Trends in Food Science & Technology 17 (2006) 8290

Viewpoint

Wheat-gluten uses and industry needs

L. Dayab*, M.A. Augustinab, I.L. Bateybc and C.W. Wrigleybc
Food Science Australia, Werribee, VIC. 3030, Australia (Tel.: C61 3 9731 3233 fax: C61 3 9731 3250; e-mail: li.day@csiro.au) b Value-Added Wheat CRC, North Ryde, NSW 1670, Australia c Food Science Australia, North Ryde, NSW 1670, Australia
Gluten, the dough-forming protein of wheat our, is the key to the unique ability of wheat to suit the production of leavened products. The past ve decades have seen the rise of gluten as a commodity in its own right, through the largescale industrial separation of wheat starch from gluten, plus the controlled drying of the gluten so as to retain its functional properties. The resulting Vital Dry Gluten is most widely used in bakery products. However, gluten (vital, de-vital or modied) is nding increasing use as a food ingredient to provide a range of functional properties at a more modest price than competitors such as milk and soy proteins.
a

&

Introduction Gluten may be dened as the cohesive, visco-elastic proteinaceous material prepared as a by-product of the isolation of starch from wheat our. A further denition might include the genes involved in the synthesis of the gluten proteins in the developing grainthe Gli-1 and Gli-2 loci coding for the gliadin proteins, plus the Glu-1 and Glu-3 loci, coding for the glutenin polypeptides (Gianibelli, Larroque, MacRitchie, & Wrigley, 2001). A biological denition might include the origins of the glutenprotein complex as being derived from the storage proteins of the wheat grain (Shwery & Halford, 2002). Such denitions are correct but there is more to tell. The most signicant aspect of the gluten story for the food industry is the
* Corresponding author.

importance (and the potential) of gluten as a commodity, sold for a wide range of uses around the world. In its most familiar form, gluten is traded in the dried state as Vital Wheat Gluten. In this form, the functional properties of wheat gluten may be regenerated by rehydration. In addition, many products are derived from gluten by various forms of modication, thereby suiting them to a wide range of value-added uses. The proteins that form gluten are storage proteins, according to their function for the wheat grain (Shewry, 1999). The grain also contains the residue of many metabolic proteins (mainly water-soluble) that have been needed by the developing grain, together with the proteins providing those putative mechanisms that must carry life on into the next generation of the wheat plant when the germination process commences (Shewry, 1999). This is the basic context in which we should see the storage proteins, not as the dough-forming gluten proteins, but as the grains storage proteins laid down specically to provide an essential supply of amino acids for the developing plant. In these respects, the storage proteins of the mature wheat may not differ much from those of other grains (Shwery & Halford, 2002). However, the distinctive feature that makes wheat unique is the visco-elastic properties of its storage protein. When the grain is milled and mixed with water, what was merely storage protein forms a dough with unique rheological properties, capable of retaining gas bubbles, suiting this dough to the wide range of products we have come to expect from wheat our. It is these properties that make wheat alone suitable for the preparation of a great diversity of food products breads, noodles, pasta, cookies, cakes, pastries and many other foods. It is also these unique properties that account for wheat being cultivated by man in such enormous quantities throughout the world. The name given to this unique group of proteins is gluten, an enigmatic complex of proteins. Given the unique properties of wheat gluten, it is not surprising that it has been the subject of intense attention by the food industry. That interest has extended to the commercial separation of gluten from the starch and soluble proteins of our. In fact, it is the cohesive properties of gluten that makes its commercial preparation a relatively simple process. Vital Wheat Gluten is now a signicant ingredient in the food industry and

0924-2244/$ - see front matter Crown Copyright q 2005 Published by Elsevier Ltd. All rights reserved. doi:10.1016/j.tifs.2005.10.003

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an important item of world trade (Boland, Brester, & Taylor, 2005; Krishnakumar & Gordon, 1995), but until halfway through the 20th century, it did not exist as such. The term gluten is also used in commerce (erroneously) to indicate the protein residue after isolating starch from corn (maize) (Patil, 2003; 2004). However, this corn gluten is functionally very different from wheat gluten. Another connotation of the term gluten relates to the family of proteins that cause dietary problems for people with coeliac disease (Feighery, 1999; Murray, 1999). In this case, the term gluten includes the storage proteins from the grains of rye, triticale, barley and possibly oats (Kasarda, 2001). Thus, the term gluten-free foods refers to food products free from these cereal proteins, or those in which cereal protein content is less than a dened amount (usually 200 ppm). In this review, only the properties and uses of wheat gluten are discussed. History of the commercial production of wheat gluten Gluten was rst prepared from our almost 300 years ago by an Italian named Beccari, who conducted a simple waterwashing experiment with wheat our (Bailey, 1941). This discovery, which can be easily reproduced in the home kitchen, has become the basis of a major cereal industry, utilising millions of tonnes of wheat annually in North America, Europe and Australia. The present commercial process is basically an efcient repetition of Beccaris experiment. Bakers, knowing the value of the gluten component of dough, have added gluten to dough for decades. Although the enrichment of bakers our with gluten has been common practice in bread manufacture since the second half of the 20th century, the purication of starch from wheat our has been practised for a much longer time. For example, as far back as 1840 in Hull, England, Isaac Reckitt was washing starch from wheat our. In doing so, he was laying the technical foundations of the major company that bears his name (Wrigley, 2002). In his own words, the procedure involved making a mash of the wheat after soaking in water for many days, and when soft enough, putting the mash through sieves, the wheat starch passing through, leaving the bran in the sieves to be cast aside for pigs (Anon, 1912). The gluten was afterwards separated from the starch by washing. Unfortunately, Reckitt saw no value in the gluten, and it was discarded for animal feed. The Hull site has continued as a major operation centre for the greatly diversied multinational ReckittBenckiser. The gluten fraction continued to be discarded for some decades before its industrial potential was realised, and before procedures were developed to isolate the gluten as a functional mass, retaining its intrinsic properties for enhancing baking quality. The following

