

[0090] In some embodiments, the protein can be dissolved in an aqueous solution to form a protein solution. In some embodiments, the protein solution may also include one or more protein softeners. In some embodiments, the protein softener is glycerol. When blended with a thermoplastic elastomer as discussed herein, the protein solution may be referred to as a protein phase, and the thermoplastic elastomer may be referred to as a polymer phase.

[0091] Thermoplastic elastomer

[0092] The compositions described herein include at least one thermoplastic elastomer. In some embodiments, the composition may include one to five, one to four, one to three, one to two, two to five, two to four, two to three, three to five, three to four, or four to five thermoplastic elastomers. In some embodiments, the composition may include one, two, three, four, or five thermoplastic elastomers. In some embodiments, the composition may include one thermoplastic elastomer. In some embodiments, the composition may include two thermoplastic elastomers.

[0093] Thermoplastic elastomers are a class of copolymers consisting of materials that have both thermoplastic and elastomeric properties. There are six major classes of thermoplastic elastomers: (1) styrenic block copolymers; (2) thermoplastic polyolefin elastomers; (3) thermoplastic vulcanizates; (4) thermoplastic polyurethanes; (5) thermoplastic copolyesters; and (6) thermoplastic polyamides. Thermoplastic elastomer compositions are versatile because they exhibit beneficial elastomeric properties and can be processed using standard thermoplastic processing equipment. To be suitable as a thermoplastic elastomer, a material must have the following characteristics: (1) the ability to be stretched to a moderate elongation and to recover to a state close to its original shape after the stress is removed; (2) be processable as a melt at elevated temperatures; and (3) be free of significant creep.

[0094] Due to the wide difference in polarity between protein and non-polar thermoplastic elastomer, protein is usually not easy to be dispersed in non-polar thermoplastic elastomer, but tends to aggregate during mixing due to the tendency to form strong intermolecular hydrogen bonds with other protein molecules. Due to the poor compatibility and dispersibility of protein and non-polar thermoplastic elastomer, it is difficult to obtain a composite material in which protein and thermoplastic elastomer form a single phase or co-continuous phase. However, it has been surprisingly found that when thermoplastic elastomer contains polar reactive groups such as anhydrides and epoxides, the compatibility of protein and thermoplastic elastomer is improved. Mixing protein with thermoplastic elastomers containing these functional groups can produce a composite material of protein and polymer phase forming a single phase or co-continuous phase.

[0095] In some embodiments, the thermoplastic elastomer comprising polar reactive groups can be chemically reactive with proteins under normal processing conditions. Without being bound by a particular theory, it is believed that the hydroxyl and / or amino groups in the protein can react with the anhydride groups, epoxy groups or other reactive functional groups present in the thermoplastic elastomer comprising polar reactive groups, so that the protein is covalently bound to the thermoplastic elastomer. Because the protein contains multiple hydroxyl and / or amino groups, they can react with multiple functional groups present in the thermoplastic elastomer, and the functional groups in the protein can react with the functional groups present on one or more polymer chains in the thermoplastic elastomer. That is, in certain embodiments, the protein can be used as a crosslinking agent. In addition, without being bound by any particular theory, it is believed that the anhydride groups, epoxy groups or other reactive functional groups present in the thermoplastic elastomer can promote non-covalent interactions with proteins, such as hydrogen bonds, van der Waals interactions, dipole-dipole forces and polarization forces, and these non-covalent interactions reduce the interfacial tension between the protein phase and the polymer phase, making the formation of co-continuous protein phases and polymer phases more feasible. It is believed that the formation of covalent bonds between the protein and the thermoplastic elastomer, the formation of non-covalent interactions between the protein and the thermoplastic elastomer, or a combination thereof may be responsible for the formation of a single phase and / or the formation of co-continuous protein and polymer phases.

[0096] Without being bound by theory, it is believed that if the protein phase and polymer phase of the blending have similar complex viscosity (e.g., complex viscosity within one order of magnitude of each other) at blending temperature and shear rate, they are more likely to form a co-continuous phase morphology. In addition, it is believed that the higher Tan (δ) and lower complex viscosity values ​​of the protein phase and polymer phase are generally conducive to fully flowing and mixing in the compounder for blending the protein phase and the polymer phase. It is also believed that if the protein phase and the polymer phase have similar volume fractions (e.g., 50:50 v / v), they are more likely to form a co-continuous phase morphology. In addition, it is believed that if the protein phase and the polymer phase have i) similar complex viscosity and ii) similar volume fractions at blending temperature and shear rate, they are more likely to form a co-continuous phase morphology.

[0097] In some embodiments, the volume fraction of the protein phase relative to the polymer phase may be about 50: 50. In some embodiments, the volume fraction of the protein phase relative to the polymer phase may be about 25:75, about 30:70, about 35:65, about 40:60, about 45:55, about 55:45, about 60:40, about 65:35, about 70:30, or about 25:75.

[0098] The complex viscosity of the protein phase and the polymer phase can be measured using a rheometer, as described herein. In some embodiments, at a temperature between about 50°C to about 180°C, the protein phase and the polymer phase may have a substantially similar complex viscosity at a certain angular frequency. In some embodiments, at a temperature between about 50°C to about 180°C, the protein phase and the polymer phase may have a complex viscosity that differs by no more than one order of magnitude at a certain angular frequency.

[0099] In some embodiments, at a temperature of about 50°C to about 180°C, the protein phase may have a first complex viscosity at a certain angular frequency, and the polymer phase may have a second complex viscosity at the angular frequency. In some embodiments, the first complex viscosity is no more than one order of magnitude greater than the second complex viscosity, and the first complex viscosity is no more than one order of magnitude less than the second complex viscosity. In some embodiments, the first complex viscosity is no more than half an order of magnitude greater than the second complex viscosity, and the first complex viscosity is no more than half an order of magnitude less than the second complex viscosity. In some embodiments, the first complex viscosity is no more than three quarters of an order of magnitude greater than the second complex viscosity, and the first complex viscosity is no more than three quarters of an order of magnitude less than the second complex viscosity. In some embodiments, the temperature between about 50°C to about 180°C can be the temperature at which the protein phase and the polymer phase are blended to form a composite material.

[0100] Unless otherwise stated, the complex viscosity (in centipoise, cP) of the protein phase and the polymer phase is measured on a non-compounded sample using the following procedure. Parallel plate fixtures are used to perform complex viscosity measurements on a TA Discovery HR-2 rheometer (or equivalent equipment). Frequency sweeps are used to measure complex viscosity at a certain temperature (e.g., 125°C or 140°C) or at a certain frequency with a temperature ramp (e.g., 25°C to 150°C). Frequency sweeps at a certain temperature are used to observe complex viscosity and Tan (δ) of the protein phase and the polymer phase. Before testing the sample, the sample is dried in an oven at 45°C for 6 to 12 hours. Immediately after drying, the sample is conditioned and tested. The samples tested using frequency sweeps are conditioned at their test temperature for about 3 minutes to about 10 minutes, maintained under moderate compression conditions (0.2 ± 0.1N), and previously determined to be within the linear viscoelastic range (usually 0.1% to 1%) under strain from 0.1rad / s to 100rad / s. The linear viscoelastic range is determined using an amplitude sweep procedure, where a sweep from 0.01% strain to 100% strain is performed at 10 rad / s, revealing the strain at which the material begins to yield. The strain within the linear viscoelastic region is then selected for the frequency sweep. For samples tested using a temperature ramp, the sample is conditioned at the starting temperature of the temperature ramp for about 3 minutes to about 10 minutes, maintained under moderate compression conditions (0.2 ± 0.1 N), and oscillated at a single frequency at a strain previously determined to be within the linear viscoelastic range (typically 0.1% to 1%).

[0101] In some embodiments, the thermoplastic elastomer may be a maleated thermoplastic elastomer. In some embodiments, the maleated thermoplastic elastomer may be a maleated polyethylene, a maleated polypropylene, a maleated styrene block copolymer such as a maleated styrene-ethylene-butylene-styrene block copolymer, a maleated styrene-butadiene-styrene block copolymer, or a maleated styrene-ethylene-propylene-styrene block copolymer, a maleated ethylene-propylene rubber, a polyhydroxyalkanoate, or a polyurethane.

[0102] In some embodiments, the thermoplastic elastomer may be natural rubber. In some embodiments, the thermoplastic elastomer may be modified natural rubber. In some embodiments, the modified natural rubber may be epoxidized natural rubber or methyl methacrylate grafted natural rubber.

