Protein Polyurethane Alloy Materials

The content of the electronically submitted sequence listing in ASCII text file (Name: 4431_091PC01_Seglisting_ST26.xml; Size: 4,669 bytes; and Date of Creation: Aug. 10, 2023) filed with the application is herein incorporated by reference in its entirety.

This disclosure relates to materials comprising a protein polyurethane alloy comprising one or more proteins dissolved in a polyurethane. In particular embodiments, this disclosure relates to materials comprising a protein polyurethane alloy and a textile substrate. In some embodiments, the materials can be used to make a textile or fabric article, such as a textile or fabric article typically prepared from natural leather.

Leather is a versatile product used across many industries, including the furniture industry, where leather is regularly used as upholstery, the clothing industry, where leather is used to manufacture pants and jackets, the shoe industry, where leather is used to prepare casual and dress shoes, the luggage industry, the handbag and accessory industry, and in the automotive industry. The global trade value for leather is high, and there is a continuing and increasing demand for leather products. Despite leather's seeming ubiquity, there are variety of costs, constraints, and social concerns associated with producing natural leather. Foremost, natural leathers are produced from animal skins, and as such, requires raising and slaughtering livestock. Raising livestock requires enormous amounts of feed, pastureland, water, and fossil fuels and contributes to air and waterway pollution, through, for example, greenhouse gases like methane. Leather production also raises social concerns related to the treatment of animals. In recent years, there has also been a fairly well documented decrease in the availability of traditional high quality hides. For at least these reasons, alternative means to meet the demand for leather are desirable.

Further, other textile or fabric materials, such as cotton and spandex, are used across many industries, including the furniture industry and the clothing industry. The demand for such materials is high and there is a continuing need for improved textile and fabric materials.

The present disclosure provides materials comprising a protein polyurethane alloy. The materials can be applied in a variety of applications, including as a replacement for natural leather and in other textile and fabric applications.

A first embodiment (1) of the present disclosure is directed to a material comprising a textile; a protein polyurethane alloy disposed over the textile, the protein polyurethane alloy comprising a protein dissolved within a polyurethane; and about 1 wt % to about 16 wt % of one or more fatliquors.

In a second embodiment (2), the protein polyurethane alloy according to the first embodiment (1) comprises greater than 50 wt % of the protein.

In a third embodiment (3), the protein polyurethane alloy according to the first embodiment (1) comprises about 60 wt % to about 90 wt % of the protein.

In a fourth embodiment (4), the one or more fatliquors according to any one of embodiments (1)-(3) comprise a functionalized oil.

In a fifth embodiment (5), the one or more fatliquors according to any one of embodiments (1)-(3) are selected from the group consisting of: a sulfited fatliquor, a sulfated fatliquor, or a combination thereof.

In a sixth embodiment (6), the material according to any one of embodiments (1)-(5) has a modulus of elasticity of 9*10{circumflex over ( )}7 Pa or less.

In a seventh embodiment (7), the material according to any one of embodiments (1)-(5) has a modulus of elasticity of 6*10{circumflex over ( )}7 Pa or less.

An eighth embodiment (8) of the present disclosure is directed to a material comprising: a textile; a protein polyurethane alloy comprising a protein dissolved within a polyurethane; a first portion having a first protein polyurethane alloy density; and a second portion having a second protein polyurethane alloy density different from the first protein polyurethane alloy density.

In a ninth embodiment (9), in the material according to the eighth embodiment (8), the first protein polyurethane alloy density is less than or greater than the second protein polyurethane alloy density by 5% or more.

In a tenth embodiment (10), the first portion of the material according to the eighth embodiment (8) or the ninth embodiment (9) comprises a first protein polyurethane alloy layer and the second portion of the material according to the eighth embodiment (8) or the ninth embodiment (9) comprises a second a protein polyurethane alloy layer.

In a eleventh embodiment (11), in the material according to the tenth embodiment (10), the textile comprises a top surface and a bottom surface, the first protein polyurethane alloy layer is disposed over the top surface of the textile, and the second protein polyurethane alloy layer is disposed over the bottom surface of the textile.

In a twelfth embodiment (12), in the material according to the eighth embodiment (8) or the ninth embodiment (9), the first portion comprises the protein polyurethane alloy integrated into the textile at the first protein polyurethane alloy density, and the second portion comprises the protein polyurethane alloy integrated into the textile at the second protein polyurethane alloy density.

In a thirteenth embodiment (13), in the material according to the eighth embodiment (8) or the ninth embodiment (9), the textile comprises a first textile layer coupled to a second textile layer, the first portion comprises the protein polyurethane alloy integrated into the first textile layer at the first protein polyurethane alloy density, and the second portion comprises the protein polyurethane alloy integrated into the second textile layer at the second protein polyurethane alloy density.