two independent accounts describe the development of gluten manufacture for commercial exploitation. The rst of these stories begins in Wellington, New Zealand in the 1930s, where a pastry cook, Harry Maltwood Williams, discovered a method of extracting gluten from our using fermentation, water-washing and the late addition of salt (Wrigley, 2000). Experiments with the gluten-enriching process produced bread of increased volume and improved texture. The process for producing Procera bread was patented worldwide. After initial exploitation in New Zealand, the patent-licensing approach was extended to the larger market of Australia. Reg Bartle, one of the two who went to Australia, travelled in his own plane to visit country bakeries, resulting in introductory telegrams such as Arriving Kempsey race course at 3 pm. Bartle, Procera. In 1932, the marketing package involved the use of a band of paper to go around each loaf produced by the Procera company, indicating the payment of a royalty charge of 0.1 penny per loaf by the baker. The resulting 1-pound loaf sold readily for two pence at a time when a 1-pound loaf cost 2.5 pence. This marketing method amounted to the modern practice of franchising. Indeed, when the Trade Mark Users Act was enacted in 1948, Procera Australia Pty Ltd became the rst major franchising company to operate in Australia. The process was also introduced to Britain, where it was known as the Procera method. In parallel with these developments, Nigel Love (N.B. Love Mills, Sydney) developed a similar product; trade marked as Promax bread. This was made from a highprotein our, and it gave results similar to the Procera bread process. As the use of the Procera method was limited to one baker in each town or region, the Promax method spread quickly with the remaining bakers. The protein-enriching Procera method involved the removal of starch, thereby producing the ongoing problem of disposing of the starchy efuent. Municipal councils complained of blocked drains and sewage difculties. These problems led to the development of an industrial-scale process to provide the protein-enriched ingredient for the Procera method in dried form (essentially as dehydrated gluten) in parallel with recovering the washed-out starch that could also be dried and used in foods. These developments, devised in 1938 by Basil Regan and Leonard Winch of Fielders Mills (Tamworth, NSW, Australia) included the problem of drying the wet gluten and retaining its vital nature. The result was the ring or ash drier in which wet gluten pieces were rolled in dry our and subjected to heat drying. From these beginnings for the bread industry has developed the signicant export commodity of dried gluten for Australia, and a worldwide industry for the production of dried gluten as a major trade commodity. The North American origins of commercial gluten production started with the industrial need for wheat starch,

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not gluten (Dubois, 1996). In the early 1900s, it had become unprotable for the Jenks family (Lake Huron, Michigan) to produce our for shipping to Detroit, due to competition from larger mills in the Midwest, so new outlets for our were sought. The process developed was designed to separate out starch, rather than specically to isolate gluten. A slack our-water dough was produced, permitting the separation of starch from gluten by gentle water washing. Initially, the gluten was discarded in favour of the starch, which sold well as laundry starch for stiffening clothing items. Initial attempts to use the gluten (in the 1920s) involved the use of heat-dried gluten (gum gluten) to bake low-carbohydrate bread for diabetics, and even later (in the 1940s) for producing monosodium glutamate by acid hydrolysis. Subsequently, the gum gluten was taken by Kelloggs to produce Special K (Thompson & Raymer, 1958). During these developments, Jenks and Rossman had used a harsh drying process that de-vitalised the functional properties of the gluten. It was thus useless as an ingredient to enhance baking quality. This situation changed, in the late 1950s, when the Huron Milling Company adopted the new type of drying process used in Australia (quoted from Dubois, 1996), based on the ring or ash drying process. This form of dry gluten retained its functional properties, when added to dough. As a result, loaf volume and crumb texture were improved. This vital dry gluten was soon exploited commercially as an additive for a variety of breads, but not as a blend with wheat our at the mill. Nevertheless, blending with our has more recently become common practice, especially in Europe where gluten fortication is essential for many lowprotein ours (Spooner, 1995). From these various origins, dry gluten has become an important commodity in international trade, both as an additive to fortify our for bread manufacture, and as an ingredient for many food and non-food uses.