[0103] In some embodiments, the thermoplastic elastomer may be polystyrene-block-poly(ethylene-random-butylene)-block-polystyrene-grafted-maleic anhydride, polyisoprene-grafted-maleic anhydride, poly(propylene-grafted-maleic anhydride), maleic anhydride-grafted-ethylene-propylene rubber, poly(ethylene-co-methyl acrylate-co-glycidyl methacrylate), polyethylene-grafted-maleic anhydride, or epoxidized natural rubber.

[0104] In some embodiments, the composition may comprise from about 10% to about 1000% by weight of the protein of the at least one thermoplastic elastomer. In some embodiments, the composition may comprise from about 10% to about 1000%, from about 10% to about 500%, from about 10% to about 200%, from about 10% to about 100%, from about 10% to about 75%, from about 10% to about 50%, from about 50% to about 1000%, from about 50% to about 500%, from about 50% to about 200%, from about 50% to about 100%, from about 50% to about 75%, from about 75% to about 1000%, from about 75% to about 500%, from about 75% to about 200%, from about 75% to about 100%, from about 100% to about 1000%, from about 100% to about 500%, from about 100% to about 200%, from about 200% to about 1000%, from about 200% to about 500%, or from about 500% to about 1000% of the at least one thermoplastic elastomer, by weight of protein. In some embodiments, the composition may comprise from about 75% to about 1000% by weight of the protein of the at least one thermoplastic elastomer.

[0105] Softener

[0106] Softeners can be incorporated into another material (usually a plastic or elastomer) to increase its flexibility, processability, or fluidity. In some embodiments, softeners can be incorporated into proteins to increase their flexibility, processability, or fluidity. In some embodiments, softeners can be incorporated into thermoplastic elastomers to increase their flexibility, processability, or fluidity. In some embodiments, softeners can be incorporated into both proteins and thermoplastic elastomers. In some embodiments, the softener incorporated into the protein is the same as the softener incorporated into the thermoplastic elastomer. In some embodiments, the softener incorporated into the protein is different from the softener incorporated into the thermoplastic elastomer. Changes in the type and content of the softener can affect the properties of the final flexible product. The selection of a specific polymer or elastomer is generally based on compatibility between components; the amount required for plasticization; processing characteristics; thermal, electrical, and mechanical properties required for the final product; durability; resistance to water, chemicals, and solar radiation; toxicity; and cost.

[0107] In some embodiments, the composition may include at least one softener. In some embodiments, the composition may include one to five, one to four, one to three, one to two, two to five, two to four, two to three, three to five, three to four, or four to five softeners. In some embodiments, the composition may include one, two, three, four, or five softeners. In some embodiments, the composition may include one softener. In some embodiments, the composition may include two softeners.

[0108] In some embodiments, the softening agent may be a protein softening agent, discussed in detail below. In some embodiments, the softening agent may be an elastomeric softening agent, also described in detail below.

[0109] In some embodiments, the composition may include at least one protein softener. In some embodiments, the composition may include at least one elastomeric softener. In some embodiments, the composition may include at least one protein softener and at least one elastomeric softener.

[0110] Protein softener

[0111] In some embodiments, the composition may include at least one protein softener. In some embodiments, the composition includes one to five, one to four, one to three, one to two, two to five, two to four, two to three, three to five, three to four, or four to five protein softeners. In some embodiments, the composition may include one, two, three, four, or five protein softeners. In some embodiments, the composition may include one protein softener.

[0112] In some embodiments, the protein softener may be water or alcohol.

[0113] In some embodiments, the protein softener may be an alcohol. In some embodiments, the protein softener may be a glycol such as glycerol, ethylene glycol, diethylene glycol, triethylene glycol, tetraethylene glycol, polyethylene glycol, sorbitol, mannitol, xylitol, 1,4-butanediol, meso-erythritol or adonitol. In some embodiments, the protein softener is glycerol.

[0114] In some embodiments, the protein softener can be polyethylene glycol (PEG) with a molecular weight (Mw) ranging from about 300 to about 20,000. In some embodiments, the protein softener can be PEG with a molecular weight (Mw) of 300, 400, 600, 800, 1500, 4000, 10,000, or 20,000. In some embodiments, the protein softener can be PEG 300 or PEG 400.

[0115] In some embodiments, the composition may include from about 1% to about 200% by weight of protein of at least one protein softener. In some embodiments, the composition may include from about 1% to about 200%, from about 1% to about 150%, from about 1% to about 100%, from about 1% to about 80%, from about 1% to about 60%, from about 1% to about 40%, from about 1% to about 20%, from about 1% to about 10%, from about 10% to about 100%, from about 10% to about 80%, from about 10% to about 60%, from about 1% to about 40%, from about 10% to about 20%, from about 1% to about 100%, from about 20% to about 80%, from about 20% to about 60%, from about 10% to about 40%, from about 10% to about 20%, from about 20% to about 100%, from about 20% to about 80%, from about 20% to about 60%. From about 60%, from about 20% to about 40%, from about 40% to about 100%, from about 40% to about 80%, from about 40% to about 60%, from about 60% to about 100%, from about 60% to about 80%, from about 80% to about 100%, from about 100% to about 120%, from about 100% to about 140%, from about 100% to about 160%, from about 100% to about 180%, from about 100% to about 200%, from about 120% to about 180%, or from about 140% to about 160% of at least one protein softener. In some embodiments, the composition may include from about 80% to about 100% of at least one protein softener by weight of protein.

[0116] Elastomer softener

[0117] In some embodiments, the composition may include at least one elastomeric softener. In some embodiments, the composition may include one to five, one to four, one to three, one to two, two to five, two to four, two to three, three to five, three to four, or four to five elastomeric softeners. In some embodiments, the composition may include one, two, three, four, or five elastomeric softeners. In some embodiments, the composition may include one elastomeric softener.

[0118] In some embodiments, the elastomer softener may be a mineral oil, a process oil, or a vegetable oil.

[0119] In some embodiments, the elastomer softener may be a process oil. In some embodiments, the process oil may be a paraffinic oil, a naphthenic oil, an aromatic oil, or a natural oil. In some embodiments, the elastomer softener may be a paraffinic oil. In some embodiments, the elastomer softener may be a paraffinic oil having a molecular weight of about 200 to about 1,000.

[0120] In some embodiments, the elastomer softener may be mineral oil.

[0121] In some embodiments, the elastomer softener can be a vegetable oil. In some embodiments, the vegetable oil can be soybean oil, linseed oil, castor oil, sunflower oil, rubber seed oil, palm oil, or coconut oil.

[0122] In some embodiments, the composition may comprise from about 0.1% to about 200%, by weight of protein, of at least one elastomer softener. In some embodiments, the composition comprises from about 0.1% to about 200%, from about 0.1% to about 100%, from about 0.1% to about 60%, from about 0.1% to about 40%, from about 0.1% to about 20%, from about 0.1% to about 10%, from about 10% to about 200%, from about 10% to about 100%, from about 10% to about 60%, from about 10% to about 40%, from about 10% to about 20%, from about 20% to about 200%, from about 20% to about 100%, from about 20% to about 60%, from about 20% to about 40%, from about 40% to about 200%, from about 40% to about 100%, from about 40% to about 60%, from about 60% to about 200%, from about 60% to about 100%, or from about 100% to about 200% of at least one elastomeric softener by weight of protein. In some embodiments, the composition may comprise from about 80% to about 100% by weight of the protein of the at least one elastomer softening agent.

[0123] Thermoplastic protein elastomer composites

[0124] The present disclosure provides a thermoplastic protein elastomer composite material. In some embodiments, the thermoplastic protein elastomer composite material includes a protein covalently bound to a thermoplastic elastomer by at least one of an amide bond, an ester bond, or an amino bond. In some embodiments, the thermoplastic protein elastomer composite material includes a protein blended with a thermoplastic elastomer, wherein the protein is present in a first phase within the composite material and the thermoplastic elastomer is present in a second phase within the composite material, and wherein the first phase and the second phase are co-continuous. In some embodiments, the thermoplastic protein elastomer composite material includes a combination of: (i) a protein covalently bound to a thermoplastic elastomer by at least one of an amide bond, an ester bond, or an amino bond, and (ii) a protein co-continuous with a thermoplastic elastomer present in the first phase within the composite material and in the second phase, wherein the protein covalently bound to the thermoplastic elastomer is present in the first phase, in the second phase, at the interface between the first phase and the second phase, or a combination thereof. In some embodiments, the protein is a protein other than collagen, gelatin, or any combination thereof.

