Oat peptide isolate

Abstract

A method of making an oat peptide isolate comprising: combining an oat proten concentrate with at least 40% w / w protein concentration with a carbohydrase to produce a first intermediate product; remov

Description

This invention relates to an oat peptide isolate. In particular, this invention relates to a method for manufacturing an oat peptide isolate using an enzymatic process, the oat peptide isolate produced by this process, and compositions containing the oat peptide isolate for use in cosmetics and skincare applications. Oats (Avena sativa) are cultivated worldwide and form an important dietary staple for people in a number of countries. They are a rich source of protein, as well as containing important minerals and lipids. Oats have long been appreciated for their beneficial effects on the skin and in reducing inflammation, and efforts have been made to produce oat derived extracts and isolates which enhance these properties. Native oat protein concentrates are commercially available, for example PrOatein Oat protein™ produced by Lantmannen Oats, Sipal™ SipaPRO-Oat by Meurens Natural, Bio Hafer Protein produced by AlpenPower™ and SipaPro-Oat produced by Meurens Natural, and typically comprise greater than 50% protein. Methods for producing such concentrates typically involves dehulling and dry milling the oats to separate the oat bran from the oat flour, followed by enzyme treatment to aid in separation of the protein. This produces a hydrolysed oat extract which often has a higher concentration of oat sugars than oat protein. An alternative method involves first isolating oat protein from oat flour or oat bran using alkaline extraction followed by iso-electric precipitation. However, this process loses about 12-16% of the oat protein in the process, in the form of acid-soluble albumins, and the resulting product can contain a significant proportion (around 12-14%) of oat oil. In addition, some minor proteins such as prolamines are not extracted. Peptides are the building blocks of proteins. Reversing the process to produce peptides from proteins requires either chemical or enzymatic treatment, with the latter process being generally preferred. However, proteins found in oats, oat flour and oat bran are bound in a complex matrix of carbohydrates, oil bodies and insoluble fibre. This makes it difficult to access the protein, to purify and / or to convert them enzymatically to peptides. All methods currently in the literature teach the use of alkaline conditions to isolate oat proteins, a convention which focuses on the solubility of protein at a higher pH. For example, CN1875737 describes an oat peptide and its extraction under alkaline conditions, using oat bran as the starting material. The process uses an alkaline active enzyme as well as a commercially unavailable protease, avenin. The product may have a purity of up to 90%. CN113699208 describes a process for producing an oat peptide and oat avenanthramides using supercritical CO2 extraction and avenin. Unfortunately, this method of processing concomitantly extracts many other unwanted compounds including sugars, polar lipids and pigments, requiring often difficult additional steps to remove these in order to obtain a high purity product. Furthermore, alkaline conditions result in protein denaturation which may cause in poor enzymatic conversion of protein to peptides, leading to lower yields. Thus, while isolation of oat protein under alkaline conditions has some effectiveness, it results in relatively poor yield. Extraction of oat proteins is further complicated by the fact that proteins found in the aleurone and sub-aleurone layers extract differently from proteins found in the endosperm. This complex matrix ultimately leads to a low conversion rate and an overall poor peptide recovery. There is therefore a need for a process that produces an oat peptide isolate having a high concentration of peptides and a high degree of purity. Thus, there is a need for a commercially viable process for the preparation of an oat peptide isolate which allows for the peptides to be broken down in a controlled manner and extracted in a usable form. There has now been developed the following invention which overcomes or substantially mitigates the problems associated with the prior art. According to a first aspect of the invention there is provided a method for the manufacture of an oat peptide isolate, the method comprising the steps of: a) combining an oat protein concentrate having a protein concentration of at least 40% w / w with an enzyme capable of facilitating carbohydrate hydrolysis, to produce a first intermediate product; b) removing the sugar fraction from the first intermediate product to produce a second intermediate product; c) combining the second intermediate product with an enzyme capable of peptide formation to hydrolyse the proteins contained therein, to produce a crude peptide isolate; and d) purifying and concentrating the crude peptide isolate to produce an oat peptide isolate comprising at least 80% w / w peptides and less than 0.1% w / w soluble fibre. It has been found that the method of the invention produces an oat peptide isolate having a purity and peptide concentration much higher than that seen in the prior art. An oat peptide isolate having at least 80% w / w oat peptides has been found to have positive effects on dermis structural components, suggesting a beneficial effect on boosting skin firmness, skin remodelling, and skin elasticity and plumping. While the oat peptide isolate of the present invention is derived from oats, the peptides contained therein have been substantially structurally altered from those contained in the original oats by the process described herein, and it is therefore not an oat extract. The method comprises a first step of combining an oat protein concentrate having a peptide concentration of at least 40% w / w with an enzyme capable of facilitating carbohydrate hydrolysis. It has been found that the method described herein is particularly effective when the starting material is an oat protein concentrate. Using whole oats, milled oats or oat bran was found to affect the final yield, due to interference from beta glucan, starch and lipids which reduced the overall effectiveness of the enzyme activity. A variety of conditions cause enzyme activity to cease, including product feedback mechanisms, liquid concentration, enzyme to substrate ratio and components present in the original material. To overcome these restrictions on enzyme activity and achieve a high yield it has been found that an oat protein concentrate having a protein concentration of at least 40% w / w should be used as a starting material. Such an oat protein concentrate will respond to protein hydrolysis while minimizing possible inhibitor effects of non-protein components. The oat protein concentrate may be a commercially available oat protein concentrate. These include, but are not limited to, PrOatein Oat protein™ produced by Lantmannen Oats, Sipal™ SipaPRO-Oat by Meurens Natural, and Bio Hafer Protein produced by Alpen Power™. The oat protein concentrate may comprise an oat product processed such that it is substantially devoid of starch, for example Sipal™ SipaPRO-Oat by Meurens Natural. Such oat products require less processing, and may therefore be desirable starting products. It has been found that improved results are obtained when an oat protein concentrate having a high protein concentration is used as the starting product, compared to using oat flour or oat bran. Thus, the oat protein concentrate may have a protein concentration of at least 45% w / w oat protein, or at least 50% w / w oat protein, or at least 55% w / w oat protein. In particular, the oat protein concentrate may have a concentration of at least 55% w / w oat protein. The oat protein concentrate may have a protein concentration of up to 70% w / w, or up to 65% w / w, or up to 60% w / w. That is, the oat protein concentrate may have a protein concentration of, for example, between 45% w / w and 70% w / w, or between 45% w / w and 65% w / w. The oat protein concentrate is mixed with at least one enzyme capable of facilitating carbohydrate hydrolysis. The at least one enzyme may be an enzyme capable of hydrolysing complex carbohydrates and other non-proteinaceous compounds. The enzyme capable of facilitating carbohydrate hydrolysis may be any enzyme capable of at least partially breaking down or degrading polymeric sugars, including starch lactose, sucrose, cellulose, hemicellulose and chitin, into simpler forms of sugar, such as glucose. Such enzymes may include amylase, cellulase, hemi-cellulase, chitinase, glucosidases, glucanase, glycosidases, lactase, maltase, sucrase trehalase, arabinase and / or xylanase. In order to facilitate the removal of starch from the solution, the at least one enzyme capable of facilitating carbohydrate hydrolysis may be amylase, cellulase, glucanase and / or glucosidase. The at least one enzyme may be a-amylase, beta glucosidase, hemi-cellulase, cellulase and / or amyloglucanase. Preferably, the at least one enzyme capable of facilitating carbohydrate hydrolysis may be a-amylase. The at least one enzyme may liquify the starches in the oat protein concentrate to maltodextrins. The use of an a-amylase, and particularly of a high temperature active a-amylase, leads to the fast liquification of the starch present in the oat protein concentrate. Alternatively, a low temperature a-amylase may be used. Where the oat protein concentrate is substantially devoid of starch, it is believed that initial treatment with the at least one enzyme capable of carbohydrate hydrolysis disrupts the complex matrix comprising primarily large molecular weight carbohydrates, lignans and other complex biomolecules. The enzyme used may particularly be cellulase, hemi-cellulose, xylanase, arabinose or any combination thereof, and leads to the hydrolysis of complex non-starch carbohydrates, thereby allowing for improved protein hydrolysis. The first step may preferably be carried out under acidic conditions. The enzyme capable of carbohydrate hydrolysis may be an acidic enzyme. The first step may be carried out under acidic conditions, with a pH of between 2.0 and 5.0, or of between 3.0 and 4.0 being preferred. It has been surprisingly found that processing the starting material under acidic conditions, as described above, has a number of benefits. Treatment at low pH results in accessing of protein in the oat biomass matrix whilst removing un-wanted non-proteinaceous compounds, as well as reducing microbial growth during the enzymatic hydrolysis, while minimising the coextraction of undesirable components (eg sugars, lipids and pigments). Moreover, pre-treatment with alkali carbohydrases will soluble protein thereby reducing the amount of protein available for protein to peptide conversion in the subsequent steps, hence the use of an acidic carbohydrase. Further, any or all of the steps of the method may be carried out under acidic conditions, e.g. with a pH of between 2.0 and 5.0, or of between 3.0 and 4.0 being preferred. Thus, steps a), or b), or c) may be carried out under acidic conditions, or steps a) and c) may be carried out under acidic conditions, or steps a), b) and c) may be carried out under acidic conditions. Water may also be added to the oat protein concentrate, to form a slurry. The water may be acidified water. Thus, step a) of the first aspect of the invention may comprise combining an oat protein concentrate having a protein concentration of at least 40% w / w with water and an enzyme capable of facilitating carbohydrate hydrolysis. Where water is added, the at least one enzyme may have the additional effect of thinning the slurry. Water may be added to the oat protein concentrate at a ratio of between 1:2 and 1:20, or of between 1:3 and 1:15, or of between 1:4 and 1:10, or of between 1:5 and 1:9, or of about 1:7. The solid to liquid ratio of the mixture may impact the conversion of starch to maltodextrins, or the hydrolysis of complex carbohydrates. In this first