In a fourteenth embodiment (14), the material according to any one of embodiments (8)-(13) further comprises a cross-linker selected from the group consisting of: an epoxy-based cross-linker, an isocyanate-based cross-linker, and a carbodiimide-based cross-linker.

In a fifteenth embodiment (15), the cross-linker according to the fourteenth embodiment (14) is a carbodiimide-based cross-linker.

A sixteenth embodiment (16) of the present disclosure is directed to an aqueous formulation comprising water; an aqueous polyurethane dispersion; a protein; about 4 wt % to about 10 wt % of one or more colored dyes; and a foam stabilizer.

In a seventeenth embodiment (17), the protein according to the sixteenth embodiment (16) is dissolved within the polyurethane of the polyurethane dispersion

An eighteenth embodiment (18) of the present disclosure is directed to a material comprising a textile; a protein polyurethane alloy integrated into the textile, the protein polyurethane alloy comprising a protein dissolved within a polyurethane; and about 100 wt % to about 250 wt % of one or more colored dyes, the wt % of the one or more colored dyes measured relative to the weight of the protein in the protein polyurethane alloy.

The indefinite articles “a,” “an,” and “the” include plural referents unless clearly contradicted or the context clearly dictates otherwise.

The terms “comprising” and “including” are open-ended transitional phrases. A list of elements following the transitional phrase “comprising” or “including” is a non-exclusive list, such that elements in addition to those specifically recited in the list can also be present. The phrase “consisting essentially of” limits the composition of a component to the specified materials and those that do not materially affect the basic and novel characteristic(s) of the component. The phrase “consisting of” limits the composition of a component to the specified materials and excludes any material not specified.

Where a range of numerical values comprising upper and lower values is recited herein, unless otherwise stated in specific circumstances, the range is intended to include the endpoints thereof, and all integers and fractions within the range. It is not intended that the disclosure or claims be limited to the specific values recited when defining a range. Further, when an amount, concentration, or other value or parameter is given as a range, one or more ranges, or as list of upper values and lower values, this is to be understood as specifically disclosing all ranges formed from any pair of any upper range limit or value and any lower range limit or value, regardless of whether such pairs are separately disclosed. Finally, when the term “about” is used in describing a value or an end-point of a range, the disclosure should be understood to include the specific value or end-point referred to. Whether or not a numerical value or end-point of a range recites “about,” the numerical value or end-point of a range is intended to include two embodiments: one modified by “about,” and one not modified by “about.”

As used herein, the term “about” refers to a value that is within ±10% of the value stated. For example, about 3 MPa can include any number from 2.7 MPa to 3.3 MPa. That said, if a percentage is listed and the value of that percentage cannot go above 100%, for example 100 wt % or 99 wt %, “about” does not modify the percentage to include values over 100%.

As used herein, a first layer described as “attached to” a second layer means that the layers are attached to each other either by direct contact and attachment between the two layers or via one or more intermediate adhesive layers. An intermediate adhesive layer can be any layer that serves to attach a first layer to a second layer.

As used herein, the phrase “disposed on” means that a first component (e.g., layer, alloy, or textile) is in direct contact with a second component. A first component “disposed on” a second component can be deposited, formed, placed, or otherwise applied directly onto the second component. In other words, if a first component is disposed on a second component, there are no components between the first component and the second component.

As used herein, the phrase “disposed over” means other components (e.g., layers or substrates) may or may not be present between a first component and a second component.

As used herein, a “bio-based polyurethane” is a polyurethane where the building blocks of polyols, such as diols and diacids like succinic acid, are derived from a biological material such as corn starch.

As used herein, the term “substantially free of” means that a component is present in a detectable amount not exceeding about 0.1 wt %.

As used herein, the term “free of” means that a component is not present in a blend or material (e.g., a protein polyurethane alloy), even in trace amounts.

As used herein “collagen” refers to the family of at least 28 distinct naturally occurring collagen types including, but not limited to collagen types I, II, III, IV, V, VI, VII, VIII, IX, X, XI, XII, XIII, XIV, XV, XVI, XVII, XVIII, XIX, and XX. The term collagen as used herein also refers to collagen prepared using recombinant techniques. The term collagen includes collagen, collagen fragments, collagen-like proteins, triple helical collagen, alpha chains, monomers, gelatin, trimers and combinations thereof. Recombinant expression of collagen and collagen-like proteins is known in the art (see, e.g., Bell, EP 1232182B1, Bovine collagen and method for producing recombinant gelatin; Olsen, et al., U.S. Pat. No. 6,428,978 and VanHeerde, et al., U.S. Pat. No. 8,188,230, incorporated by reference herein in their entireties) Unless otherwise specified, collagen of any type, whether naturally occurring or prepared using recombinant techniques, can be used in any of the embodiments described herein. That said, in some embodiments, the collagen described herein can be prepared using bovine Type I collagen. Collagens are characterized by a repeating triplet of amino acids, -(Gly-X-Y)n-, so that approximately one-third of the amino acid residues in collagen are glycine. X is often proline and Y is often hydroxyproline. Thus, the structure of collagen may consist of three intertwined peptide chains of differing lengths. Different animals may produce different amino acid compositions of the collagen, which may result in different properties (and differences in the resulting leather).