[0125] The present disclosure provides a thermoplastic protein elastomer composite material, the thermoplastic protein elastomer composite material comprising a protein containing at least one first reactive functional group, the protein having been reacted with a thermoplastic elastomer containing at least one second reactive functional group, wherein the protein is a protein other than collagen, gelatin, or any combination thereof. In some embodiments, the present disclosure provides a thermoplastic elastomer composite material, the thermoplastic elastomer composite material comprising a protein containing at least one first reactive functional group and at least one thermoplastic elastomer containing at least one second reactive functional group, wherein the protein and the at least one thermoplastic elastomer are covalently bound together by reaction of the first reactive functional group and the second reactive functional group.

[0126] In some embodiments, the protein may be selected from the group consisting of soy protein, cellulase, zein, egg white albumin, and pea protein. In some embodiments, the protein may be selected from the group consisting of soy protein, cellulase, and zein. In some embodiments, the soy protein may be soy protein isolate.

[0127] In some embodiments, the first reactive functional group may be an amino group, a hydroxyl group, or a carboxylic acid group. In some embodiments, the second reactive functional group may be a maleic anhydride, an epoxy group, a silane group, or a glycidyl group. In some embodiments, the second reactive functional group is an epoxy group.

[0128] In some embodiments, the thermoplastic elastomer may have randomly positioned functional groups. In some embodiments, the thermoplastic elastomer having randomly positioned functional groups may be a random maleated polymer, a random epoxidized polymer, a random silylated polymer, or a random glycidylated polymer.

[0129] In some embodiments, the thermoplastic elastomer with randomly positioned functional groups may be a random maleated polymer. In some embodiments, the random maleated polymer may be a random maleated polyethylene, a random maleated propylene, a random maleated ethylene-propylene copolymer (random maleated EPR or random maleated ethylene-polypropylene rubber), a random maleated ethylene-propylene-diene monomer terpolymer (random maleated EPDM), a random maleated block copolymer such as a styrene block copolymer, or an acrylic block copolymer. In some embodiments, the random maleated polymer is a random maleated EPR, a random maleated EPDM, or a random maleated styrene block copolymer such as a random maleated poly(styrene-block-hydrogenated butadiene-block-styrene) (SEBS) or a maleated poly(styrene-block-hydrogenated isoprene-styrene) (SEPS).

[0130] In some embodiments, the thermoplastic elastomer having randomly positioned functional groups may be a random epoxidized polymer. In some embodiments, the random epoxidized polymer may be a random epoxidized diene-containing polymer. In some embodiments, the random epoxidized polymer may be a polymer containing isoprene monomer units (such as random epoxidized natural rubber (ENR)), a random epoxidized isoprene-containing block copolymer (such as poly (styrene-block-isoprene) or poly (styrene-block isoprene-block styrene)), a random epoxidized ethylene-propylene-diene monomer (epoxidized EPDM), or a random epoxidized polyisobutylene.

[0131] In some embodiments, the epoxidized natural rubber comprises about 10%, about 20%, about 30%, about 40%, about 50%, about 60%, about 70%, about 80%, or about 90% of the epoxidized olefinic bonds. In some embodiments, the epoxidized natural rubber comprises about 50% of the epoxidized olefinic bonds. In some embodiments, the epoxidized natural rubber comprises about 40% to about 60% of the epoxidized olefinic bonds. In some embodiments, the epoxidized natural rubber comprises about 10% to about 30%, about 10% to about 50%, about 10% to about 70%, about 10% to about 90%, about 20% to about 40%, about 20% to about 60%, about 20% to about 80%, about 40% to about 80%, about 50% to about 70%, about 50% to about 90%, about 60% to about 80%, or about 70% to about 90% of the epoxidized olefinic bonds.

[0132] In some embodiments, the randomly epoxidized polymer may present its epoxide groups through one or more randomly positioned glycidyl groups, i.e.

[0133]

[0134] In some embodiments, the thermoplastic elastomer having randomly positioned glycidyl groups may be a copolymer of glycidyl methacrylate or a polymer grafted with glycidyl methacrylate.

[0135] In some embodiments, the thermoplastic elastomer with randomly positioned functional groups may be a random silanized polymer. In some embodiments, the random silanized polymer may be a random silane functionalized ethylene-propylene-diene monomer (silane functionalized EPDM), a random silanized cellulose polymer, a random silanized polyvinyl alcohol or partially hydrolyzed polyvinyl acetate, a random silane functionalized polydimethylsiloxane, or a random silanized adhesive polymer.

[0136] In some embodiments, the thermoplastic elastomer may have groups placed in block form, as a coupling agent, or on the ends. Examples of such polymers include, but are not limited to, block copolymers containing glycidyl methacrylate blocks. Polymers coupled with silane coupling agents, where the functionality remains on the silane coupling agent, include styrene-butadiene rubber and styrylamine block copolymers.

[0137] In some embodiments, about 50 mol % to about 99 mol % of the protein is covalently bound to the thermoplastic elastomer. In some embodiments, about 60 mol % to about 99 mol %, about 70 mol % to about 99 mol %, about 80 mol % to about 99 mol %, about 90 mol % to about 99 mol %, about 60 mol % to about 90 mol %, about 70 mol % to about 90 mol %, about 80 mol % to about 90 mol %, about 60 mol % to about 80 mol %, about 70 mol % to about 80 mol %, or about 60 mol % to about 80 mol % of the protein is covalently bound to the thermoplastic elastomer.

[0138] In some embodiments, about 50% to about 99% by weight of the protein is covalently bound to the thermoplastic elastomer. In some embodiments, about 60% to about 99% by weight, about 70% to about 99% by weight, about 80% to about 99% by weight, about 90% to about 99% by weight, about 60% to about 90% by weight, about 70% to about 90% by weight, about 80% to about 90% by weight, about 60% to about 80% by weight, about 70% to about 80% by weight, or about 60% to about 80% by weight of the protein is covalently bound to the thermoplastic elastomer.

[0139] In some embodiments, about 20 mol% to less than about 50 mol% of the protein is covalently bound to the thermoplastic elastomer. In some embodiments, about 30 mol% to less than about 50 mol%, about 40 mol% to less than about 50 mol%, about 20 mol% to about 40 mol%, about 30 mol% to about 40 mol%, or about 20 mol% to about 30 mol% of the protein is covalently bound to the thermoplastic elastomer.

[0140] In some embodiments, about 20% to less than about 50% by weight of the protein is covalently bound to the thermoplastic elastomer. In some embodiments, about 30% to less than about 50% by weight, about 40% to less than about 50% by weight, about 20% to about 40% by weight, about 30% to about 40% by weight, or about 20% to about 30% by weight of the protein is covalently bound to the thermoplastic elastomer.

[0141] In some embodiments, a detectable amount of protein to less than about 20 mole % of the protein is covalently bound to the thermoplastic elastomer. In some embodiments, a detectable amount of protein to less than about 10 mole % of the protein is covalently bound to the thermoplastic elastomer.

[0142] In some embodiments, a detectable amount of protein to less than about 20% by weight of the protein is covalently bound to the thermoplastic elastomer. In some embodiments, a detectable amount of protein to less than about 10% by weight of the protein is covalently bound to the thermoplastic elastomer.

[0143] In some embodiments, the protein is not covalently bound to the thermoplastic elastomer.

[0144] In some embodiments, the thermoplastic protein elastomer composite material described herein can be subjected to finishing treatments identical or similar to those for processing natural leather. The process for processing natural leather generally has three steps: preparation of rawhide, tanning, retanning, fatting and finishing. Tanning can be carried out in many well-known ways, including contacting the thermoplastic protein elastomer composite material with vegetable tanning agent, blocked isocyanate compound, chromium compound, aldehyde, synthetic tanning agent, natural resin, tanning natural oil or modified oil. Blocked isocyanate compound can include X-tan. Vegetable tannin can include tannin based on pyrogallol or catechol, such as oak bowl, mimosa, ten, Tara, oak, pine, sumac, broken axe tree and chestnut tannin. Chrome tanning agent can include chromium salt, such as chromium sulfate. Aldehyde tanning agent can include glutaraldehyde and oxazolidine compound. Syntans may include aromatic polymers, polyacrylates, polymethacrylates, copolymers of maleic anhydride and styrene, condensation products of formaldehyde with melamine or dicyandiamide, lignin, and natural cereal flours.