step, the slurry may be heated to cause starch gelatinization and to increase enzyme activity. The slurry may be heated to a temperature of at least 60°C, and up to 95°C, or of between 65°C and 95°C, or of between 75°C and 85°C, to encourage gelatinization of the starch and allow hydrolysis to occur. Alternatively, the slurry may be heated to between 40°C and 70°C, or between 45°C and 60°C, to facilitate carbohydrate hydrolysis. Typically, the slurry may be maintained under acidic conditions, with a pH of between 2.0 and 5.0, or of between 3.0 and 4.0 being preferred. Breakdown of the starch may be detected / determined using a negative iodine starch test. The second step of the invention comprises removing the sugar fraction, to form a second intermediate product. Methods for removing the sugar fraction are known in the art. The sugar fraction may be separated and removed by centrifuge, eg by decanter centrifuge and / or clarifying disk centrifuge. The sugar fraction may be separated by passing the second intermediate product through a decanting centrifuge followed by a clarifying disk centrifuge. Where the enzyme used in the first step is a-amylase, the sugar fraction typically comprises maltodextrin. The maltodextrin fraction may be further treated by an amylopectinase to convert maltodextrins to simple sugars. Once the sugar fraction (which may comprise maltodextrins) has been removed by centrifugation, the resulting oat protein concentrate containing a higher relative concentration of oat protein may be redispersed into water. The second intermediate product may contain at least 60% w / w oat protein, or at least 65% w / w oat protein, or at least 70% w / w oat protein, or at least 72% w / w oat protein. The second intermediate product may be washed with water to remove any residual sugars and non-proteinaceous matter that may reduce the overall purity of the oat peptides being produced and to minimize glycation (reaction between protein and a reducing sugar). The second intermediate product may be washed with water at a ratio of from 1:3 to 1:10. In a third step, the second intermediate product is combined with an enzyme capable of peptide formation to hydrolyse the proteins contained therein, to produce a crude peptide isolate. The crude peptide isolate may be soluble. The third step may be carried out under acidic conditions. The pH of the solution during this step may be acidic, and may be between 2.0 and 4.5. The second intermediate product comprises an enriched oat protein concentrate. Water may be added to the second intermediate product in this step, to dilute the solution. A high dilution with water may be used, typically between 1:70 and 1:110, or between 1:80 and 1:100. It has been found that a high dilution results in a better conversion of protein to peptides. The at least one enzyme capable of peptide formation may be a protease, and may be an endoprotease or endopeptidase, or an exopeptidase or exoprotease. The at least one enzyme capable of peptide formation may be an acidic protease. An acidic protease is a protease which is active in acidic conditions (ie a pH of between 2.0 and 5.0, or of less than 4.5). It has been found that an acidic protease reduces the possibility of solubilising non-proteinaceous compounds, and leads to a higher yield and purity. It has been found that the use of an acidic protease typically leads to a protein to peptide conversion of 70-72%, compared to the 54-56% protein to peptide conversion observed for an alkali enzymatic protease. The at least one enzyme capable of peptide formation may be a serine-specific endopeptidase. In this third step the solution may be heated. The solution may be heated to a temperature between about 40°C and 60°C, or between about 50°C and 55°C. In a fourth step of the method, the crude peptide isolate is purified and concentrated to produce an oat peptide isolate comprising at least 80% w / w peptides. The oat peptide isolate may comprise at least 85% w / w peptides, or at least 90% w / w peptides. Any suitable purification and / or concentration methods known in the art may be used. In particular, purification and / or concentration may comprise multiple steps, and may include one or more of the following stages: i. separating the solids from the crude peptide isolate to produce a crude peptide solution, for example by filtration or centrifugation; ii. purifying the crude peptide solution, for example using ultra-filtration; iii. concentrating the peptides to produce a peptide concentrate, for example by reverse osmosis; and / or iv. treating the peptide concentrate of step iii. with activated carbon, and filtering the resulting solution to remove residues of activated carbon, to deodorise and / or decolourise the solution. The purification and / or concentration steps may also comprise producing an oat peptide powder, the process comprising: v. pasteurising the peptide concentrate; and / or vi. spray drying the peptide concentrate. One or more, or all, of the steps i. to vi. may form step d) of the first aspect of the invention. The resultant powder is 100% water soluble and freely flowable, and so can be easily incorporated into cosmetic compositions. The crude peptide isolate may be processed to separate the solids and produce a crude peptide solution, as in step i. above. This separation step may be carried out using filtration, or a horizontal bowl decanter centrifuge, or a clarifying centrifuge. This step may particularly be carried out through using a clarifying disk centrifuge. The solids separated from the solution may comprise unreacted or partially unreacted protein solids. The solids may be washed to remove and retain as much of the crude peptide solution as possible. The crude peptide isolate or crude peptide solution may be purified using ultrafiltration, as in step ii. above. In the ultrafiltration process, hydrostatic pressure forces the liquid against a semi-permeable membrane. Types of membrane modules may include spiral, flat plate, hollow fiber and tubular designs. Suspended solids and solutes of high molecular weight are retained, while water and low molecular weight solutes, including peptides, pass through the membrane. It has been found that the use of an acidic protease enzyme to hydrolyse the proteins in step c) of the invention is effective at producing low molecular weight peptides, which negates the need to use low molecular weight cut-off (MWCO) membranes during ultrafiltration, thereby increasing throughput and reducing costs. Thus, step c) may be carried out at a pH of between 2.0 and 6.0, or of between 2.0 and 5.0. However, further purification by nano filtration may also be used. Ultrafiltration may be carried out using a MWCO of between 1 and 50kDa, or between 3 and 10 kDa. The solution may be concentrated, as in step iii. above. The solution, e.g. the purified crude peptide solution, may be concentrated using reverse osmosis, which uses pressure greater than the current osmotic pressure to drive water out of the purified solution, across the membrane, leaving a more concentrated isolate. Typically, reverse osmosis is carried out at ambient temperature. Methods which involve a high temperature, such as evaporators (eg. Falling film tubular, Wiped film, etc.), may cause adverse coloured compounds to be produced (e,g. Amadori compounds) and so are less desirable. The use of reverse osmosis may produce a concentrated and purified oat peptide solution having at least 10% w / w dry matter, or at least 15% w / w dry matter, or at least 20% w / w dry matter, or up to 30% w / w dry matter, or up to 25% w / w dry matter, or between 20 and 25% dry matter. Protein isolates can be undesirable skincare additives due to their colour and / or odour. The isolate may be further treated with activated carbon to deodorise and / or decolorise the product as in step iv. above. This step may comprise treating the peptide isolate, peptide solution or concentrated isolate above with activated carbon, and filtering the resulting solution to remove residues of activated carbon. It has been found that activated carbon deodorises and / or decolourises the product with minimal or negligible loss of peptides. Filtration may be carried out using any suitable method, including basket centrifuge, filter press or canister filter system. The product may be further treated by pasteurisation as in step vi. above. Pasteurisation may be used to sterilise the product. Pasteurisation may be carried out either by batch pasteurisation or high temperature, short time (HTST) processes. Batch pasteurisation may be carried out at a temperature of between 70 and 90QC, or between 72 and 85 QC, for at least 1 minute, or at least 2 minutes, or at least 3 minutes. Batch pasteurisation may be carried out at a temperature of between 72 and 85QC for at least 3 minutes. The final oat peptide isolate may be in liquid or solid form. The final oat peptide isolate may typically be in powder form. The powder may be produced by spray-drying the product as in step vi. above, for example using a conventional food grade spray dryer such as is known in the art. The method described above may comprise one or more additional steps. The one or more additional steps may comprise defatting. Defatting may be carried out at any appropriate point in the method. The defatting step may particularly occur before step a) in the above-described method. That is, defatting may form the first step of the described method, or a pre-treatment step. The defatting process may comprise taking an oat protein concentrate having a protein concentration of at least 40% w / w and a lipid concentration of at least 5% w / w, and treating it with a solvent capable of reducing the lipid concentration to less than 3% w / w. This defatted oat protein concentrate is then used as the oat protein concentrate in the following steps of the method. In the context of the invention, ‘lipids’ comprise fatty components, including triglycerides, free fatty acids, phospholipids, glycolipids, ceramides, waxes, fatty alcohols, sterols, lipoproteins, and any other fatty component that may be removed by solvent extraction. The fat or lipid content of oats typically ranges from 3-12% w / w in oat bran, and up to 14% w / w in oat protein concentrates. It has been found that removal of the excess lipids from the oat protein concentrate results in a higher yield product with greater purity. It is believed that this increased yield is seen because, if the oats have not been defatted before protein extraction, these lipids get carried over into the protein stream, creating a protein concentrate with a high oil content. This can then cause emulsions to be formed during the extraction phase, decreasing protein recovery. It has been further found that protein conversion during enzymatic hydrolysis is higher where the lipid concentration in the starting material is lower. Defatting may be carried out where the lipid concentration in the oat protein concentrate is in excess of 5% w / w, or in excess of 3%w / w. Defatting is carried out by solvent extraction and any suitable solvent known in the art may be used, including (but not limited to) hexane, ethanol and supercritical fluid carbon dioxide. Supercritical fluid carbon dioxide may be particularly preferred as it is considered a green solvent and does not leave any residual solvent in the final product. Supercritical fluid carbon dioxide may be combined with a solvent entrainer, such as ethanol, which has been found to remove additional polar lipids. The one or more additional steps may (additionally or alternatively) comprise treating the oat protein concentrate with microwave or ultrasonic-assisted extraction. This step may be carried out either prior to or during step a). That is, it may form a pretreatment step, or part of step a). Treatment with microwave or ultra-sonic assisted extraction significantly reduces overall treatment time, and accelerates the enzymatic hydrolysis of complex carbohydrates within the mixture. In comparison to conventional extraction methods where larger quantities of solvent are used, longer