In some embodiments, the collagen can be chemically modified to promote solubility in water.

Any type of collagen, truncated collagen, unmodified or post-translationally modified, or amino acid sequence-modified collagen can be used as part of the protein polyurethane alloy.

In some embodiments, the collagen can be plant-based collagen. For example, the collagen can be a plant-based collagen made by CollPlant.

In some embodiments, a collagen solution can be fibrillated into collagen fibrils. As used herein, collagen fibrils refer to nanofibers composed of tropocollagen or tropocollagen-like structures (which have a triple helical structure). In some embodiments, triple helical collagen can be fibrillated to form nanofibrils of collagen.

In some embodiments, a recombinant collagen can comprise a collagen fragment of the amino acid sequence of a native collagen molecule capable of forming tropocollagen (trimeric collagen). A recombinant collagen can also comprise a modified collagen or truncated collagen having an amino acid sequence at least 70, 80, 90, 95, 96, 97, 98, or 99% identical or similar to a native collagen amino acid sequence (or to a fibril forming region thereof or to a segment substantially comprising [Gly-X-Y]n). In some embodiments, the collagen fragment can be a 50 kDa portion of a native collagen. Native collagen sequences include the amino acid sequences of Col1A1, Col1A2, and Col3A1, described by Accession Nos. NP_001029211.1, NP_776945.1 and NP_001070299.1, which are incorporated by reference. In some embodiments, the collagen fragment can be a portion of human collagen alpha-1(III) (Col3A1; Uniprot #P02461, Entrez Gene ID #1281). In some embodiments, the collagen fragment can be the amino acid sequence listed as SEQ ID NO: 1. In some embodiments, the collagen fragment can be the amino acid sequence listed as SEQ ID NO: 2. In some embodiments, the collagen fragment comprises an amino sequence having at least 80% sequence identity to SEQ ID NO: 2. Example proteins comprising at least 80% sequence identify to SEQ ID NO: 2 are disclosed in PCT/US2022/027016, the disclosure of which is incorporated herein by reference.

Methods of producing recombinant collagen and recombinant collagen fragments are known in the art. For example, U.S. Pub. Nos. 2019/0002893, 2019/0040400, 2019/0093116, and 2019/0092838 provide methods for producing collagen and collagen fragments that can be used to produce the recombinant collagen and recombinant collagen fragments disclosed herein. The contents of these four publications are incorporated by reference in their entirety.

Protein polyurethane alloys described herein can comprise a protein that is miscible with only one of a plurality of phases of a polyurethane, or a plurality of polyurethanes, with which it is blended. For example, in some embodiments, the protein polyurethane alloy can include a protein that is miscible with only the hard phase of the polyurethane, or the plurality of polyurethanes, having both a hard phase and a soft phase. Protein polyurethane alloys described herein can be free of or substantially free of protein in form of particles dispersed in a polyurethane. For example, in some embodiments, the protein polyurethane alloys can be free of or substantially free of protein particles having an average diameter of greater than 1 micron (μm).

In some embodiments, the protein polyurethane alloys can be free of or substantially free of soy protein particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of collagen particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of gelatin particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of bovine serum albumin particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of pea protein particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of egg white albumin particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of casein protein particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of peanut protein particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of edestin protein particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of or substantially free of whey protein particles having an average diameter of greater than 1 micron (μm) In some embodiments, the protein polyurethane alloys can be free of or substantially free of karanja protein particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of, or substantially free of, cellulase particles having an average diameter of greater than 1 micron (μm). In some embodiments, the protein polyurethane alloys can be free of, or substantially free of, recombinant collagen fragment particles having an average diameter of greater than 1 micron (μm).

In particular embodiments, the present disclosure provides a unique combination of a protein and a polyurethane in which the protein is dissolved in only the hard phase of the polyurethane. The present disclosure also provides methods of making the protein polyurethane alloys described herein. The present disclosure also provides materials including one or more protein polyurethane alloys and methods of making the materials. In some embodiments, the present disclosure provides layered materials including one or more of the protein polyurethane alloy layers and methods of making the layered materials. The protein polyurethane alloys and the protein polyurethane alloy layers can include one or more types of protein and one or more polyurethanes.