[0145] In order to tan the composite material, the pH of the material can be adjusted in the presence of 10% salt (e.g., sodium chloride, sodium sulfate or sodium salt), for example, reduced to a pH in the range of about 2.5 to about 3.0, to allow the tanning agent to penetrate. After penetration, the pH of the composite material can be adjusted again, for example, raised to a pH in the range of about 3.5 to about 4.0, to fix the tanning agent. In some embodiments, the composite material can be immersed in a bath of chromium sulfate (III) comprising 2% by weight (based on the weight of the protein injected into the composite material), and the pH can be adjusted according to the needs of penetration and fixation. For example, for 10 grams of a composite material with 10% by mass protein, 0.02 grams of chromium sulfate (III) powder can be dissolved in enough water to cover the composite material in the container (the amount of water will depend on the size of the container). The composite material can then be added to the container, and the container can be stirred, for example, on an orbital oscillator with 50 rpm. Stirring can be carried out at a pH of about 2.8 to about 3.2, and continues for a time sufficient to allow chromium sulfate (III) to penetrate into the composite material. After infiltration, the pH of the bath can be increased and fixation of the chromium (III) sulfate can be performed at a pH between about 3.8 and about 4.2. The duration of the fixation step can be selected to achieve the desired color of the composite material.

[0146] In some embodiments, after tanning, the thermoplastic protein elastomer composite material may be retanned. Retanning refers to post-tanning treatment. Such treatments may include second tanning, wetting, squeezing, dehydration, neutralization, addition of colorants (such as dyes), fatliquoring, fixing unbound chemicals, peeling, rewetting, softening and / or grinding.

[0147] In some embodiments, colorants can be incorporated into thermoplastic protein elastomer composites. In some embodiments, colorants can be incorporated into the protein before mixing with the thermoplastic elastomer. In some embodiments, the colorant reacts with the protein before the protein reacts with the reactive thermoplastic elastomer.

[0148] In some embodiments, the colorant may be a dye. In some embodiments, the dye may include one or more chromophores containing reactive side groups capable of forming covalent bonds. These dyes can achieve high wash fastness and a wide range of bright tones. Exemplary dyes include but are not limited to sulfate ethyl sulfone (Remazol), vinyl sulfone and acrylamide dyes. In some embodiments, the dye may be anionic dyes. Exemplary anionic dyes include but are not limited to azo, stilbene, phthalocyanine and dioxazine.

[0149] In some embodiments, about 0.01% to about 7.5% by weight of the dye, based on the weight of the protein, may be used. In some embodiments, the weight percentage of the dye, based on the weight of the protein, may be about 0.01% to about 7.5%, about 0.01% to about 5%, about 0.01% to about 3%, about 0.01% to about 1%, about 0.01% to about 0.5%, about 0.01% to about 0.1%, about 0.1% to about 7.5%, about 0.1% to about 5%, about 0.1% to about 3% , about 0.1 wt % to about 1 wt %, about 0.1 wt % to about 0.5 wt %, about 0.5 wt % to about 7.5 wt %, about 0.5 wt % to about 5 wt %, about 0.5 wt % to about 3 wt %, about 0.5 wt % to about 1 wt %, about 1 wt % to about 7.5 wt %, about 1 wt % to about 5 wt %, about 1 wt % to about 3 wt %, about 3 wt % to about 7.5 wt %, about 3 wt % to about 5 wt %, or about 5 wt % to about 7.5 wt %.

[0150] In some embodiments, the lubricant used during greasing includes fat, bio-oil, mineral oil or synthetic oil, cod oil, sulfonated oil, polymer, organofunctional siloxane or other hydrophobic compounds or reagents for greasing conventional leather or their mixture.Other lubricants include surfactants, anionic surfactants, cationic surfactants, cationic polymer surfactants, anionic polymer surfactants, amphiphilic polymers, fatty acids, modified fatty acids, nonionic hydrophilic polymers, nonionic hydrophobic polymers, polyacrylic acid, polymethacrylic acid, acrylic resins, natural rubber, synthetic rubber, resins, amphiphilic anionic polymers and copolymers, amphiphilic cationic polymers and copolymers and their mixtures, and emulsions or suspensions of these materials in water, alcohol, ketones and other solvents.Lubricants can be incorporated in any amount to give leather-like properties (such as flexibility, brittleness reduction, durability or water resistance).In some embodiments, the amount of the lubricant applied to the thermoplastic protein elastomer composite can be in the range of about 0.1 weight % to about 60 weight % of the thermoplastic protein elastomer composite. For example, the amount of lubricant applied may be about 0.1 wt %, about 1 wt %, about 5 wt %, about 10 wt %, about 15 wt %, about 20 wt %, about 25 wt %, about 30 wt %, about 35 wt %, about 40 wt %, about 45 wt %, about 50 wt %, about 55 wt %, or about 60 wt %, or within a range having any two of these values ​​as endpoints, inclusive.

[0151] In some embodiments, water can be removed by filtration, evaporation, freeze drying, solvent exchange, vacuum drying, convection drying, heating, radiation or microwave treatment, or by other known methods for water removal.

[0152] The tanned thermoplastic protein elastomer composite can be mechanically or chemically finished. For example, mechanical finishing can include polishing the composite to produce a shiny surface; ironing and electroplating the composite to achieve a flat, smooth surface; stamping the composite to form a three-dimensional print or pattern on the surface of the material; or tumbling the composite to provide a more pronounced grain and smooth surface. Chemical finishing can involve applying a film, natural or synthetic coating, or other treatment. The chemical treatment can be applied, for example, by spraying, curtain coating, roller coating, or reverse transfer coating.

[0153] Method for preparing thermoplastic elastomer composite material

[0154] Most plastic products are prepared by so-called "hot compounding" techniques, where the ingredients in a composition are combined under heat and shear, which produces the plastic in a molten state (melt), which is shaped into the desired product, cooled, and allowed to develop final properties of strength and integrity. Hot compounding methods include, but are not limited to, calendaring, extrusion, spraying, and compression molding.

[0155] The present disclosure provides a method for preparing a thermoplastic protein elastomer composite, the method comprising compounding a mixture comprising:

[0156] (a) a protein comprising a first functional group, wherein the protein is a protein other than collagen, gelatin, or any combination thereof;

[0157] (b) a reactive thermoplastic elastomer comprising a second functional group capable of reacting with the first functional group during compounding; and

[0158] (c) Softeners.

[0159] The present disclosure also provides a method for preparing a thermoplastic protein elastomer composite, the method comprising compounding a mixture comprising:

[0160] (a) Protein;

[0161] (b) thermoplastic elastomers; and

[0162] (c) softeners,

[0163] wherein, after compounding, the protein is present in a first phase within the composite and the thermoplastic elastomer is present in a second phase within the composite, and wherein the first phase and the second phase are co-continuous.

[0164] In some embodiments, compounding may be carried out at a temperature in the range of about 50° C. to about 120° C., about 50° C. to about 150° C., about 50° C. to about 180° C., about 80° C. to about 150° C., about 80° C. to about 125° C., about 80° C. to about 100° C., about 100° C. to about 180° C., about 100° C. to about 150° C., about 100° C. to about 125° C., about 125° C. to about 180° C., about 100° C. to about 150° C., or about 150° C. to about 180° C. In some embodiments, compounding may be carried out at a temperature in the range of about 125° C. to about 150° C. In some embodiments, compounding may be carried out at a temperature in the range of about 140° C.

[0165] In some embodiments, compounding can be carried out with a stirring speed of about 20 rpm to about 1000 rpm, about 20 rpm to about 500 rpm, about 20 rpm to about 250 rpm, about 20 rpm to about 200 rpm, about 20 rpm to about 100 rpm, about 100 rpm to about 1000 rpm, about 100 rpm to about 500 rpm, about 100 rpm to about 250 rpm, about 100 rpm to about 200 rpm, about 200 rpm to about 1000 rpm, about 200 rpm to about 500 rpm, about 200 rpm to about 250 rpm, about 250 rpm to about 1000 rpm, about 250 rpm to about 500 rpm, or about 500 rpm to about 1000 rpm. In some embodiments, compounding can be carried out with a stirring speed of about 20 rpm to about 100 rpm.