extraction times are required and the possibility of thermal or oxidative degradation exists, both microwave and ultrasonic-assisted extractions significantly reduce the amount of solvent and time, and typically result in higher selectivity and yield(s) of the target molecule(s). In the case of microwave-assisted extraction (MAE), microwaves are used to disrupt hydrogen bonds as well as increasing pressure, and providing good solvent penetration into the biomass. MAE is a low energy consumption process using less but uniform heating, while providing high efficiency extraction of the target molecule(s). An alternative process which may be used is ultrasonic-assisted extraction (UAE). Ultrasonic energy is used to disrupt the physical matrix by causing a cavitation phenomenon, leading to high shear forces within the extraction media. This results in the physical breakdown of the biomass, allowing for better extraction of the target molecule(s). Similar to MAE, UAE utilizes less solvent compared conventional extraction methods and reduces extraction time from hours to minutes, resulting in much higher yields of the target molecule (s). During this step, the slurry, comprising the biomass and the solvent may be passed through a chamber and subjected to micro- or ultrasonic waves. In the case of UAE, probes may be inserted directly into the extraction vessel. A number of industrial scale systems for both pre-treatment and extraction methods are commercially available. It is believed that the product produced by the method of the invention is also new. Thus, according to a further aspect of the invention there is provided an oat peptide isolate having a peptide concentration of greater than 80% w / w, and containing less than 0.1% w / w total soluble fibre It has been found that an oat peptide isolate having a high peptide concentration , of greater than 80% w / w, has positive effects on dermis structural components suggesting a beneficial effect on boosting skin firmness, skin remodelling, and skin elasticity and plumping. In particular, the oat peptide isolate of the invention has been found to increase collagen 1 and collagen 5 levels in the skin. Collagen is a structural protein primarily produced by fibroblasts in the dermis, and decreases in collagen 1 are associated with an altered inflammatory response and, if not in balance with elastin content, a decrease in skin elasticity. The expression of collagen 1 also plays an important role in wound healing and the development of scar tissue. Moreover, the oat protein isolate of the invention has low levels of other components, in particular containing less than 0.1% w / w total soluble fibre. The beneficial effects on the skin, including increasing skin firmness and skin remodelling, mean that it may be used in cosmetic compositions where such function is desirable, for example in moisturising products, skin creams, anti-aging products, make-up products and / or sunscreens. Thus, according to a further aspect of the invention there is provided a cosmetic composition comprising an oat peptide isolate, wherein the oat peptide isolate has a peptide concentration of greater than 80% w / w, and contains less than 0.1% w / w total soluble fibre. The oat peptide isolate according to the first, second or third aspects of the invention may be an oat peptide powder, and has a peptide concentration of greater than 80% w / w, or greater than 85% w / w, or greater than 90% w / w. The oat peptide powder may have a peptide concentration of up to 99% w / w, or up to 95% w / w. The oat peptide powder may have a concentration of from about 80% to about 99% w / w, or of from about 85% to about 99% w / w, or of from about 90% to about 99% w / w. The oat peptide powder may have a peptide concentration of from about 85% w / w to about 99% w / w. In the oat peptide isolate of the invention, approximately 40-70% of the peptides contained therein may have a molecular weight of from 300-1000 Da. Approximately 30-60% of the peptides contained therein may have a molecular weight of from 1000-3000 Da. It has been found that an isolate having such low to medium molecular weight peptides has beneficial effects on collagen and elastin levels in the skin, suggesting beneficial effects on boosting skin firmness, skin remodelling and skin elasticity. The oat peptide isolate may contain some soluble sugars. The oat peptide isolate may contain a very low level of soluble sugars. The oat peptide isolate may contain less than 5% w / w, or less than 2% w / w soluble sugars. The oat peptide isolate of the invention may comprise only low levels of starch, such as short chain oligosaccharides. The oat peptide isolate may contain less than 0.01% w / w starch, such as short chain oligosaccharides. The oat peptide isolate may contain substantially no starch. The oat peptide isolate may contain no measurable starch content. The oat peptide isolate of the invention may have a moisture content of between 1 and 15% w / w, or of between 2 and 10% w / w, or of between 2 and 5% w / w. The oat peptide isolate may have a moisture content of between 2 and 5% w / w. The oat peptide isolate of the invention may contain less than 0.1% w / w lipids. The oat peptide isolate may contain less than 0.01% w / w lipids. The oat peptide isolate may contain no measurable lipid content. Oats contain a higher level of lipids than other cereals, most of which are found in the endosperm. However, the oat peptide isolate of the invention may contain very low levels of, or no measurable, lipids, increasing the purity of the product. The oat peptide isolate of the invention may contain no preservatives. It may be preservative free. The oat peptide isolate may be in solid or liquid form. The oat peptide isolate may be in solid form. The oat peptide isolate may be in powder form. The oat peptide isolate may be a freely flowable powder. The oat peptide isolate may be water soluble. The oat peptide isolate of the invention contains less than 0.1% w / w total soluble fibre, such as 1,3- or 1,4- beta glucan, arabinoxylan, or xyloglucan. It may contain less than 0.01% w / w total soluble fibre. The oat peptide isolate of the invention may contain less than 0.1% w / w 1,3- or 1,4- beta glucan, arabinoxylan or xyloglucan, or less than 0.01% w / w 1,3- or 1,4- beta glucan, arabinoxylan or xyloglucan. The oat peptide isolate may comprise no measurable soluble fibre, or no measurable beta glucan, arabinoxylan or xyloglucan. The oat peptide isolate of the invention may have an ash concentration of less than 15% w / w, or less than 10% w / w, or less than 3% w / w. The oat peptide isolate may have a molecular weight of less than 3000 Da. The oat peptide isolate may have a molecular weight of less than 2000 Da, or less than 1500 Da, or less than 1200 Da. The oat peptide isolate may have a molecular weight of less than 1200 Da. The oat peptide isolate of the invention may comprise a range of amino acids. The oat peptide isolate of the invention may comprise amino acids not found in natural oats. The oat peptide isolate of the invention may comprise one or more of the following amino acids: alanine, arginine, aspartic acid, glutamic acid, glycine, histidine, hydroxyproline, isoleucine, leucine, lysine, ornithine, phenylalanine, proline, serine, threonine, tyrosine, valine, cysteine and cystine, methionine and tryptophan. The oat peptide isolate of the invention may comprise any combination of, or all of, the foregoing amino acids. The oat peptide isolate of the invention may comprise glutamic acid, and may comprise between 20 and 25% w / w glutamic acid, or between 22.5 and 22.9% w / w glutamic acid. The oat peptide isolate of the invention may comprise alanine, and may comprise between 3 and 5% w / w alanine. The oat peptide isolate of the invention may comprise arginine, and may comprise between 5 and 6% w / w arginine. The oat peptide isolate of the invention may comprise lysine, and may comprise between 2 and 3% w / w lysine. The oat peptide isolate of the invention may comprise histidine, and may comprise between 1.5 and 2% w / w histidine. The oat peptide isolate of the invention may comprise aspartic acid, and may comprise between 6 and 7% w / w aspartic acid. The composition of the third aspect of the invention may comprise from 0.01% w / w to 30% w / w oat protein isolate. The composition may comprise from 0.01% w / w to 10% w / w oat protein isolate. The composition may comprise from 0.05% w / w to 5% w / w oat protein isolate. The composition may comprise from 0.05% w / w to 1% w / w oat protein isolate. The composition may comprise from 0.1% w / w to 0.5% w / w oat protein isolate. The composition may comprise at least 0.01% w / w, or at least 0.05% w / w, or at least 0.1% w / w oat protein isolate. The composition may comprise 5% w / w or less, or 2% w / w or less, or 1 % w / w or less, or 0.7% w / w or less, or 0.5% w / w or less oat protein isolate. The composition may comprise 0.1% w / w oat protein isolate. The composition may comprise 0.5% w / w oat protein isolate. While it is commonly found that peptide isolates can impart an undesirable smell and / or colour to cosmetic compositions, it has been surprisingly found that the oat peptide isolate of the invention produces a composition having both acceptable odour and colour. The composition of the invention may further comprise one or more additional active ingredients selected from anti-acne actives, anti-bacterial agents, anti-inflammatory agents, anti-irritant agents, desquamation actives, anti-cellulite agents, chelating agents, flavonoids, tanning active, non-vitamin antioxidants and radical scavengers, anti-wrinkle actives, anti-ageing agent, anti-atrophy actives, minerals, phytosterols and / or plant hormones, N-acyl amino acid compounds, antimicrobial or antifungal actives, peptides, anti-ageing peptides, plants extracts, conditioning agents, moisturising agents, humectants, skin lightening agents, preservatives, antioxidants, penetration enhancers, emollients, astringent, biocidal compounds, sunscreens or UV absorbers, pigments, perfumes, anti-aging agents, enzymes, proteins, waxes, vitamins or other useful skin care agents. The conditioning agents which can be used include polyquatemium, such as the copolymer of N,N'-bis((dimethylamino)-3 propyl)urea and oxy-1,1'bis(2-chloro)ethane or polyquaternium-2, the copolymer of diallyldimethyl ammonium chloride and acrylamide or polyquaternium-7, and cationic polysaccharide derivatives such as cocodimonium hydroxyethyl cellulose, guar hydroxypropyl trimonium chloride, hydroxypropyl guar hydroxypropyl trimonium chloride aloe extracts, allantoin, bisabolol, ceramides, dimethicone, hyaluronic acid, and dipotassium glycyrrhizate. Suitable moisturising agents include glycerol, sorbitol, urea, collagen, gelatine, aloe vera, hyaluronic acid, amino acids, chondroitin sulfate, diglycerin, erythritol, fructose, glucose, glycerin, glycerol polymers, glycol, 1,2,6-hexanetriol, honey, hydrogenated honey, hydrogenated starch hydrolysate, inositol, lactitol, maltitol, maltose, mannitol, natural moisturizing factor, PEG-15 butanediol, polyglyceryl sorbitol, salts of pyrrolidone carboxylic acid, potassium PCA, propylene glycol, sodium glucuronate, sodium PCA, sucrose, trehalose, and xylitol. Other examples of moisturizers include: acetylated lanolin, acetylated lanolin alcohol, acrylates / C 10-30 alkyl acrylate crosspolymer, acrylates copolymer, alanine, algae extract, aloe barbadensis, aloe-barbadensis extract, aloe barbadensis gel, althea officinalis extract, (Prunus armeniaca) kernel oil, arginine, arginine aspartate, arnica montana extract, ascorbic acid, ascorbyl palmitate, aspartic acid, avocado (Persea gratissima) oil, barium sulfate, barrier sphingolipids, butyl alcohol, beeswax, behenyl alcohol, betasitosterol, BHT, birch (betula alba) bark extract, borage (Borago officinalis) extract, 2-bromo-2-nitropropane-1,3-diol, butcherbroom (Ruscus aculeatus) extract, butylene glycol, calendula officinalis extract, calendula officinalis oil, candelilla (Euphorbia cerifera) wax, canola oil, caprylic / capric