Proteins suitable for use in the alloys disclosed herein can be un-modified or chemically modified. In some embodiments, the protein can be modified to facilitate miscibility of the protein with the hard phase of the polyurethane. In some embodiments, the protein can be chemically modified to promote solubility in water. In such embodiments, the chemical modification to promote solubility in water can facilitate miscibility of the protein with the hard phase of the polyurethane. In some embodiments, the chemically modified protein can be a partially hydrolyzed protein. In some embodiments, the chemically modified protein can be a protein modified by covalent attachment of hydrophilic polymer chains, such as polyethylene glycol (PEG) chains, to the protein.

Suitable polyurethanes for use in the protein polyurethane alloys described herein include those that comprise at least two phases including a “soft phase” and a “hard phase.” The soft phase is formed from polyol segments within the polyurethane that separate from the urethane-containing phase due to differences in polarity. The urethane-containing phase is referred to as the hard phase. This phase separation is well known in the art and is the basis of the many of the properties of polyurethanes.

The soft phase is typically elastomeric at room temperature, and typically has a softening point or glass transition temperature (Tg) below room temperature. The Tg can be measured by Dynamic Mechanical Analysis (DMA) and quantified by either the peak of tan(S) or the onset of the drop in storage modulus. Alternately, Tg can be measured by Differential Scanning Calorimetry (DSC). In some cases, there can be crystallinity in the soft phase, which can be seen as a melting point, typically between 0° C. and about 60° C. For example, the peak in the tan(S) curve at about 35° C. for UD-108 polyurethane inindicates crystallinity in the soft phase of the polyurethane.

The hard phase typically has a Tg or melting point above room temperature, more typically above about 80° C. The softening of the hard phase can be measured by measuring the onset of the drop in storage modulus (sometimes referred to as stiffness) as measured by DMA.

The “soft phase” for the polyurethane or the protein polyurethane alloy including the polyurethane comprises the polyol component of the polyurethane. Its function is to be soft and flexible at temperatures above its Tg to lend toughness, elongation, and flexibility to the polyurethane. Typical soft segments can comprise polyether polyols, polyester polyols, polycarbonate polyols, and mixtures thereof. They typically range in molecular weight from about 250 daltons to greater than about 5 kiloDaltons. The “hard phase” for the polyurethane or the protein polyurethane alloy including the polyurethane comprises the urethane segments of the polymer that are imparted by the isocyanate(s) used to connect the polyols along with short chain diols such as butane diol, propane diol, and the like. Typical isocyanates useful for the present polyurethanes include, but are not limited to, hexamethylene diisocyanate, isophorone diisocyanate, methylene diisocyanate, phenyl diisocyanate, and the like. These molecules are more polar and stiffer than the polyols used to make the soft segment. Therefore, the hard segment is stiffer and has a higher softening point compared to the soft segment. The function of the hard phase is to provide, among other properties, strength, temperature resistance, and abrasion resistance to the polyurethane.

In some embodiments described herein, the protein can be miscible with only the hard phase, leaving soft phase transitions substantially unaltered. Without wishing to be bound particular theory, it is believed that when the protein is dissolved in the hard phase, it significantly increases the temperature at which the hard phase begins to soften, thus increasing the temperature resistance of the alloy described herein. Protein polyurethane alloys described herein can also have increased stiffness and increased strength relative to the base polyurethane (i.e., the polyurethane by itself, in the absence of protein).

Protein polyurethane alloys and layers described herein can be formed by blending one or more proteins with one or more water-borne polyurethane dispersions in a liquid state and drying the blend. In some embodiments, the protein polyurethane alloys and layers described herein can be formed by blending one or more proteins dissolved or dispersed in an aqueous solution with one or more water-borne polyurethane dispersions in a liquid state and drying the blend. In some embodiments, the polyurethane dispersion can be ionic, and either anionic or cationic. In some embodiments, the polyurethane dispersion can be nonionic. In some embodiments, the blended protein and polyurethane can be formed into a sheet and can, in certain embodiments, be attached to a substrate layer using a suitable attachment process, such as direct coating, a lamination process or a thermo-molding process. In certain embodiments, the lamination process can include attaching the sheet to the substrate layer using an adhesive layer. In some embodiments, the blended protein and polyurethane can be coated or otherwise deposited over a substrate layer to attach the blended protein and polyurethane to the substrate layer. In some embodiments, attaching the blended protein and polyurethane to the substrate layer can result in a portion of the blended protein and polyurethane being integrated into a portion of the substrate layer.