[0166] In some embodiments, compounding can be performed over a period of about 1 minute to about 20 minutes, about 1 minute to about 15 minutes, about 1 minute to about 10 minutes, about 1 minute to about 5 minutes, about 5 minutes to about 20 minutes, about 5 minutes to about 15 minutes, about 5 minutes to about 10 minutes, about 10 minutes to about 15 minutes, about 10 minutes to about 20 minutes, or about 15 minutes to about 20 minutes. In some embodiments, compounding can be performed over a period of about 15 minutes.

[0167] In some embodiments, the method can include mixing the protein and the softener to form a protein solution, and compounding the protein solution and the reactive thermoplastic elastomer to form a thermoplastic protein elastomer composite.

[0168] In some embodiments, the compounded mixture further comprises a catalyst configured to promote a reaction between the second functional group and the first functional group during compounding. In some embodiments, the catalyst may be a base. In some embodiments, the catalyst may be 1,4-diazabicyclo[2.2.2]octane (DABCO), quinuclidine ((1-azabicyclo[2.2.2]octane), DBU (1,8-diazabicyclo[5.4.0]undec-7-ene), DBN (1,5-diazabicyclo[4.3.0]non-5-ene), pyridine, or DMAP (4-dimethylaminopyridine).

[0169] In some embodiments, the compounded mixture further comprises a cross-linking agent configured to form a covalent bond between a protein and a polymer, between two protein molecules, between two polymer molecules, or a combination thereof. In some embodiments, the cross-linking agent is EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide). In some embodiments, the cross-linking agent is a compound comprising an aryl azide, a diazirine, an N-hydroxysuccinimide (NHS) ester, an imidate, a hydrazide, or a combination thereof.

[0170] In some embodiments, the method further comprises heat pressing the thermoplastic protein elastomer composite to form a thermoplastic protein composite film.

[0171] In some embodiments, the thermoplastic protein elastomer composite material can be hot pressed into film. In some embodiments, the thickness of the film can be in the range of about 0.5mm to about 50mm, including sub-ranges. In some embodiments, the thickness of the film can be about 0.5mm, about 1mm, about 2mm, about 3mm, about 4mm, about 5mm, about 10mm, about 15mm, about 20mm, about 25mm, about 30mm, about 35mm, about 40mm, about 45mm, or about 50mm. In some embodiments, the thickness of the film can be about 0.5mm to about 5mm, about 2mm to about 10mm, about 5mm to about 20mm, about 15mm to about 30mm, about 25mm to about 40mm, or about 35mm to about 50mm.

[0172] In some embodiments, the method also includes attaching the thermoplastic protein composite material to the fabric. In some embodiments, the fabric can be made of one or more natural fibers, such as fibers made of cotton, linen, silk, wool, kenaf, flax, cashmere, angora goat wool, bamboo, bast, hemp, soybean, seaweed fiber, milk or milk protein, spider silk, chitosan, mycelium, cellulose (including bacterial cellulose) or wood. In some embodiments, the fabric can be made of one or more synthetic fibers, such as fibers made of polyester, nylon, aramid, polyolefin fibers (such as polyethylene, polypropylene), rayon, lyocell, viscose, antimicrobial yarn (AMY), Sorbtek, nylon, elastomers such as LYCRA, spandex elastic fibers or ELASTANE, polyester-polyurethane copolymers, aramid, carbon (including carbon fibers and fullerenes), glass, silicon, minerals, metals or metal alloys (including those containing iron, steel, lead, gold, silver, platinum, copper, zinc and titanium) or mixtures thereof.

[0173] Articles comprising thermoplastic elastomer composites

[0174] The present disclosure also provides articles comprising the thermoplastic elastomer composites described herein. Examples of articles comprising the thermoplastic protein elastomer composites include, but are not limited to, footwear, clothing, gloves, furniture, vehicle decoration and other goods and products such as coats, coats, jackets, shirts, trousers, pants, shorts, swimwear, underwear, uniforms, badges or letters, costumes, ties, skirts, dresses, blouses, leggings, gloves, mittens, shoes, shoe parts (such as soles, shoe waists, shoe tongues, shoe collars, welts and shoe counters), dress shoes, athletic shoes, running shoes, casual shoes, Shoes, parts of sports shoes, running shoes or casual shoes (such as toes, cleats, outsoles, insoles, uppers, laces, eyelets, collars, pads, Achilles grooves, heels and counters), fashion shoes or women's shoes and shoe parts (such as uppers, outer soles, toe caps, cleats, decorations, vamps, pads, insoles, midsoles, platforms, counters, and heels or high heels), boots, sandals, buttons, sandals, hats, masks, head covers, headbands, headscarves and belts; jewelry, such as bracelets, watch straps and necklaces; gloves, umbrellas, canes, wallets, mobile phone or wearable computer covers, purses, backpacks, suitcases, handbags, folios, folders, boxes and other personal effects; sports, athletic, hunting or recreational gear, such as harnesses, bridles, reins, bits, leads, mittens, tennis rackets, golf clubs, polo, hockey or lacrosse gear, chess and game boards, medicine balls, children's soccer, baseball and other types of balls, and toys; book bindings, book covers, picture frames or works of art; furniture and residential, office or other interior or exterior furnishings, including chairs, chairs, doors, seats, ottomans, room dividers, coasters, mouse pads, desk blotters, or other mats, tables, beds, floors, wall or ceiling coverings, floor coverings, automobile, boat, aircraft and other vehicle products, including seats, headrests, upholstery, paneling, steering wheels, joystick or control coverings and other wrappings or coverings.

[0175] The embodiments discussed herein will be further illustrated in the following examples.It should be understood that these examples are not limited to the embodiments described above.

[0176] Example

[0177] Example 1: Compounding of gelatin / 50 wt% glycerol and epoxidized natural rubber

[0178] 150 g of gelatin (gel strength 300, type A, from Sigma-Aldrich) was added to 850 g of deionized water, heated to 50°C on a hot plate, and mixed with an impeller blade for approximately 30 minutes to dissolve the gelatin. 75 g of glycerol was then added to the solution and mixed for an additional 5 minutes to obtain a gelatin solution with 50% by weight glycerol based on the weight of glycerol relative to the weight of gelatin. The gelatin solution was then cast in a wide pan at a thickness of less than 2 cm and dried at 45°C for 2 days. After drying, the cast solution was conditioned at ambient conditions (23°C and 50% relative humidity) for 1 day.

[0179] After conditioning, 25 g of epoxidized natural rubber-50 (ENR-50, 50% olefin epoxidation) was loaded into the CW ATR PLASTI- The mixture was placed in a compounder and compounded at 140°C for 10 minutes at 60 revolutions per minute (rpm). Then, 15 g of the conditioned and cast gelatin solution was loaded into the compounder. Immediately after the solution was added, 0.12 g of 1,4-diazabicyclo[2.2.2]octane (DABCO) was loaded into the compounder, the rpm of the compounder was set to 45, and the cast gelatin solution and DABCO were compounded with ENR-50 for 3 minutes to form a composite compound. During this period, the temperature of the compound was approximately 130°C. The torque in the compounder stabilized at 10 N*m at the end of the three-minute compounding period. This steady state indicates that the compounding of the components was successful under the mixing conditions used. The resulting composite compound was scraped out of the compounder and placed in an Auto Series Heat press machine The sheets were pressed between each other at 120°C and 4 tons of pressure for 5 minutes to produce a thin, flat spring disk.

[0180] Example 2: Compounding of SPI / 50 wt% glycerol and epoxidized natural rubber

[0181] Test A :

[0182] 170 g of water was warmed to 50°C on a hot plate and NaOH was added to form a 0.05 N NaOH solution. Then 30 g of soy protein isolate (SPI; XT 221D-IP; DuPont; available from Solae LLC) and the solution was mixed with an impeller blade for approximately 30 minutes. After mixing for 30 minutes, 15 g of glycerol was added and the solution was mixed for an additional 5 minutes to produce an SPI solution having 50% by weight glycerol based on the weight of glycerol relative to the weight of SPI. The SPI solution was then cast in a wide pan at a thickness of less than 2 cm and dried at 45° C. for 2 days. After drying, the cast solution was conditioned at ambient conditions (23° C. and 50% relative humidity) for 1 day.