triglyceride, cardamon (Elettaria cardamomum) oil, carnauba (Copernicia cerifera) wax, carrageenan (Chondrus crispus), carrot (Daucus carota sativa) oil, castor (Ricinus communis) oil, ceramides, ceresin,ceteareth-5, ceteareth-12, ceteareth-20, cetearyl octanoate, ceteth-20, ceteth-24, cetyl acetate, cetyl octanoate, cetyl palmitate, chamomile (anthemis nobilis) oil, cholesterol, cholesterol esters, cholesteryl hydroxystearate, citric acid, clary (Salvia sclarea) oil, cocoa (Theobroma cacao) butter, coco-caprylate / caprate, coconut (Cocos nucifera) oil, collagen, collagen amino acids, corn (Zea mays) oil, fatty acids, decyl oleate, dextrin, diazolidinyl urea, dimethicone copolyol, dimethiconol, dioctyl adipate, dioctyl succinate, dipentaerythrityl hexacaprylate / hexacaprate, DMDM hydantoin, erythritol, ethoxydiglycol, ethyl linoleate, eucalyptus globulus oil, evening primrose (oenothera biennis) oil, fatty acids, tructose, gelatin, geranium maculatum oil, glucosamine, glucose glutamate, glutamic acid, glycereth-26, glycerin, glycerol, glyceryl distearate, glyceryl hydroxystearate, glyceryl laurate, glyceryl linoleate, glyceryl myristate, glyceryl oleate, glyceryl stearate, glyceryl stearate SE, glycine, glycol stearate, glycol stearate SE, glycosaminoglycans, grape (Vitis vinifera) seed oil, hazel (Corylus americana) nut oil, hazel (Corylus avellana) nut oil, hexylene glycol, honey, hyaluronic acid, hybrid safflower (Carthamus tinctorius) oil, hydrogenated castor oil, hydrogenated coco-glycerides, hydrogenated coconut oil, hydrogenated lanolin, hydrogenated lecithin, hydrogenated palm glyceride, hydrogenated palm kernel oil, hydrogenated soybean oil, hydrogenated tallow glyceride, hydrogenated vegetable oil, hydrolyzed collagen, hydrolyzed elastin, hydrolyzed glycosaminoglycans, hydrolyzed keratin, hydrolyzed soy protein, hydroxylated lanolin, hydroxyproline, imidazolidinyl urea, iodopropynyl butylcarbamate, isocetyl stearate, isocetyl stearoyl stearate, isodecyl oleate, isopropylisostearate, isopropyl lanolate, isopropyl myristate, isopropyl palmitate, isopropyl stearate, isostearamide DEA, isostearic acid, isostearyl lactate, isostearyl neopentanoate, jasmine (jasminum officinale) oil, jojoba (buxus chinensis) oil, kelp, kukui (aleurites moluccana) nut oil, lactamide MEA, laneth-16, laneth-10 acetate, lanolin, lanolin acid, lanolin alcohol, lanolin oil, lanolin wax, lavender (lavandula angustifolia) oil, lecithin, lemon (citrus medica limonum) oil, linoleic acid, linolenic acid, macadamia ternifolia nut oil, magnesium stearate, magnesium sulfate, maltitol, matricaria (chamomilla recutita) oil, methyl glucose sesquistearate, methylsilanol PCA, microcrystalline wax, mineral oil, mink oil, mortierella oil, myristyl lactate, myristyl myristate, myristyl propionate, neopentyl glycol dicaprylate / dicaprate, octyldodecanol, octyldodecyl myristate, octyldodecyl stearoyl stearate, octyl hydroxystearate, octyl palmitate, octyl salicylate, octyl stearate, oleic acid, olive (olea europaea) oil, orange (citrus aurantium dulcis) oil, palm (elaeis guineensis) oil, palmitic acid, pantethine, panthenol, panthenyl ethyl ether, paraffin, PCA, peach (prunus persica) kernel oil, peanut (arachis hypogaea) oil, PEG stearates pentadecalactone, peppermint (mentha piperita) oil, petrolatum, phospholipids, polyamino sugar condensate, polyglyceryl-3 diisostearate, polyquaternium-24, polysorbate 20, polysorbate 40, polysorbate 60, polysorbate 80, polysorbate 85, potassium myristate, potassium palmitate, potassium sorbate, potassium stearate, propylene glycol, propylene glycol dicaprylate / dicaprate, propylene glycol dioctanoate, propylene glycol dipelargonate, propylene glycol laurate, propylene glycol stearate, propylene glycol stearate SE, PVP, pyridoxine dipalmitate, quaternium- 15, quaternium-18 hectorite, quaternium-22, retinol, retinyl palmitate, rice (oryza sativa) bran oil, RNA, rosemary (rosmarinus officinalis) oil, rose oil, safflower (carthamus tinctorius) oil, sage (salvia officinalis) oil, salicylic acid, sandalwood (santalum album) oil, serine, serum protein, sesame (sesamum indicum) oil, shea butter (butyrospermum parkii), silk powder, sodium chondroitin sulfate, sodium hyaluronate, sodium lactate, sodium palmitate, sodium PCA, sodium polyglutamate, sodium stearate, soluble collagen, sorbic acid, sorbitan laurate, sorbitan oleate, sorbitan palmitate, sorbitan sesquioleate, sorbitan stearate, sorbitol, soybean (glycine soja) oil, sphingolipids, squalane, squalene, stearamide MEA-stearate, stearic acid, stearoxy dimethicone, stearoxytrimethylsilane, stearyl alcohol, stearyl glycyrrhetinate, stearyl heptanoate, stearyl stearate, sunflower (helianthus annuus) seed oil, sweet almond (prunus amygdalus dulcis) oil, synthetic beeswax, tocopherol, tocopheryl acetate, tocopheryl linoleate, tribehenin, tridecyl neopentanoate, tridecyl stearate, triethanolamine, tristearin, urea, vegetable oil, water, waxes, wheat (triticum vulgare) germ oil, and ylang ylang (cananga odorata) oil. Suitable emollients include alkylmonoglycerides, alkyldiglycerides, triglycerides such as oils extracted from plants and from vegetables (eg palm oil, coprah oil, cottonseed oil, soya bean oil, sunflower seed oil, olive oil, grapeseed oil, sesame oil, peanut oil, castor oil, Jojoba Oil, Macadamia Nut Oil, Argan Oil, Avocado Oil, Almond Oil, Evening Primrose Oil, Rosehip Oil, Tamanu Oil, Borage Seed Oil, Coconut Oil, Corn Oil, Hazelnut Oil, Meadowfoam Seed Oil, Pomegranate Seed Oil,Rice Bran Oil, Wheat Germ Oil, Emu Oil, Kukui Nut Oil, Marula Oil, Neem Oil) or oils of animal origin (eg tallow, fish oils, lanolin, emu oil, etc), derivatives of these oils such as hydrogenated oils, lanolin derivatives, olive squalane, mineral oils or paraffin oils, perhydrosqualane, squalene, diols such as 1,2-propanediol, 1,3-butanediol, cetyl alcohol, stearyl alcohol, oleic alcohol, Myristyl Alcohol, Behenyl Alcohol, polyethylene glycols or polypropylene glycols, fatty esters such as isopropyl palmitate, 2-ethylhexyl cocoate, myristyl myristate, Ethylhexyl Palmitate, Glyceryl Stearate, Isopropyl Myristate, Oleyl Oleate, Triethylhexanoin, Hydrogenated Polydecene, Dicaprylyl Ether, Isostearyl Isostearate, Octyldodecanol, Sorbitan Isostearate, Sorbitan Sesquioleate, Cetyl Palmitate, esters of lactic acid, stearic acid, behenic acid, isostearic acid, silicone oils such as polydimethylsiloxanes, silicone copolyols (dimethicone copolyol, cetyldimethicone copolyol), diphenyldimethicones, phenyltrimethicones, dimethiconols, . Suitable sunscreen agents and UV filters are known in the art and include both inorganic and organic sunscreens. Inorganic sunscreens include microfine titanium dioxide, microfine zinc oxide, iron oxides, talcs and boron nitride. Organic sunscreen agents include: a) p-aminobenzoic acids, esters and derivatives thereof, for example, 2-ethylhexyl p-dimethylaminobenzoate and the octyl ester of p-aminobenzoic acid; b) methoxycinnamate esters such as 2-ethylhexyl p-methoxycinnamate, 2-ethoxyethyl p-methoxycinnamate or a,[3-di-(p-methoxycinnamoyl)-a'-(2-ethylhexanoyl)-glycerin; c) benzophenones such as oxybenzone; d) 2-phenylbenzimidazole-5-sulfonic acid and disodium phenyl dibenzimidazole tetrasulfonate and terphthalylidene dicamphor sulfonic acid; e) alkyl-[3,[3-diphenylacrylates, for example alkyl a-cyano-[3,[3-diphenylacrylates such as octocrylene; f) triazines such as 2,4,6-trianilino-(p-carbo-2-ethylhexyl-1 ’-oxy)-1,3,5 triazine and bis-octyloxyphenol methoxyphenyl triazine; g) camphor derivatives such as methylbenzylidene camphor; h) organic pigment sunscreening agents such as methylene bis-benzotriazole tetramethyl butylphenol; i) silicone derivatives such as drometrizole trisiloxane, benzylidene malonate polysiloxane and dimethicodiethyl benzal malonate k) salicylates such as octyl salicylate; and I) Organic nano particles such as Methylene Bis-Benzotriazolyl Tetramethylbutylphenol Suitable perfumes include benzaldehyde, caraway oil, cardamom oil, cinnamon oil, ethylvanillin, eucalyptus globulus oil, glutamic acid, clove oil, orange oil, peppermint oil, thymol, phenethyl alcohol, bergamot oil, geranium oil, lavender oil, rose oil, sandalwood oil, vanilla extract, ylang-ylang oil, jasmine oil, patchouli oil, vetiver oil, musk, ambergris, and various floral, fruity, woody, and spicy notes. Suitable anti-aging agents include carrot extract, Ceramide 33, hydrolyzed serum protein, palmitoyl peptides, retinoids, vitamin C derivatives, alpha hydroxy acids (AHAs), beta hydroxy acids (BHAs), polyhydroxy acids (PHAs), peptides, antioxidants, hyaluronic acid and its derivatives, niacinamide, epidermal growth factors (EGFs), plant stem cells, ceramides, essential fatty acids (EFAs), resveratrol, ferulic acid, growth factors, collagen and elastin peptides, astaxanthin, alpha lipoic acid, and carnosine Suitable enzymes include lipase, papain, soy protein, coenzymes such as ubiquinone Q10, bromelain, lactase, amylase, protease, and superoxide dismutase (SOD). Suitable proteins include collagen, collagen derivatives, keratin, elastin, silk protein, soy protein, wheat protein, oat protein, rice protein, pea protein, milk protein, egg protein, quinoa protein, hemp protein, and various plant-based protein extracts. Suitable vitamins include retinol, retinyl palmitate, tocopherol, tocopherol acetate, menadione, ascorbic acid, ascorbyl palmitate, niacinamide (vitamin B3), panthenol (provitamin B5), biotin (vitamin B7), pyridoxine (vitamin B6), riboflavin (vitamin B2), thiamine (vitamin B1), folic acid (vitamin B9), cyanocobalamin (vitamin B12), cholecalciferol (vitamin D3), ergocalciferol (vitamin D2), phylloquinone (vitamin K1), and various plant-based vitamins and derivatives. Suitable preservatives, as approved by national cosmetic regulator bodies, include methylparaben, propylparaben, ethylparaben, butylparaben, benzyl alcohol, phenoxyethanol, sodium benzoate, potassium sorbate, chlorphenesin, ethylhexylglycerin, caprylyl glycol, benzalkonium chloride, triclosan, and various plant-derived preservatives such as grapefruit seed extract, rosemary extract, and tea tree oil. The efficacy of the invention is illustrated in the attached Figures, in which: Figure 1 shows the in situ visualization and quantification of Coll levels -Representative images of skin sections were obtained by epifluorescence microscopy. Coll is visualized in green. The specific labelling is superposed to the total cellular nuclei staining (in cyan, DAPI). Scale bar, 50 pm. Figure 2 shows the quantification of Coll levels - Specific Coll intensity levels are reported in the table 3 and as histograms (mean values ± SEM from n=3 images). P-values are calculated using one-way ANOVA and Dunnett’s post-hoc test - Multiple comparison vs Control group *, P <0.05; **, P <0,01; ***, P <0.001; ns, not significant. Figure 3 shows the in situ visualization and quantification of Col3 levels -Representative images of skin sections were obtained by epifluorescence microscopy. Col3 is visualized in green. The specific labelling is superposed to the total cellular nuclei staining (in cyan, DAPI). Scale bar, 50 pm. Figure 4 shows the quantification of Col3 levels - Specific Col3 intensity levels are reported in the table 4 and as histograms (mean values ± SEM from n=3 images). P-values are calculated using one-way ANOVA and Dunnett’s post-hoc test - Multiple comparison vs Control group *, P <0.05; **, P <0,01; ***, P <0.001; ns, not significant. Figure 5 shows the in situ visualization and quantification of Col5 levels -Representative images of skin sections were obtained by epifluorescence microscopy. Col5 is visualized in green. The specific labelling is superposed to the total cellular nuclei staining (in cyan, DAPI). Scale bar, 50 pm. Figure 6 shows the quantification of Col5 levels - Specific Col5 intensity levels are reported in the table 5 and as histograms (mean values ± SEM from n=3 images). P-values are calculated using one-way ANOVA and Dunnett’s post-hoc test - Multiple comparison vs Control group *, P <0.05; **, P <0,01; ***, P <0.001; ns, not significant. Figure 7 shows the in situ visualization and quantification of ELA levels -Representative images of skin sections were obtained by epifluorescence microscopy. ELA is visualized in green. The specific labelling is superposed to the total cellular nuclei staining (in cyan, DAPI). Scale bar, 50 pm. Figure 8 shows the quantification of ELA levels - Specific ELA intensity levels are reported in the table 6 and as histograms (mean values ± SEM from n=3 images). P- values are calculated using one-way ANOVA and Dunnett’s post-hoc test - Multiple comparison vs Control group *, P <0.05; **, P <0,01; ***, P <0.001; ns, not significant. The invention is further illustrated by reference to the following Examples. Example 1: Production of oat peptide powder isolate from an oat protein concentrate containing starch Example 1a): Oat protein concentrate (100kg) (PrOatein Oat protein™ by Lantmannen) was added to acidified water (900kg; pH 4.2) while mixing. The slurry was steam injected with culinary steam to a temperature of 72QC. An acidic alphaamylase was added (0.2% w / w) and the slurry mixed until no presence of starch was detected by I2. The slurry was cooled to 45QC before being centrifuged to remove the liquid stream. The solids were then washed with acidified water (pH 4.0) and centrifuged a second time. The solids were added to acidified water (pH 3.5) at a ratio of 1:100 and an acidic protease (Amano U-DS protease) was added. The slurry was allowed to mix at 45-50QC for 4 hours. The resulting mixture was processed by centrifugation to remove all remaining solids. The crude peptide extract was further filtered through a 0.45um cartridge filter before being processed by Ultrafiltration using a 50kDa membrane. The resulting permeate containing oat peptides was concentrated by reverse osmosis at 40QC. To the resulting concentrated oat peptides was added 2% w / w activated carbon and mixed at 40QC for 30 minutes. The resulting slurry was filtered through a 1 urn bag filter, followed by a 0.45um cartridge filter resulting in a purified, concentrated oat peptide solution. The solution was pH adjusted to 6 with NaOH (10%) and passed through a high temperature, short time (HTST) pasteurizer. The resulting solution was spray dried to produce a high purity (>85%) oat peptide powder. Example 1 b: In an alternative purification method, the liquid stream from the centrifuge after starch digestion was concentrated by reverse osmosis, neutralized to pH 7 with NaOH (10%), pasteurized by HTST and then spray dried producing a maltodextrin powder. Alternatively, the above liquid stream could be further processed with an amyloglucosidase / glycoamylase and concentrated to produce a syrup of high DE. Example 2: Production of oat peptide powder isolate from an oat peptide concentrate not containing starch Oat protein concentrate (100kg) (Sipal™ SipaPRO-Oat by Meurens Natural) was added to water (900kg) while mixing. An acidic enzyme (Viscozyme L) was added and the pH adjusted to 4.0-4.2. The slurry was allowed to mix for 2 hours at 45-50QC before being centrifuged to remove the liquid stream. The solids were then washed with acidified water (pH 4.0) and centrifuged a second time. The solids were added to acidified water (pH 3.5) at a ratio of 1:100 and an acidic protease (Amano U-DS protease) was added. The slurry was allowed to mix at 45-50QC for 4 hours. The resulting mixture was processed by centrifugation to remove all remaining solids. The crude peptide extract was further filtered through a 0.45um cartridge filter before being processed by Ultrafiltration using a 50kDa membrane. The resulting permeate containing oat peptides was concentrated by reverse osmosis at 40QC. To the resulting concentrated oat peptides was added 2% w / w activated carbon and mixed at 40C for 30 minutes. The resulting slurry was filtered through a 1 urn bag filter, followed by a 0.45um cartridge filter resulting in a purified, concentrated oat peptide solution. The solution was pH adjusted to 6 with NaOH (10%) and passed through a high temperature, short time (HTST) pasteurizer. The resulting solution was spray dried to produce a high purity (>85%) oat peptide powder. Example 3: Gene Expression Analysis - A study of how test material influences gene expression in the skin. A 3D in vitro skin model contain epidermal keratinocytes and dermal fibroblasts (Mattek EFT-400) was used. The epidermal keratinocytes are derived from the neonatal foreskin of a Caucasian male and the dermal fibroblasts are derived from the neonatal foreskin of a Caucasian male. Gene expression was assessed using Genemarkers Standard Skin Panel, a qPCR-based gene expression panel which contains 107 target genes that play important roles in skin biology, and 5 endogenous control genes. Four tissue replicates were included in each of the following groups: • TM2: 0.5% Oat peptides in water • VEH: Water (Vehicle Control) Cytotoxicity (LDH Assay) Cytotoxicity was assessed with a lactate dehydrogenase (LDH) assay using media 5 collected from the wells of the tissues. Increased LDH activity is an indicator of damaged or dead cells. A positive control (Triton X-100), was included in the analysis for reference. LDH analysis showed <10% cytotoxicity for all test groups (Graph 1). Gene Expression Statistically significant (unpaired t-test, p<0.05, N=4) changes in gene expression are shown in Table 1 and statistically significant (unpaired t-test, p<0.1, N=4) changes in gene expression are shown in Table 2 for TM2 vs the Vehicle Control group. Linear 15 fold change values (FC) are listed below, and % change is also listed as an alternative view of the data. FC values of 2 or greater are typically considered biologically relevant, with FC values of 1.5 or greater being relevant in the personal care industry. Gene ID vs. VEH water Oat Peptides 0.5% Associated Function(s) in Skin FC %△ COL1A1 1.52 52% Extracellular Matrix Integrity IL1B -3.44 -71% Inflammation / lmmune Response Gene ID vs. VEH water Oat Peptides 0.5% Associated Function(s) in Skin FC %△ COL1A1 1.52 52% Extracellular Matrix Integrity CXCL8 / IL8 -2.68 -63% Inflammation / lmmune Response IL1B -3.44 -71% Inflammation / lmmune Response IL23A -3.52 -72% Inflammation / lmmune Response MMP1 -1.95 -49% Extracellular Matrix Breakdown TIMP2 1.1 10% Extracellular Matrix Integrity TXN 1.13 13% Antioxidant / stress response This data showed that TM2 resulted in approximately a 50% increase in the expression of COL1A1. TM2 also decreased the expression of IL1B, a pro-5 inflammatory gene, suggesting anti-inflammatory properties. Changes in gene expression were observed over time frames varying from two hours to several days. Experimental Procedure The test material (TM) was provided as a solid powder and stored at room temperature (RT), protected from light until use. The TM was prepared in molecular 10 grade water to a 0.5% or 1 % working concentration. Tissue Equilibration: EFT-400 tissues (MatTek lot# 3214, Kits I and S) were equilibrated overnight at 37°C with 5% CO2 and -95% relative humidity. The following day, equilibration medium was removed from each well and replaced with 2.5mL fresh maintenance medium (MatTek EFT medium lot# 041221GSA). 15 Treatment and Maintenance of Cultures: Using a calibrated positive displacement pipette, a 15pL volume of TM was applied to the centre of each EFT-400 culture. Four cultures were included in each treatment group. A sterile glass spreader was used to distribute the topical material across the surface. Each culture was visually inspected to ensure even distribution. For the LDH (+) control tissues (N=1), 100 pL of 1% Triton X-100 was applied to the surface of each EFT culture; three untreated tissues served as the LDH (-) control tissues. Following topical application, cultures were returned to the incubator at 37°C with 5% CO2 and -95% relative humidity for 24 hours. Tissue and Medium Collections: After 24 hours, test medium from each tissue well was collected for an LDH assay (described below). For each tissue collection, the topical material was washed from the surface of the culture with sterile DPBS. Following the removal of the topical material, each culture was placed into a tube containing RNAIater preservative solution. Tissues were incubated for 1-2 hours at room temperature, and then transferred to a 4°C refrigerator until RNA was isolated. LDH Cytotoxicity Assay: An aliquot of used culture medium was diluted 1:10 with sterile Phosphate-Buffered Saline (PBS). Background control (diluted culture medium that was not used for the cell culture), “Low Control” (diluted treatment medium collected from the Untreated Culture wells), and “High Control” (diluted culture medium collected from the 1% Triton X-100 treated culture wells) samples were included in the assay. Each diluted sample was added to an optically clear, flat bottom 96-well plate in duplicate. The LDH reaction mixture (Takara) was prepared and added to each aliquot of diluted medium (1:1). The reaction plate was incubated for -20 minutes at room temperature, protected from light. Stopping solution (1 .ON HCI) was then added to each well and absorbance was measured at 492nm with a reference filter at 620nm. The absorbance value of each sample was calculated by subtracting the absorbance value of the blank sample from the mean OD492-OD620 value for the duplicate reaction wells. The % Cytotoxicity was then calculated relateive to the Untreated (negative control, set to 0% cytotoxicity) and the Triton X-100 treated (positive control, set to 100% cytotoxicity) absorbance values, according to kit instructions: % Cytotoxicity - [(Test Media Value - Low Control) / (High control - Low Control)]*100 RNA Isolation: RNA was isolated from each tissue using a Maxwell 16 Simply RNA Tissue kit (Promega) following the manufacturer’s instructions. If necessary, the RNA samples were vacuum-concentrated until the concentration was at or above 200ng / pL, as required for OpenArray processing. RNA concentration and purity were determined using a Nanodrop 2000 spectrophotometer (Table 3). cDNA synthesis: cDNA was generated using a High Capacity cDNA Synthesis Kit according to the manufacturer’s instructions (Applied Biosystems). cDNA was generated from 2000ng RNA per sample for OpenArray processing. qPCR Processing: qPCR reactions were run using validated Taqman® gene expression assays in an OpenArray format. OpenArrays were run in a Life Technologies QuantStudio 12K Flex instrument. Each gene was assayed in duplicate. Data Analysis: qPCR data quality and statistical analysis was assessed and performed of the raw data files using ThermoFisher Connect Software (Life Technologies). Statistical analysis was performed using the relative quantitation (RQ) method. In the first step of an RQ analysis, the Cq value of the target gene is normalized to the Cq value of an endogenous control gene to generate the delta Cq (dCq). dCq values are calculated in order to normalise for variability between the samples that may occur during the experimental procedures. See the Endogenous Control Gene Selection section for more details. Statistical Data Analysis Using ThermoFisher Connect Software: Unpaired t-tests were carried out using ThermoFisher Connect software. The statistical comparison generated delta delta Cq [dd Cq] values (the mean d Cq of the treated group - the mean d Cq of the control group). The statistical software converts the dd Cq values into log and linear RQ values for export [RQ = 2-2^]. The linear RQ values were converted to linear fold-change values to simplify data interpretation; linear fold change data was calculated form exported linear RQ values using Microsoft Excel: • For RQ values >1.0: Linear fold-change value = RQ value • For RQ values <1.0: Linear fold-change value = -1 / RQ value RNA Quality Sample concentration and purity were determined using a Nanodrop spectrophotometer. A260 / 280 readings indicate sample purity with idea measurements that range from 1.8-2.1. The A260 / 230 ratio is an additional measure of sample purity where a value of 1.0 or greater is ideal. All samples showed high quality RNA metrics (Table 3). Sample ID Group Vacuum Concentration ng / pL RNA 260 / 280 260 / 230 D21-092 0.5% Oat Peptides 250.6 2.12 2.17 D21-093 0.5% Oat Peptides 269.9 2.12 2.04 D21-094 0.5% Oat Peptides 292.2 2.12 2.18 D21-095 0.5% Oat Peptides 219.9 2.11 2.15 D21-096 water 305.2 2.11 2.17 D21-097 water 224.6 2.11 2.14 D21-098 water 333.4 2.12 2.13 D21-099 water 225.2 2.11 2.16 Endogenous Control Gene Selection 5 It is important to select an endogenous control gene that is consistently expressed in all of the samples of a comparison. Five candidate control genes (GAPDH, GUSB, HPRT1, PPIA, and UBC) were analysed. The most consistent endogenous control gene was chosen based on the stability score given by the Thermo Fisher Data Connect RQ software. Lower stability scores represent more consistent expression 10 between samples in the study. The stability scores for each endogenous control are shown below (Table 4). Based on the stability score, PPIA was selected as the endogenous control. Statistics (unpaired t-tests) were carried out for each comparison using dCq values normalised to PPIA. Gene ID Gene Name Stability Score GAPDH Glyceraldehyde 3-phosphate dehydrogenase 0.153 GUSB Glucuronidase Beta 0.174 HPRT1 Hypoxanthine Phosphoribosyltransferase 1 0.139 PPIA Peptidylprolyl Isomerase A 0.133 UBC Ubiquitin C 0.138 qPCR Data Quality and Statistical Data Analysis qPCR data quality is assessed using a combination of factors, including visual analysis of the shape of the qPCR curve and Cq value. Cq values are an indication of the total amount of transcript present in the sample and can impact the quality of the qPCR data. qPCR amplification takes place over a total of 40 cycles, and typically occurs before cycle 28. The relative amount of the gene transcript level is associated with the Cq value of the PCR reaction. Cq values typically correspond with the following: • Cq values less than 28: associated with high transcript levels and robust, high quality PCR data • Cq values greater than 28: lower level transcripts, less robust qPCR data; review data cautiously. All of the genes in the study amplified with Cq values <28. Two genes that showed high quality qPCR amplification curves with Cq values less than 28 are keratin 1 (KRT1) which is associated with the epidermal barrier, and serpin family B member 3 (SERPINB3) which is associated with extracellular matrix breakdown. Efficacy Study The efficacy of three products (A, B and C) at one concentration on ex vivo skin explants at basal level was evaluated through the evaluation of: 1. Collagen 1 (Coll) levels as a structural biomarker of dermis associated with skin firmness 2. Collagen 3 (Col3) levels as a structural biomarker of dermis associated with skin remodelling 3. Collagen 5 (Col5) levels as a structural biomarker of dermis associated with skin firmness 4. Elastin (ELA) levels as a biomarker of skin elasticity and pumping. The products (A, B, and C) were received from the sponsor and inventoried at Oxiproteomics. Skin explants were obtained with the informed consent from abdominal surgery of a 37-year- old female Caucasian donor (phototype III, Ref. 20230928-F37Yo) and cultured in Oxi Proteomics® medium at 37°C in 5% CO2 humidified air. Products were topically applied on skin explants at the dose of 2 mg / cm2 and renewed twice a day for 3 consecutive days. Twenty-four (24) hours after the last application, the explants were sampled and then skin explants were prepared for biomarkers analysis. Summary of Results When compared to the control: • the Product A at 0.1 % increased Col 1 levels by 5% and Col 5 by 13% • the Product B at 0.5% increased Col 1 levels by 4% and Col 5 by 19% • the Product C at 0.5% increased Col 1 levels by 4% and Col 5 by 10%. The presence of the tested Products showed positive effects on dermis structural component suggesting a beneficial effect on boosting skin firmness. When compared to the control, the Product A at 0.1%, and Product C at 0.5% significantly increased the levels of Col3 by 20%. The presence of the tested Product A and C showed positive effects on dermis suggesting a beneficial effect on boosting skin remodelling. Compared to the control group, the levels of Elastin showed significant increases of 19% for Product A at a concentration of 0.1% and 11% for Product B at a concentration of 0.5%. The presence of the tested Product A and B showed positive effects on elastin fibres suggesting a beneficial effect on boosting skin elasticity and pumping. Tested Products Product details Internal Index Batch / lnformation Other details Product A (P303) PGE0623AECO - Product A : 7536 Oat Peptide Product B (P304) PGE0623AECO - Product B : 7536 Oat Peptide Product C (P305) 0002156733 - Product C Matrixyl ® 3000 See also Table 11 for peptide content of batch PGE0623AECO. Products A and B comprise the same peptide at different concentrations (0.1% and 0.5% respectively). Experimental Procedure Skin explants were obtained with the informed consent from abdominal surgery of a 37-year- old female Caucasian donor (phototype III, Ref. 20230928-F37Yo). After surgery, they were kept alive by culturing on metal grids into standard 12-well plates in contact in Oxi Proteomics® medium at 37°C in 5% CO2 humidified air. After reception, the explants were distributed in 5 experimental groups (n=3 per group; Table 6), the culturing medium was renewed every 24 hours. The products were topically applied on skin explants at the dose of 2 mg / cm2 and maintained in contact twice a day for 3 consecutive days. Twenty-four (24) hours after the last application, the explants were sampled, transferred in OCT for cryopreservation and snap-frozen in liquid nitrogen and conserved at -80°C until analysis. The control group did not receive any treatment or exposure, except for the renewal of the culture medium. Experimental Results Batch Description Treatment 1 Control Not Treated 2 Vehicle Control Twice a day for 3 days treated 3 Product A at 0.1% Twice a day for 3 days treated 4 Product B at 0.5% Twice a day for 3 days treated 5 Product C at 0.5% Twice a day for 3 days treated Explant sections of 5 pm of thickness were obtained using a cryostat (Leica) and fixed with a solution containing 95% Ethanol and 5% acetic acid for 10 min. A saturating step of the non- specific sites was carried out with a solution of PBS containing 3% BSA (PBS-BSA). Skin sections were incubated with primary antibodies targeting Coll (Abeam I ab34710), Col3 (Abeam I ab34710), Col5 (Abeam / ab7046) and Ela (Santa Cruz I sc-166543). The excess of primary antibodies was eliminated with washing steps with a PBS containing 0.1% Tween (PBS-T) solution, then cells were then incubated for 1 hour with the secondary antibody coupled to a fluorophore (lnvitrogen / A21244 or lnvitrogen / A21235) in PBS-BSA. The cellular nuclei were labelled with using 4',6-diamidino-2-phenylindole (DAPI). Finally, the antibody and DAPI excess were removed with a sequence of washing steps with PBS-T. Fluorescent images were collected with an epi-fluorescent microscope (EVOS M5000 Imaging System) and analysed with Imaged software (Schneider, 2012). The source images (16bit, format .TIFF) were collected in a full range of intensity of specific signal from and analysed with Imaged software. The images were collected using strictly the same acquisition time and resolution per series of acquisition (10x and 40X objective). The quantification of biomarker levels was carried out by the integration of the specific signal intensity over threshold normalized by the evaluated surface including three (3) replicates per condition. One (1) representative image per condition was realized and annexed in D12EG2023.ppt file in HD format. Analysis The quantification of biomarkers was normalized in relation to the control (considered at 100%). A mean value and a standard deviation were obtained per condition. Statistical analyses were carried out using the “GraphPad” software (La Jolla, California, USA) by using one-way ANOVA and Dunnett’s post-hoc test for multi-comparisons analyses (vs Control group, confidence interval of 95%). The raw data and their integrations are included in Annex- D12EG2023.pptx and Annex-D12EG2023.xlsx files. An induction (or increase) value (%) was obtained for the experimental groups using the control group as reference: Induction % (group x) = Biomarker level (group x) -1 * 100 Biomarker level (control) The Coll levels (%) are reported in the following table (Table 7) and bar graph representation (Figure 2) as mean values + / - SD per experimental group normalized to the control. The treatments of cells with Product A (0.1%), B (0.5%), and C (0.5%) significantly increased Coll levels (5%, 4%, and 4% of induction, respectively) in comparison to control. Collagen 1 levels Exp. Group Coll levels (MEAN) Std. Dev. p-Value (vs Control) Induction (% vs Control) N Control 100 0 / / 3 Vehicle Control 100 1 ns 0% 3 Product A 0.1% 105 2 ** 5% 3 Product B 0.5% 104 2 ** 4% 3 Product C 0.5% 104 1 * 4% 3 The Col3 levels (%) are reported in the following table (Table 8) and bar graph representation (Figure 4) as mean values + / - SD per experimental group normalized to the control. The treatments of cells with Product A (0.1%), and C (0.5%) 5 significantly increased Col3 levels (20%, and 20% of induction, respectively) in comparison to control. Collagen 3 levels Exp. Group Col3 levels (MEAN) Std. Dev. p-Value (vs Control) Induction (% vs Control) N Control 100 4 / / 3 Vehicle Control 100 2 ns 0% 3 Product A 0.1% 120 2 *** 20% 3 Product B 0.5% 101 4 ns 1% 3 Product C 0.5% 120 1 *** 20% 3 The Col5 levels (%) are reported in the following table (Table 9) and bar graph representation (Figure 6) as mean values + / - SD per experimental group normalized 10 to the control. The treatments of cells with Product A (0.1 %), Product B (0.5%), and C (0.5%) significantly increased Col5 levels (13%, 19% and 10% of induction, respectively) in comparison to control. Collagen 5 levels Exp. Group Col5 levels (MEAN) Std. Dev. p-Value (vs Control) Induction (% vs Control) N Control 100 2 / / 3 Vehicle Control 101 3 ns 0% 3 Product A 0.1% 113 2 *** 13% 3 Product B 0.5% 119 2 *** 19% 3 Product C 0.5% 110 2 *** 10% 3 The ELA levels (%) are reported in the following table (Table 10) and bar graph 5 representation (Figure 8) as mean values + / - SD per experimental group normalized to the control. The treatments of cells with Product A (0.1%), and B (0.5%) significantly increased ELA levels (19%, and 11% of induction, respectively) in comparison to control, while Product C (0.5%) significantly decrease ELA levels. Elastin levels Exp. Group Col5 levels (MEAN) Std. Dev. p-Value (vs Control) Induction (% vs Control) N Control 100 2 / / 3 Vehicle Control 99 2 ns 0% 3 Product A 0.1% 119 1 *** 19% 3 Product B 0.5% 111 6 ** 11% 3 Product C 0.5% 85 2 *** 0% 3 Example formulations, prepared using the oat peptide isolate of the invention, are provided below. Example 4: Structural peptide analysis 5 The peptide structure present in oat peptide isolate produced according to the method of the invention (as described herein and in Examples 1 and 2), can be seen in Table 11. The efficacy studies described herein were carried out on Batch PGE0623AECO in Table 11 (see also Table 5). In general, it was found that processing time affected the peptide structure, with long 10 processing times (in excess of 16 hours) leading to low molecular weight peptides in the resulting product. EcoPep - Peptide sequencing Batch DF20201103C PGE0623AECO DF20240628B T+4 DF20240627J T+16 Starting material Proatein (Lantmannen) Proatein (Lantmannen) NatuPRO-Oat (Meurens) NatuPRO-Oat (Meurens) Enzyme choping time - 4 hours 4 hours 16 hours Sample preparation Treated with dithiothreitol and iodoacetamide and desalted with C18 Dissolve with 0.1% of Trifluoroacetic acid and desalted Dissolve with 0.1% of Trifluoroacetic acid and desalted Dissolve with 0.1% of Trifluoroacetic acid and desalted Method LC-MS nano LC-MS / MS nano LC-MS / MS nano LC-MS / MS Total peptide detected 4714 24279 32951 25314 Average Molecular Weight (Da) 1845 981 865 824 Max Molecular Weight (Da) 4886 2106 3922 3097 Min Molecular Weight (Da) 755 357 356 351 Average Peptide Length 24.2 8.8 7.7 7.3 Max Peptide Length 49 20 33 29 Min Peptide Length 16 3 3 3 Molecular weight Peptides distribution DF20201103C PGE0623AECO DF20240628BT+4 DF20240627J T+16 5000 - 3000 Da 13% 0% 0% 0% 3000 -1000 Da 85% 57% 41% 31% 1000 - 500 Da 2% 41% 53% 62% < 500 Da 0% 2% 6% 7% Table 11: peptide composition Example 5: Formulations Formulation 1 - Aftersun Lotion Ingredient %w / w 5 Aqua to 100.000 Hydrated silica 5.000 Isopropyl palmitate 4.000 Arachidyl propionate 2.000 Dimethicone 2.000 10 Glycerin 2.000 Steareth-21 1.960 Steareth-2 1.683 Cetyl alcohol 1.000 Tribehenin 1.000 15 Glyceryl stearate 1.000 Paraffinum liquidum 0.994 Panthenol 0.750 Parfum 0.300 Xanthan gum 0.300 Sodium citrate 0.250 Oat Peptide 0.500 Tocopheryl acetate 0.200 Hydroxyethylcellulose 0.100 Bisabolol 0.095 Citric acid 0.050 Preservative q.s Extruded colloidal oatmeal 5.000 Method 1. The citric acid, sodium citrate and hydroxyethylcellulose are added to the water. Using a propeller stirrer, the mixture is stirred until dispersed. The xanthan gum is pre-dispersed in the glycerin and this is then added to the bulk, which is then heated to 70°C. 2. The isopropyl palmitate, arachidyl propionate, dimethicone, steareth-21, steareth-2, cetyl alcohol, tribehenin, glyceryl stearate, paraffinum liquidum are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, step 2 is added to step 1 and is mixed until emulsified and uniform. The emulsion is cooled to below 35° C using stirring. Once below 35°C, the remaining materials are added, including the Extruded colloidal oatmeal. The product is made to weight using purified water, and mixed until uniform. Formulation 2 - Aftersun Lotion Ingredient %w / w Aqua to 100.000 Hydrated silica 5.000 Isopropyl palmitate 4.000 Arachidyl propionate 2.000 Dimethicone 2.000 Glycerin 2.000 Steareth-21 1.960 Steareth-2 1.683 Cetyl alcohol 1.000 Tribehenin 1.000 Glyceryl stearate 1.000 Paraffinum liquidum 0.994 Panthenol 0.750 Oat peptide 1.000 Parfum 0.300 Xanthan gum 0.300 Sodium citrate 0.250 Tocopheryl acetate 0.200 Hydroxyethylcellulose 0.100 Bisabolol 0.095 Citric acid 0.050 Preservative q.s Extruded colloidal oatmeal 10.000 Method 1. The citric acid, sodium citrate and hydroxyethylcellulose are added to the water. Using a propeller stirrer, the mixture is stirred until dispersed. The xanthan gum is pre-dispersed in the glycerin and this is then added to the bulk, which is then heated to 70°C. 2. The isopropyl palmitate, arachidyl propionate, dimethicone, steareth-21, steareth-2, cetyl alcohol, tribehenin , glyceryl stearate, paraffinum liquidum are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, step 2 is added to step 1 and is mixed until emulsified and uniform. The emulsion is cooled to below 35° C using stirring. Once below 35°C, the remaining materials are added, including the Extruded colloidal oatmeal. The product is made to weight using purified water, and mixed until uniform. Formulation 3 - Dav Cream Ingredient Aqua %w / w to 100.000 Butylene glycol 5.000 Dicaprylyl maleate 4.000 Paraffinum liquidum 4.000 Octyl methoxycinnamate 3.000 Petrolatum 3.000 Cetyl Alcohol 2.000 Glycerin 2.000 Dimethicone 2.000 Cetearyl alcohol 1.600 Butyl methoxydibenzoylmethane 1.000 Hydroxyethylcellulose 0.400 PEG-20 stearate 0.400 Polyacrylamide 0.400 Parfum 0.300 C13-14 isoparaffin 0.215 Retinyl palmitate 0.150 Tetrasodium EDTA 0.100 Citric acid 0.080 Laureth-7 0.055 Oat Peptide 1.000 Extruded colloidal oatmeal 1.000 Preservative q.s Method 1. Tetrasodium EDTA and citric acid are added to the water using a propeller stirrer. The hydroxyethylcellulose is added and dispersed using a homogeniser. butylene glycol, glycerin and methylparaben are added and the bulk is heated to 70°C. 2. The dicaprylyl maleate, paraffinum liquidum, octyl methoxycinnamate, petrolatum, cetyl alcohol, dimethicone, cetearyl alcohol, butyl methoxydibenzoylmethane, PEG-20 stearate, C13-14 isoparaffin, laureth-7 and BHT are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and the bulk is mixed until emulsified and stable. The product is then cooled to below 35°C using stirring. The remaining raw materials, including the Extruded colloidal oatmeal are added and the product is mixed using a propeller stirrer until uniform. The product is made to weight using purified water. 5 Formulation 4 - Dav Cream Ingredient %w / w Aqua to 100.000 Butylene glycol 5.000 Dicaprylyl maleate 4.000 10 Paraffinum liquidum 4.000 Octyl methoxycinnamate 3.000 Petrolatum 3.000 Cetyl Alcohol 2.000 Glycerin 2.000 15 Dimethicone 2.000 Cetearyl alcohol 1.600 Butyl methoxydibenzoylmethane 1.000 Hydroxyethylcellulose 0.400 PEG-20 stearate 0.400 20 Polyacrylamide 0.400 Parfum 0.300 C13-14 isoparaffin 0.215 Retinyl palmitate 0.178 Tetrasodium EDTA 0.100 25 Citric acid 0.080 Laureth-7 0.055 Oat Peptide 0.500 Preservative q.s 30 Method 1. Tetrasodium EDTA and citric acid are added to the water using a propeller stirrer. The hydroxyethylcellulose is added and dispersed using a homogeniser. butylene glycol, glycerin and methylparaben are added and the bulk is heated to 70°C. 2. The dicaprylyl maleate, paraffinum liquidum, octyl methoxycinnamate, petrolatum, cetyl alcohol, dimethicone, cetearyl alcohol, butyl methoxydibenzoylmethane, PEG-20 stearate, C13-14 isoparaffin, laureth-7 and BHT are mixed and heated to 70°C to melt the waxes. 5 3. Using a homogeniser, stage 2 is added to stage 1 and the bulk is mixed until emulsified and stable. The product is then cooled to below 35°C using stirring. The remaining raw materials are added, and the product is mixed using a propeller stirrer until uniform. The product is made to weight using purified water. 10 Formulation 5 - Sun Lotion %w / w Ingredient Aqua to 100.000 C12-15 Alkyl Benzoate 8.000 15 Butylene glycol 5.000 Butyl methoxydibenzoylmethane 2.200 Dimethicone 2.000 Polyglyceryl-3 methylglucose distearate 2.000 PVP / hexadecene copolymer 1.750 20 Octyl methoxycinnamate 1.700 Theobroma cacao 0.500 Parfum 0.500 Tocopheryl acetate 0.200 Acrylates / vinyl isodecanoate crosspolymer 0.150 25 Potassium hydroxide 0.034 Tetrasodium EDTA 0.020 Preservative q.s Oat lipid Complex 3.000 Oat Peptide 0,250 30 Method 1. The EDTA is dispersed into the water. Using a propeller stirrer, the acrylates / vinyl isodecanoate crosspolymer are added and dispersed and hydrated. Butylene glycol is added and the aqueous phase is heated to 70°C. 2. The C12-15 alkyl benzoate, butyl methoxydibenzoylmethane, dimethicone, polyglyceryl-3 methylglucose distearate, PVP / hexadecene copolymer, octyl methoxycinnamate, theobroma cacao. Oat lipid complex and tocopheryl acetate are mixed and heated to 70°C to melt the waxes. 5 3. Using a homogeniser, stage 2 is added to stage 1 and the bulk is mixed until emulsified and uniform. The emulsion is cooled to below 35°C with stirring. The remaining materials are added and mixed. The product is made to weight using purified water and stirred until uniform. 10 Formulation 6 - Sun Lotion %w / w to 100.000 8.000 Aqua C12-15 Alkyl Benzoate Butylene glycol 5.000 15 Butyl methoxydibenzoylmethane 2.200 Dimethicone 2.000 Polyglyceryl-3 methylglucose distearate 2.000 PVP / hexadecene copolymer 1.750 Octyl methoxycinnamate 1.700 20 Theobroma cacao 0.500 Parfum 0.500 Tocopheryl acetate 0.200 Acrylates / vinyl isodecanoate crosspolymer 0.150 Potassium hydroxide 0.034 25 Tetrasodium EDTA 0.020 Preservative q.s Extruded colloidal oatmeal 5.000 Oat Peptide 1.000 30 Method 1. The EDTA is dispersed into the water. Using a propeller stirrer, the acrylates / vinyl isodecanoate crosspolymer are added and dispersed and hydrated. Butylene glycol is added, and the aqueous phase is heated to 70°C. 2. The C12-15 alkyl benzoate, butyl methoxydibenzoylmethane, dimethicone, polyglyceryl-3 methylglucose distearate, PVP / hexadecene copolymer, octyl methoxycinnamate, theobroma cacao and tocopheryl acetate are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and the bulk is mixed until emulsified and uniform. The emulsion is cooled to below 35°C with stirring. The remaining materials, including the Extruded colloidal oatmeal are added and mixed. The product is made to weight using purified water and stirred until uniform. Formulation 7 - Sunburn Treatment %w / w Aqua to 100.000 Petrolatum 3.000 Cetyl Alcohol 2.000 Dimethicone 2.000 Glycerin 2.000 Ceteath-20 1.700 Paraffinum Liquidum 1.000 Sodium chloride 0.800 Theobroma cacao 0.700 Glyceryl stearate 0.500 Parfum 0.300 Allantoin 0.200 Hydroxyethylcellulose 0.100 Triclosan 0.100 Citric acid 0.020 Preservative q.s Extruded colloidal oatmeal 10.000 Oat lipid Complex 2.000 Oat Peptide 0.500 Method 1. Into the water, sodium chloride and citric acid are added and dispersed. Using a propeller stirrer, hydroxyethylcellulose is added and dispersed. This phase is then heated to 70°C. 2. The petrolatum, cetyl alcohol, dimethicone, ceteath-20, paraffinum liquidum, theobroma cacao, oat lipid comlex and glyceryl stearate are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1, this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C with stirring. The remaining materials, including the Extruded colloidal oatmeal are then added and mixed. The product is made to weight using purified water and stirred until uniform. Formulation 8 - Sunburn Treatment %w / w Aqua to 100.000 Petrolatum 3.000 Cetyl Alcohol 2.000 Dimethicone 2.000 Glycerin 2.000 Ceteath-20 1.700 Paraffinum Liquidum 1.000 Sodium chloride 0.800 Theobroma cacao 0.700 Glyceryl stearate 0.500 Parfum 0.300 Allantoin 0.200 Hydroxyethylcellulose 0.100 Triclosan 0.100 Citric acid 0.020 Preservative q.s Extruded colloidal oatmeal 7.000 Oat Peptide 1.000 Method 1. Into the water, sodium chloride and citric acid are added and dispersed. Using a propeller stirrer, hydroxyethylcellulose is added and dispersed. This phase is then heated to 70°C. 2. The petrolatum, cetyl alcohol, dimethicone, ceteath-20, paraffinum liquidum, theobroma cacao and glyceryl stearate are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1, this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C with stirring. The remaining materials, including the Extruded colloidal oatmeal are then added and mixed. The product is made to weight using purified water and stirred until uniform. Formulation 9 - Eye Cream %w / w Aqua to 100.000 Butylene glycol 6.000 Paraffinum liquidum 5.000 Octyl methoxycinnamate 4.000 Dimethicone 2.000 Petrolutum 2.000 Cetearyl octanoate 1.800 Cetearyl alcohol 1.600 Glyceryl stearate 1.500 Cetyl alcohol 1.000 Prunus dulcis 1.000 Glycerin 0.570 Hydrogenated vegetable glycerides citrate 0.500 Tocopheryl acetate 0.500 Bisabolol 0.475 Panthenol 0.450 Sodium phosphate 0.420 PEG-20 stearate 0.400 Isopropyl myristate 0.200 Carbomer 0.150 PEG-12 isostearate 0.125 Allantoin 0.100 Tetrasodium EDTA 0.100 Lactic acid 0.088 Disodium phophate 0.083 Potassium hydroxide 0.051 Oat Lipid Complex 1.000 Oat peptide 0.250 Preservative q.s Method 1. Into the water, citric acid, EDTA, sodium phosphate, disodium phosphate and lactic acid are added and dispersed. Using a homogeniser, carbomer is added and hydrated. The aqueous phase is then heated to 70°C. 2. The paraffinum liquidum, octyl methoxycinnamate, dimethicone, petrolatum, cetearyl octanoate, cetearyl alcohol, glyceryl stearate, cetyl alcohol, hydrogenated vegetable glycerides citrate, tocopheryl acetate, PEG-20 stearate, isopropyl myristate, oat lipid complex and PEG-12 isostearate are mixed and heated to 70°Cto melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials, including the Extruded colloidal oatmeal are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. Formulation 10 - Eye Cream Aqua Butylene glycol Paraffinum liquidum Octyl methoxycinnamate Dimethicone Petrolutum Cetearyl octanoate %w / w to 100.000 6.000 5.000 4.000 2.000 2.000 1.800 Cetearyl alcohol 1.600 Glyceryl stearate 1.500 Cetyl alcohol 1.000 Prunus dulcis 1.000 Glycerin 0.570 Hydrogenated vegetable glycerides citrate 0.500 Tocopheryl acetate 0.500 Bisabolol 0.475 Panthenol 0.450 Sodium phosphate 0.420 PEG-20 stearate 0.400 Isopropyl myristate 0.200 Carbomer 0.150 PEG-12 isostearate 0.125 Allantoin 0.100 Tetrasodium EDTA 0.100 Lactic acid 0.088 Disodium phophate 0.083 Potassium hydroxide 0.051 Extruded colloidal oatmeal 4.000 Oat Peptide 0.500 Preservative q.s Method 1. Into the water, citric acid, EDTA, sodium phosphate, disodium phosphate and lactic acid are added and dispersed. Using a homogeniser, carbomer is added and hydrated. The aqueous phase is then heated to 70°C. 2. The paraffinum liquidum, octyl methoxycinnamate, dimethicone, petrolatum, cetearyl octanoate, cetearyl alcohol, glyceryl stearate, cetyl alcohol, hydrogenated vegetable glycerides citrate, tocopheryl acetate, PEG-20 stearate, isopropyl myristate and PEG-12 isostearate are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials, including the Extruded colloidal oatmeal are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. Formulation 11 Eye Gel %W / W Aqua to 100.000 PVP / VA copolymer 2.000 Propylene glycol 2.000 Carbomer 1.000 PEG-40 hydrogenated castor oil 1.000 Panthenol 1.000 Sodium hydroxide 0.300 Phenoxyethanol 0.200 Tetrasodium EDTA 0.100 Oat Peptide 0.500 Method 1. The EDTA, Methyldibromo glutaronitrile, PVP / VA copolymer and Carbomer were added to the water and mixed using a homogeniser to ensure that the polymers were hydrated. 