[0183] After conditioning, 25 g of ENR-50 was loaded into the CW ATR PLASTI- The compounder was placed in a 140°C compounder and compounded at 60 rpm for 10 minutes. Then, 15 grams of the conditioned and cast SPI solution were loaded into the compounder. Immediately after the addition of the solution, 0.12 g of DABCO was added, the rpm of the compounder was set to 30, and the solution and DABCO were compounded with ENR-50 for 5 minutes to form a composite compound. During this period, the temperature of the compound was about 135°C. The torque in the compounder stabilized at 9 N*m at the end of the five-minute compounding period. This steady state indicates that compounding occurred completely to the extent possible under the conditions used. The resulting compound was scraped out of the compounder and placed in an AutoSeries Heat press machine The sheets were pressed between each other at 120°C and 4 tons of pressure for 5 minutes to produce a thin, flat spring disk.

[0184] The resulting elastomeric disks were heterogeneous, with numerous large, dispersed SPI particles visible within the polymer matrix.

[0185] Test B

[0186] The elastic disk was prepared as described in Experiment A above, however, the compounding conditions were changed as follows. First, the total mass of the mixture comprising SPI solution, DABCO and ENR-50 was 50 g, with the component ratios remaining the same. Second, ENR-50 was mixed by itself for 20 minutes to form a melt before compounding with the SPI solution and DABCO. Third, the ENR-50 melt was cooled to 110°C before adding the SPI solution, so that the mixing temperature was approximately 115°C. Fourth, the composite compound comprising SPI solution, DABCO and ENR-50 was compounded for 10 minutes instead of 5 minutes. During the 10 minutes of compounding, the torque stabilized at 11 N*m. This stable state indicates that the compounding of the components was successful under the conditions used. The resulting elastic disk was more uniform than the elastic disk produced in Experiment A, but there were still many visible dispersed SPI particles.

[0187] Example 3: Compounding and dyeing of SPI / 100 wt% glycerol with epoxidized natural rubber

[0188] The SPI solution was prepared using 100 wt% glycerol instead of 50 wt% glycerol as described in Example 2. The SPI solution, DABCO and ENR-50 were mixed to form a compound in the same manner as described in Example 2, Test B. The torque in the compounder was stabilized at 10 N*m during compounding.

[0189] The resulting elastomeric disc is visually uniform. The composite compound of the elastomeric disc is a co-continuous phase of SPI and ENR-50, a finely mixed dispersed phase of SPI and ENR-50 containing small dispersed SPI particles, or a mixture of the two. The elastomeric disc is also translucent and uniformly dyed when dyed using the following procedure. The elastomeric disc swells significantly in water, and it appears that the elastomeric disc loses mass after swelling in water, as the thickness of the elastomeric disc decreases significantly after drying. This thinning indicates that the SPI within the elastomeric disc is exposed to water, and most likely, glycerol (and possibly SPI) leached from the elastomeric disc into the water. Since the SPI / glycerol phase morphology may be co-continuous, there is a possibility that SPI or glycerol has leached from the elastomeric disc. However, the elastomeric disc is still flexible after swelling and drying, but is slightly less flexible than before dyeing.

[0190] The plywood was dyed using the following procedure. A 1% (w / w) acid dye solution was prepared by dissolving 2 g of acid navy dye "3140" (Limonta) in 198 g of deionized (DI) water. A square plywood (63 mm x 63 mm and approximately 0.5 mm to 1.5 mm thick) was placed in the dye bath and allowed to react at room temperature (23°C) on a shaker at 60 rpm for 18 hours. The plywood was then removed from the bath and hand washed under deionized water. After washing, the plywood was placed in a pure deionized water bath on a shaker at 60 rpm for another 4 hours. Finally, the plywood was dried in a laboratory fume hood at ambient temperature for 2 days.

[0191] Example 4: Compounding of purified cellulase AC20P / 50 wt% glycerol with epoxidized natural rubber

[0192] Cellulase AC20P (Sunson Industry Group Co.) was purified using the following procedure. Cellulase was added to water at a concentration of 25 wt% and mixed until a homogeneous solution was formed. The solution was centrifuged in a HSD-1 disc stack centrifuge. The feed flow rate was 81 L / h and the discharge timer was set to 180 s. The centrifuge (light phase) was collected and used with a 50 kDa The product was further purified by ultrafiltration using a TFF Accela slide with a PES spiral wound filter (MQ-2B-3838). The feed flow rate was 220 L / min, the feed pressure was 50 psi, and water was used as the diafiltration buffer. Once the ultrafiltration was complete, the resulting retentate solution was concentrated to 25% total solids. The retentate solution was spray dried in a Lab2 spray dryer. The aspirator speed was 1500 rpm to 2000 rpm, the atomization pressure was 1.5 bar to 2 bar, the inlet temperature was 220° C., and the outlet temperature was 90° C. Once drying was complete, the purified cellulase AC20P in powder form was collected from the main drying chamber and used as described below.

[0193] 60 g of purified cellulase AC20P was added to 340 g of deionized water and mixed with an impeller blade for approximately 30 minutes to dissolve the purified cellulase. 30 g of glycerol was then added to the solution and mixed for an additional 5 minutes to obtain a purified cellulase solution with 50% by weight glycerol based on the weight of glycerol relative to the weight of purified cellulase. The cellulase solution was then cast in a wide pan at a thickness of less than 2 cm and dried at 45° C. for 2 days. After drying, the cast solution was conditioned at ambient conditions (23° C. and 50% relative humidity) for 1 day.

[0194] After conditioning, 25g of ENR-50 was loaded into ATR Plasti- The ENR-50 was then cooled to 110°C and 15 g of the conditioned and cast purified cellulase solution was loaded into the compounder. Immediately after the addition of the solution, 0.12 g of DABCO was loaded into the compounder, the rpm of the compounder was set to 30, and the cellulase solution and DABCO were mixed with the ENR-50 for 5 minutes to form a composite compound. During this period, the temperature of the compound was approximately 135°C. The torque in the compounder stabilized at 9 N*m at the end of the 5 minute compounding period. This steady state indicates that the formed compound was fully compounded to the extent possible under the conditions used. The resulting composite compound was scraped out of the compounder and placed in an Auto Series Heat press machine The sheets were pressed between each other at 120°C and 4 tons of pressure for 5 minutes to produce a thin, flat spring disk.

[0195] The resulting puck was very heterogeneous with many large dispersed cellulase particles. The puck was not dyed.

[0196] Example 5: Compounding of AC20P Cellulase / 100 wt% Glycerol with Epoxidized Natural Rubber

[0197] As described in Example 4, an unpurified cellulase solution was prepared using 100 wt % glycerol instead of 50 % glycerol and using the raw cellulase AC20P without a purification step. The spring disk was prepared as described in Example 4 above, however the compounding conditions were changed as follows. First, the mass of ENR-50 used was 31.25 g. Second, ENR-50 was compounded at 140°C at 60 rpm for 15 minutes. Third, 18.75 g of an unpurified cellulase solution of 100 wt % glycerol was used. Fourth, mixing was performed at 60 rpm for 10 minutes at an approximate temperature of 115°C. The torque in the compounder stabilized at 10 N*m at the end of the 10 minute compounding period. This indicates that the formed compound was fully compounded to the extent possible under the conditions used.

[0198] The resulting plywood was visually uniform. The composite compound of the plywood was a co-continuous phase of cellulase and ENR-50, a finely mixed dispersed phase of cellulase and ENR-50 containing small dispersed cellulase particles, or a mixture of both. A small amount of streaking occurred, which may be attributed to impurities. The plywood was also translucent and uniformly dyed when dyed using the dyeing procedure described in Example 3 above. The solution with a higher weight % of glycerol appears to have formed a cellulase solution with a lower viscosity compared to the plywood prepared in Example 4, which had a more viscous and more dispersed phase, which may have resulted in a more co-continuous or well-compounded plywood. The plywood swelled slightly in water, but there was little noticeable change in material feel or flexibility.

[0199] Example 6: Compounding of unpurified AC20P cellulase added directly to epoxidized natural rubber

[0200] 31.25g of ENR-50 ATR PLASTI- Compounding was performed in a compounder at 140°C at 60 rpm for 15 minutes. ENR-50 was then cooled to 110°C at 0 rpm and 18.75 g of Cellulase AC20P (unpurified) was added and compounded at an approximate temperature of 115°C at 60 rpm for 10 minutes. The torque in the compounder stabilized at 13 N*m at the end of the 10 minute compounding period. This indicates that compounding occurred under the conditions used. The resulting composite compound was mixed at 140°C at 150°C. The sheets were pressed at a temperature of 120°C, a force of 4 tons and a duration of 5 minutes to form a spring disk.

[0201] The resulting puck was visually uniform and less transparent than the pucks of the other examples. The opacity of the cellulase solution and its inability to flow by itself (due to its hardness / viscosity) indicated that the final phase structure had dispersed cellulase particles, but finely dispersed, unlike some of the pucks described in the previous examples. The puck dyed uniformly and was water stable when dyed using the dyeing procedure described in Example 3 above. The puck swelled less than the other cellulase pucks. This swelling behavior may be due to the lower ability of the dispersed cellulase to come into contact with water and swell.

[0202] Example 7: Compounding of Uncast Glycerol, AC20P Cellulase and Epoxidized Natural Rubber

[0203] 9.275 g of AC20P cellulase powder (without any purification step), 9.375 g of glycerol (100 wt % glycerol relative to the weight of cellulase) and 31.25 g of ENR-50 were loaded into ATR PLASTI- The loading was performed as follows. ENR-50 was compounded in the compounder at 150°C at 60 rpm for 15 minutes. The compounder was then stopped and the ENR-50 was allowed to cool to 110°C. The compounder was then restarted at 60 rpm and glycerin and cellulase were added independently. The mixture of ENR-50, glycerin and cellulase was then compounded at approximately 115°C for 10 minutes. During the 10 minute compounding period, the torque stabilized at 7.5 N*m. The resulting compound was placed in a The sheets were pressed at a temperature of 120°C, a force of 4 tons and a duration of 5 minutes to form a spring disk.

[0204] The resulting puck was highly heterogeneous with large areas of glycerol that appeared to be mixed with neither the cellulase nor the ENR- 50. The puck was not tested for dyeing or water stability.

[0205] Example 8: Compounding of pea protein isolate 870P / 50 wt% glycerol and epoxidized natural rubber

[0206] 150g Pea protein 870 (Ingredion) was added to 850 g of deionized water and mixed with an impeller blade for approximately 30 minutes. 75 g of glycerol was then added and mixed for an additional 5 minutes to form a pea protein solution with 50% glycerol by weight based on the weight of glycerol relative to the weight of pea protein. The pea protein solution was then poured into a wide pan at a thickness of less than 2 cm and dried at 45° C. for 2 days. After drying, the poured pea protein solution was conditioned for 1 day under ambient conditions (23° C. and 50% relative humidity). When dried, the pea protein solution was hard and cracked significantly in the container used for drying, but appeared to be uniform.

[0207] 25g of ENR-50 ATR Plasti- The mixture was compounded in a compounder at 60 rpm at 140°C for 10 minutes. 15 g of the cast pea protein solution was loaded into the compounder. 0.12 g of DABCO was loaded into the compounder immediately after the protein solution was added, and the contents of the compounder were compounded at an approximate temperature of 135°C for 5 minutes at 30 rpm. The resulting compound was then heated at 120°C and 4 tons. The sheets were pressed for 5 minutes between each other to form a plywood. The resulting plywood was clearly not uniform, with many scattered areas of pea protein. However, when dyed using the dyeing procedure described in Example 3 above, the plywood did dye uniformly, probably because ENR-50 itself is dyeable. The plywood was also water stable, with no noticeable changes after soaking in a water bath.

[0208] Example 9: Compounding of Zein / 50 wt% Glycerol and Epoxidized Natural Rubber

[0209] 150g of zein powder (Sigma-Aldrich) was added to 850g of deionized water and mixed with impeller blades for about 30 minutes. Then 75g of glycerol was added and mixed for another 5 minutes to obtain a zein mixture with 50% by weight glycerol based on the weight of glycerol relative to the weight of zein. The zein particles are insoluble in water, but clearly remain suspended and fall rapidly when agitation is stopped. The zein mixture is then poured in a wide pan and dried at 45°C for 2 days with a thickness less than 2cm. After drying, the poured zein mixture is conditioned for 1 day under ambient conditions (23°C and 50% relative humidity). After drying, the protein mixture is very brittle (not solid and easily broken) and does not form a uniform film. The zein particles are still the same size as those particles in the zein powder initially used to form the protein mixture, and may be gently held together by glycerol.

[0210] 31.25g of ENR-50 ATR Plasti- The mixture was mixed in a compounder at 60 rpm at 140°C for 15 minutes. The compounder was then stopped and the ENR-50 was allowed to cool to 110°C. Then, 18.75 g of the cast zein mixture was loaded into the compounder, and the ENR-50 and zein mixture were mixed at 60 rpm at about 115°C for 10 minutes to form a composite compound. The torque stabilized at 10 N*m at the end of the 10 minute mixing period. This steady state indicates that the compound was mixed as completely as possible under the conditions used. The resulting compound was then The sheets were pressed between each other at a temperature of 120° C. and a force of 4 tons for 5 minutes to form a padded disc. The resulting padded disc appeared to be uniform and relatively opaque, similar to the padded disc described in Example 6. Similar to Example 6, the composite compound may include highly dispersed protein particles.

[0211] The puck dyed uniformly when dyed using the dyeing procedure described above in Example 3. In addition, very little swelling in water was evident, probably because in a very dispersed state, the water was unable to reach the zein to cause significant swelling. After soaking in water, the final properties of the puck appeared to be the same as the puck described in Example 6.

[0212] Example 10: Compounding of Egg White Albumin / 50 wt% Glycerol and Epoxidized Natural Rubber

[0213] 30 g of egg white albumin powder (Sigma-Aldrich) was added to 170 g of deionized water and mixed with an impeller blade for about 30 minutes to dissolve the egg white albumin powder. 15 g of glycerol was then added and mixed for another 5 minutes to obtain an albumin solution with 50% by weight glycerol based on the weight of glycerol relative to the weight of albumin. The protein solution was then poured into a wide pan at a thickness of less than 2 cm and dried at 45° C. for 2 days. After drying, the cast protein solution was conditioned at ambient conditions (23° C. and 50% relative humidity) for 1 day. After drying, the protein solution was uniform and relatively hard.

[0214] The composite compound was prepared as described in Example 9 using the albumin solution instead of the zein solution. The torque was stabilized at 10 N*m during the 10 minute mixing period. The composite compound was then The sheets were pressed between each other at a temperature of 120°C with a force of 4 tons for 5 minutes. The resulting puck was highly non-uniform with many protein particles found as large fragments with relatively straight edges throughout the polymer. Many of the particles appeared to burn from the process. The puck was not dyed.

[0215] Example 10: Complex viscosity test

[0216] The complex viscosity of three samples was tested at 100° C. and 120° C. The first sample was epoxidized natural rubber-50 (ENR-50, 50% olefinic bonds were epoxidized). The second sample was a cast and dried SPI solution prepared according to Example 2 ("SPI+50% glycerol"). The third sample was a cast and dried cellulase solution prepared according to Example 4 ("cellulase+50% glycerol"). Figure 1 The complex viscosity measured at 100°C is shown for all three samples. Figure 2 The complex viscosity measured at 120°C is shown for all three samples.

[0217] Although various embodiments have been described herein, they are presented by way of example only and not by way of limitation. It is apparent that, based on the teachings and guidance given herein, adjustments and modifications are intended to fall within the meaning and scope of equivalents of the disclosed embodiments. Therefore, it will be apparent to those skilled in the art that, without departing from the essence and scope of the present disclosure, various forms and details of changes may be made to the embodiments disclosed herein. The elements of the embodiments presented herein are not necessarily mutually exclusive, but are interchangeable to satisfy various situations as will be understood by those skilled in the art.

[0218] Embodiments of the present disclosure are described in detail herein with reference to the embodiments shown in the accompanying drawings, wherein similar figure numbers are used to indicate identical or functionally similar elements. References to "one embodiment," "embodiment," "some embodiments," "in certain embodiments," etc. indicate that the embodiments described may include specific features, structures, or characteristics, but each embodiment may not necessarily include specific features, structures, or characteristics. Moreover, such phrases do not necessarily refer to the same embodiment. In addition, when describing specific features, structures, or characteristics in conjunction with an embodiment, whether or not explicitly described, it is believed that a person skilled in the art will be able to implement such features, structures, or characteristics in conjunction with other embodiments.

[0219] The examples are intended to illustrate rather than limit the present disclosure. Other suitable modifications and adaptations of the various conditions and parameters normally encountered in the art and which will be apparent to those skilled in the art are within the spirit and scope of the present disclosure.

[0220] It should be understood that the phraseology or terminology employed herein is for the purpose of description and not limitation.The breadth and scope of the present disclosure should not be limited by any of the above-described exemplary embodiments, but should be defined in accordance with the following claims and their equivalents.