2. With continued homogenising, the Cystine hydroxypropyl polysiloxane was added and mixed into the product. 3. The remaining materials were added individually and mixed using a prop. Stir until the product was homogenous. Formulation 12- Refreshing cream %w / w Aqua to 100.000 Butylene glycol 7.500 Silica 7.200 Arabinogalactan 5.350 Dimethicone 5.350 Petrolatum 5.350 Hydrated silica 3.750 Steareth-2 2.700 Prunus dulcis 2.700 Steareth-21 0.900 PVP / hexadecene copolymer 0.800 Carbomer 0.320 Sodium PCA 0.200 Parfum 0.200 Hydroxyethylcellulose 0.160 Potassium hydroxide 0.100 Propylene glycol 0.100 Oat peptide 1.000 Preservative q.s Method 1. Into the water, the carbomer is added and hydrated using a homogeniser. The aqueous phase is then heated to 70°C. 2. The silica, arabinogalactan, PVP / hexadecene copolymer, dimethicone, petrolatum, hydrated silica, steareth-2 and steareth-21 are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. Formulation 13-Skin Protection Lotion %w / w Aqua to 100.000 Dimethicone 5.000 Glycerin 3.000 Kaolin 3.000 Dicaprylyl maleate 2.500 Isopropyl myristate Stearate-2 2.500 2.000 Octyl methoxycinnamate Steareth-21 1.000 1.000 Cetyl alcohol Butyl methoxydibenzoylmethane Propylene glycol Hydroxyethylcellulose Xanthan gum Serica 0.750 0.500 0.500 0.400 0.240 0.100 Sodium C8-16 isoalkylsuccinyl lactoglobulin sulfonate Tetrasodium EDTA 0.100 0.100 Citric acid 0.050 Oat Peptide Oat lipid complex Preservative 1.000 5.000 q.s Method 1. Into the water, the citric acid and EDTA are added and dispersed. The hydroxyethylcellulose is added and hydrated using a propeller stirrer. Xanthan gum is pre-dispersed in glycerin and added to the bulk. This is stirred until uniform. The aqueous phase is then heated to 70°C. 2. The dimethicone, dicaprylyl maleate, isopropyl myristate, stearate-2, octyl methoxycinnamate, steareth-21, cetyl alcohol oat lipid complex and butyl methoxydibenzoylmethane are mixed and heated to 70 °C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. Formulation 14 - Night Cream Aqua %w / w to 100.000 Glycerin Paraffinum liquidum Dicaprylyl maleate Dimethicone 5.000 4.500 3.000 3.000 5 Petrolatum 3.000 Paraffin 2.900 Cetyl alcohol 2.000 Steareth-2 2.000 Glyceryl stearate 1.500 10 Butyrospermum parkii 1.500 Steareth-21 1.000 Mannitol 1.000 Cera microcristallina 0.262 Buxus chinensis 0.50 15 Propylene glycol 0.480 Parfum 0.400 Borago officinalis 0.300 Hydroxyethylcellulose 0.300 Lactis proteinum 0.300 20 Xanthan gum 0.250 Alcohol denat. 0.080 Sodium citrate 0.080 Lecithin 0.075 Rosemary Extract 0.250 25 Faex 0.040 Phospholipids 0.030 Citric acid 0.025 Oat Lipid Complex 5.000 Oat peptide 0.500 30 Preservative q.s Method 1. Into the water, the citric acid and sodium citrate are added and dispersed. The hydroxyethylcellulose is added and hydrated using a propeller stirrer. Xanthan gum is pre-dispersed in glycerin and added to the bulk. This is stirred until uniform. The aqueous phase is then heated to 70°C. 2. The paraffinum liquidum, dicaprylyl maleate, dimethicone, petrolatum, paraffin, cetyl alcohol, steareth-2 , glyceryl stearate, steareth-21, cera microcristallina and oat lipid complex are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials, including the Extruded colloidal oatmeal are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. Formulation 15 - Sun Lotion for Sensitive Skin %w / w Aqua to 100.000 C12-15 alkyl benzoate 12.000 Butylene glycol 5.000 Octyl methoxycinnamate 3.800 Butyl methoxydibenzoylmethane 3.000 Dimethicone 2.000 Polyglyceryl-3 methylglucose distearate 2.000 PVP / hexadecene copolymer 1.750 C18-36 acid glycol ester 1.500 Polysorbate 60 0.500 Titanium dioxide 0.300 Tocopheryl acetate 0.200 Acrylates / vinyl isodecanoate crosspolymer 0.140 Potassium hydroxide 0.035 Tetrasodium EDTA 0.020 Oat Peptide 0.500 Preservative q.s Extruded colloidal oatmeal 4.500 Method 1. Into the water, citric acid is added and dispersed. The acrlyates / vinyl isodecanoate crosspolymer are added and dispersed using a propeller stirrer. The aqueous phase is then heated to 70°C. 2. The C12-15 alkyl benzoate, PVP / hexadecene copolymer, octyl methoxycinnamate, butyl methoxydibenzoylmethane, dimethicone, polyglyceryl-3 methylglucose distearate, C18-36 acid glycol ester, polysorbate 60, titanium dioxide and tocopheryl acetate are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials, including the Extruded colloidal oatmeal are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. Formulation 16 - Sun Lotion for Sensitive Skin %w / w Aqua to 100.000 C12-15 alkyl benzoate 12.000 Butylene glycol 5.000 Octyl methoxycinnamate 3.800 Butyl methoxydibenzoylmethane 3.000 Dimethicone 2.000 Polyglyceryl-3 methylglucose distearate 2.000 PVP / hexadecene copolymer 1.750 C18-36 acid glycol ester 1.500 Polysorbate 60 0.500 Titanium dioxide 0.300 Tocopheryl acetate 0.200 Acrylates / vinyl isodecanoate crosspolymer 0.140 Potassium hydroxide 0.035 Tetrasodium EDTA 0.020 Preservative q.s Extruded colloidal oatmeal 10.000 Oat Peptide 0.500 Method 1. Into the water, citric acid is added and dispersed. The acrylates / vinyl isodecanoate crosspolymer are added and dispersed using a propeller stirrer. The aqueous phase is then heated to 70°C. 2. The C12-15 alkyl benzoate, PVP / hexadecene copolymer, octyl methoxycinnamate, butyl methoxydibenzoylmethane, dimethicone, polyglyceryl-3 methylglucose distearate, C18-36 acid glycol ester, polysorbate 60, titanium dioxide and tocopheryl acetate are heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials, including the Extruded colloidal oatmeal are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. . Formulation 17 - Anti-ageing Foundation %w / w Aqua to 100.000 Butylene glycol 9.800 Cetearyl isononanoate 4.900 Dimethicone 3.200 Glycerin 1.960 Silica 1.900 Caprylic / capric triglyceride 1.670 Paraffinum liquidum 1.670 Petrolatum 1.670 Hydrogenated coco-glycerides 1.670 Cetearyl octanoate 1.500 Cetearyl alcohol 1.350 Octyl methoxycinnamate 1.280 Talc 1.000 Glyceryl stearate 0.950 PEG-100 stearate 0.900 Butyl methoxydibenzoylmethane 0.600 Saccharide isomerate 0.540 Lactic acid 0.450 Sodium polyacrylate 0.450 Boron nitride 0.420 Sodium PCA 0.400 Borago officinalis 0.400 Tocopheryl acetate 0.400 PVP / hexadecene copolymer 0.400 PEG-20 stearate 0.330 Glycolic acid 0.200 Sodium stearoyl lactylate 0.200 Isopropyl myristate 0.170 Polyaminopropyl biguanide 0.160 Tetrasodium EDTA 0.100 Xanthan gum 0.100 Citric acid 0.060 Alcohol denat. 0.040 Lecithin 0.037 Preservative q.s Oat Peptide 1.000 Method 1. Into the water, citric acid, EDTA and lactic acid are added and dispersed. Xanthan gum is pre-dispersed in butylene glycol and is added to the bulk. The aqueous phase is then heated to 70°C. 2. The cetearyl isononanoate, dimethicone, silica, PVP / hexadecene copolymer, caprylic / capric triglyceride, paraffinum liquidum, petrolatum, hydrogenated coco-glycerides, cetearyl octanoate, cetearyl alcohol, octyl methoxycinnamate, talc, glyceryl stearate, PEG-100 stearate, butyl methoxydibenzoylmethane, borago officinalis, tocopheryl acetate, sodium stearoyl lactylate, isopropyl myristate and lecithinoil phase are mixed and heated to 70°C to melt the waxes. 3. Using a homogeniser, stage 2 is added to stage 1 and this is mixed until emulsified and uniform. The emulsion is then cooled to below 35°C using stirring. The remaining materials are then added and mixed. The product is then made to weight using purified water and is stirred until uniform. Formulation 18 - Toner &Cleanser 2 In 1 %w / w Alcohol denat. 48.000 Aqua PEG-8 to 100.000 6.000 Glycerin Propylene glycol 2.000 0.500 Sodium C8-16 isoalkylsuccinyl lactoglobulin sulfonate 0.020 Laminaria saccharina 0.010 Hamamelis virginiana Citrullus vulgaris Preservative 0.006 0.001 q.s Oat peptide 0.200 Method 1. Into the water, alcohol denat. Is added and dispersed until uniform. Using a propeller stirrer, all materials including the Extruded colloidal oatmeal, are slowly added and stirred until uniform. The product is made to weight using purified water and stirred until uniform. Formulation 19 - Lipstick % w / w Ricinus communis 22.000 Octyldodecanol Pentaerythrityl tetracaprylate / caprate Mica Bis-diglyceryl caprylate / caprate / isostearate / Stearate / hydroxystearate adipate Paraffin 15.000 14.000 10.000 7.500 5.000 Cera microcristallina 6.000 Propylene glycol 2.000 Hydrogenated castor oil 2.600 Candelilla cera 3.000 Carnauba 3.000 Synthetic wax 3.000 Butyrospermum parkii 5.000 Titanium dioxide 0.500 Tocopheryl acetate 0.200 Polyquaternium-37 0.200 Pigments and dyes q.s Oat peptide 1.000 Method 1. The oat peptide is pre-dispersed in propylene glycol, with stirring. 2. The remaining materials are mixed in a vessel and heated to 850C until melted and uniform. The product is cooled and the oat peptide pre-mix is added below 70C. The product poured into a suitable container and allowed to cool to room temperature to set. Formulation 20- Facial Soothing Cream % w / w Aqua 88.800 Sodium Gluconate 0.200 Sodium Acrylates Copolymer, Lecithin 1.500 Benzoic Acid, Benzyl Alcohol, Carpylyl Glycol 1.000 Caprylic / Capric Triglyceride 3.000 Aqua, Sodim Hydroxide 5.000 Oat Peptide 0.500 Method 1. Add the water into the main vessel, with stirring add and dissolve Sodium Gluconate crystals. Add Oat Peptide under propeller stirring until smooth and uniform, with no lumps. Sprinkle Lecigel on to the surface and propeller stir until a uniform gel is obtained. Add the preservative with stirring. 2. Apply homogenisation and then add Surfac MCTG. Homogenise for 5 minutes until bright, shiny and uniform. Ensure the pH is 5.0-6.0. 5 Formulation 21 - Face Mask % w / w Aqua 67.950 Glycerin 2.000 Xantham Gum 0.500 10 Disodium EDTA 0.050 Phenoxyethanol, Ethylhexylglycerin 1.000 Bentonite 4.000 Glyceryl Stearate, PEG-100 Stearate 2.500 Stearic Acid 2.000 15 Glyceryl Stearate SE 4.000 Ethylene Glycol Monostearate 3.000 Butyrospermum Parkii (Shea) Butter 2.000 Caprylic / Capric Triglyceride 7.000 Theibroma Cacao (Cocoa) Seed Butter 1.000 20 Avena Sativa Kernel Flour 2.500 Oat Peptide 0.500 Method 1. Pre-mix Glycerin and Xantham gum and leave to one side 25 2. Add water and pre mix from stage 1 and stir until all Xantham Gum is hydrated. Add Disodium EDTA, Avena Sativa Kernel Flour, Oat Peptide and Phenoxyethanol, Ethylhexylglycerin, with Stirling and heat to 70’C, with stirring. 3. In a side vessel, add Bentonite Glyceryl Stearate, PEG-100 Stearate 30 Stearic Acid, Glyceryl Stearate SE, Ethylene Glycol Monostearate, Butyrospermum Parkii (Shea) Butter, Caprylic I Capric Triglyceride and Theibroma Cacao (Cocoa) Seed Butter, heat to 70-75’C with stirring. 4. Add stage 3 to stage 2 in the main vessel and homogenise until uniform. Stir the bulk cool and make up weight.

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