Claims

1. A thermoplastic protein elastomer composite comprising a protein containing at least one first reactive functional group, the protein having been reacted with a thermoplastic elastomer containing at least one second reactive functional group The protein is a protein other than collagen, gelatin or any combination thereof.

2. The composite material of claim 1, wherein the protein and the thermoplastic elastomer are covalently bonded together by reaction of the first reactive functional group and the second reactive functional group.

3. The composite material according to claim 1 or 2, wherein the protein is selected from the group consisting of soy protein, cellulase, corn protein, egg white albumin and pea protein. 4 . The composite material according to claim 1 , wherein the first reactive functional group is an amino group, a hydroxyl group or a carboxylic acid group. 5 . The composite material according to claim 1 , wherein the second reactive functional group is maleic anhydride, epoxy, silane or glycidyl. The composite material according to claim 5 , wherein the second reactive functional group is an epoxy group.

7. The composite material according to any one of claims 1 to 6, wherein the thermoplastic elastomer is selected from the group consisting of maleated polyethylene, maleated polypropylene, maleated styrene-ethylene-butylene-styrene block copolymers, maleated styrene-butadiene-styrene block copolymers, maleated styrene-ethylene-propylene-styrene block copolymers, maleated ethylene-propylene rubber, epoxidized natural rubber, methyl methacrylate grafted natural rubber, polyhydroxyalkanoates and polyurethanes.

8. The composite material according to any one of claims 1 to 6, wherein the thermoplastic elastomer is epoxidized natural rubber.

9. The composite material of claim 8, wherein the epoxidized natural rubber comprises about 50% epoxidized olefinic bonds.

10. The composite material according to any one of claims 1 to 9, wherein the composite material is a film.

11. A method for preparing a thermoplastic protein elastomer composite material, the method comprising: A mixture comprising: (a) a protein comprising a first functional group, wherein the protein is a protein other than collagen, gelatin, or any combination thereof; (b) a reactive thermoplastic elastomer comprising a second functional group capable of reacting with the first functional group during compounding; and (c) Softeners.

12. The method of claim 11, wherein the protein is selected from the group consisting of soy protein, cellulase, zein, egg white albumin, and pea protein.

13. The method according to claim 11 or 12, wherein the softening agent is a protein softening agent.

14. The method of claim 13, wherein the protein softener is an alcohol.

15. The method of claim 14, wherein the alcohol is glycerol.

16. The method according to any one of claims 11 to 15, comprising: mixing the protein and the softening agent to form a protein solution, and The protein solution and the reactive thermoplastic elastomer are compounded to form the thermoplastic protein elastomer composite.

17. The method of any one of claims 11 to 16, wherein the mixture further comprises a catalyst configured to promote a reaction between the second functional group and the first functional group during compounding.

18. The method according to any one of claims 11 to 17, further comprising heat pressing the thermoplastic protein elastomer composite to form a thermoplastic protein composite film.

19. A method according to any one of claims 11 to 18, further comprising attaching the thermoplastic protein composite to a fabric.

20. An article comprising the composite material according to any one of claims 1 to 19.

21. A thermoplastic protein elastomer composite, comprising a protein blended with a thermoplastic elastomer, wherein the protein is present in a first phase within the composite and the thermoplastic elastomer is present in a second phase within the composite, and wherein the first phase and the second phase are co-continuous.

22. The composite material of claim 21, wherein from about 50% to about 99% of the protein is covalently bonded to the thermoplastic elastomer.

23. The composite material of claim 21, wherein from about 20% to less than about 50% of the protein is covalently bonded to the thermoplastic elastomer.

24. The composite material of claim 21, wherein a detectable amount of said protein to less than about 20% of said protein is covalently bound to said thermoplastic elastomer.

25. The composition material of claim 21, wherein the protein is not covalently bound to the thermoplastic elastomer.

26. The composite material of claim 21, wherein the protein and the thermoplastic elastomer are covalently bonded together by reaction of a first functional group on the protein and a second reactive functional group on the thermoplastic elastomer.

27. The composite material of any one of claims 21 to 26, wherein the protein is a protein other than collagen, gelatin or any combination thereof.

28. The composite material according to any one of claims 21 to 26, wherein the protein is selected from the group consisting of soy protein, cellulase and zein.

29. The composite material of any one of claims 21 to 28, wherein the thermoplastic elastomer is selected from the group consisting of maleated polyethylene, maleated polypropylene, maleated styrene-ethylene-butylene-styrene block copolymers, maleated styrene-butadiene-styrene block copolymers, maleated styrene-ethylene-propylene-styrene block copolymers, maleated ethylene-propylene rubber, epoxidized natural rubber, methyl methacrylate grafted natural rubber, polyhydroxyalkanoates and polyurethanes.

30. The composite material according to any one of claims 21 to 28, wherein the thermoplastic elastomer is epoxidized natural rubber.

31. The composite material of claim 30, wherein the epoxidized natural rubber comprises about 50% epoxidized olefinic bonds.

32. The composite material of any one of claims 21 to 31, wherein the composite material is a film.

33. The composite material of any one of claims 21 to 32, wherein at a temperature between about 50°C and about 180°C, the first phase has a first complex viscosity at a certain angular frequency and the second phase has a second complex viscosity at the angular frequency, Further, the first complex viscosity is no greater than the second complex viscosity by no more than one order of magnitude, and The first complex viscosity is less than the second complex viscosity by no more than one order of magnitude.

34. A method for preparing a thermoplastic protein elastomer composite material, the method comprising: A mixture comprising: (a) Protein; (b) thermoplastic elastomers; and (c) softeners, wherein, after compounding, the protein is present in a first phase within the composite and the thermoplastic elastomer is present in a second phase within the composite, and wherein the first phase and the second phase are co-continuous.

35. The method of claim 34, wherein the protein is a protein other than collagen, gelatin, or any combination thereof.

36. The method of claim 34, wherein the protein is selected from the group consisting of soy protein, cellulase, and zein.

37. A method according to any one of claims 34 to 36, wherein the softening agent is an alcohol.

38. The method of claim 37, wherein the alcohol is glycerol.

39. The method according to any one of claims 34 to 38, further comprising: mixing the protein and the softening agent to form a protein solution, and The protein solution and the thermoplastic elastomer are compounded to form the thermoplastic protein elastomer composite.

40. The method of any one of claims 34 to 39, further comprising heat pressing the thermoplastic protein elastomer composite to form a thermoplastic protein composite film.

41. A method according to any one of claims 34 to 40, further comprising attaching the thermoplastic protein composite to a fabric.

42. The method of any one of claims 34 to 41, wherein at a temperature between about 50°C and about 180°C, the first phase has a first complex viscosity at an angular frequency and the second phase has a second complex viscosity at the angular frequency, Further, the first complex viscosity is no greater than the second complex viscosity by no more than one order of magnitude, and The first complex viscosity is less than the second complex viscosity by no more than one order of magnitude.

43. A method according to any one of claims 34 to 42, wherein: After compounding, from about 50% to about 99% of the protein is covalently bound to the thermoplastic elastomer.

44. The method according to any one of claims 34 to 42, wherein: After compounding, from about 20% to less than about 50% of the protein is covalently bonded to the thermoplastic elastomer.

45. The method according to any one of claims 34 to 42, wherein: After compounding, a detectable amount of the protein to less than about 20% of the protein is covalently bound to the thermoplastic elastomer.

46. ​​A method according to any one of claims 34 to 42, wherein: After compounding, the protein is not covalently bonded to the thermoplastic elastomer.

47. A method according to any one of claims 34 to 42, wherein: After compounding, the protein and the thermoplastic elastomer are covalently bonded together through the reaction of the first functional group on the protein and the second reactive functional group on the thermoplastic elastomer.

48. An article comprising the composite material according to any one of claims 21 to 47.

49. A composite material according to any one of claims 22 to 24, wherein the percentage of the protein covalently bound to the thermoplastic elastomer is measured in mole %.

50. A composite material according to any one of claims 22 to 24, wherein the percentage of the protein covalently bound to the thermoplastic elastomer is measured in weight %.

51. The method of any one of claims 43 to 45, wherein the percentage of the protein covalently bound to the thermoplastic elastomer is measured in mole %.

52. The method of any one of claims 43 to 45, wherein the percentage of the protein covalently bound to the thermoplastic elastomer is measured in weight %.

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