The gluten industry at present The principle of gluten washing still remains similar to that of Beccari hundreds of years ago. Most commercial operations now use variations of either the Batter Process or the Martin Process (Knight, 1965). In the Martin Process, wheat dough is washed with water while it passes through a tumbling cylindrical agitator so that the starch comes out of the dough, while the protein content increases in the remaining dough. The dough is moved along the cylinder by the tumbling action, while the starch passes through small holes in the wall leaving the protein mass inside to receive further washing until it falls out at the end. On the other hand, the Batter Process involves preparing a thick suspension (batter) of our. During several hours of stirring, the starch separates from the gluten, so that when the mixture is passed over a ne sieve, the starch granules

separate and the curds of gluten are retained on the screen. Further washing of this gluten removes further starch in a similar manner to the Martin Process. Following either process, the gluten is ash dried. Various modications have been made to these basic methods, for example, the Alfa-Laval Raisio process. Modern applications also use centrifugal techniques (either conventional industrial centrifuges or hydro-cyclones) to separate the starch from the protein. In particular, hydrocyclones serve at least in cleaning the starch, but also, in some cases, for the actual separation of the starch and gluten. Some of the newer methods process whole ground grain as the raw material, avoiding the production of our in a dry-milling step, but cleaning bran from the protein and starch fractions creates problems with these methods. Improved milling processes have reduced the amount of endosperm remaining in the bran and offal fractions in conventional milling, so there is little advantage to be gained in wet-milling for starch and gluten recovery. Nevertheless, modications of the traditional processes have remained the preferred choice for most of the gluten produced worldwide. The drying stage is critical for retention of functional properties as they are very susceptible to heat when wet, and even relatively low temperatures may destroy glutens visco-elastic properties. The principle of the ring drier involves mixing wet gluten (70% moisture) with dry gluten, thus reducing moisture to about 20%. This material is comminuted and subjected to ash drying. A portion of the dried gluten is drawn off from the drying ring, while new moist gluten is introduced. The rate of drying and the temperature of the moist gluten must be carefully controlled because the functional properties of gluten are easily destroyed by moist heat. Alternative approaches to drying include dispersion in aqueous ammonia or acetic acid, followed by spray-drying, but this approach is limited by its cost and by environmental concerns. A dramatic approach is to produce de-vital gluten, a product that no longer retains visco-elastic properties. In this case, severe temperatures may be intentionally applied, e.g. by drum drying. De-vital gluten retains the insolubility and water-binding capacity of vital gluten, so it is used in applications where the cohesiveness of vital gluten is a disadvantage. A critical consideration in gluten washing is the amount of water needed per tonne of our processed. All processes produce a waste stream, carrying soluble protein, damaged starch, sugars and bre. Disposal measures include fermentation (generating ethanol or methane), drying for animal feed, and discharge into the sewerage system, but this last option has become less common due to environmental concerns. The composition and properties of commercial gluten Although sold as a protein, gluten contains more than just protein. As a commodity, dry gluten usually contains

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approximately 75% protein, up to 8% moisture, and varying amounts of starch, lipid and bre. The starch and bre become entrapped in the cohesive matrix of the protein and become more difcult to remove as the protein content increases. The amount of starch varies, and more extensive washing can reduce the starch and bre content and increase the protein content. The extra water needed for this creates its own problems by producing a larger amount of efuent from the process, and increasing the total biological oxygen demand (BOD) of that efuent. Consequently, gluten of higher protein content is only produced as a special order and at a premium price. Much of the lipid content of the our becomes associated with the protein during the washing process. The gluten proteins are largely hydrophobic in nature and the lipids bind to the hydrophobic areas of the protein as they are repelled by the water used in the washing. Therefore, the lipids are strongly bound to gluten proteins and are removed with much more difculty than they are removed from the original our. The lipid content of gluten is primarily determined by the lipid content of the our from which it came, and is unaffected by additional washing. The protein that makes up gluten is a complex mixture of proteins, containing many, probably several hundred, polypeptides, about half of the protein being monomeric (gliadins) and the remainder being disuldecross linked polypeptides that form the polymeric glutenin fraction, whose sizes range up into the tens of millions of Daltons (Gianibelli, et al., 2001; Wrigley, 1996). By the nature of its preparation, gluten is a protein that is insoluble in water. While there may be small amounts of water-soluble proteins trapped in the gluten matrix, these are essentially not extractable into water under normal conditions. Despite its insolubility and its hydrophobic nature, gluten absorbs approximately twice its dry weight of water to form a hydrated viscoelastic mass. This material is effectively the same as the wet gluten rst isolated from our. In the case of commercially prepared gluten, drying conditions may cause some deterioration of the functional properties, but gluten prepared in the laboratory shows little change in its properties after freeze-drying and rehydration. Gliadin can be solubilised in 70% aqueous ethanol, one of the steps of the Osborne fractionation of wheat proteins,

and the residue after this extraction is considered to be glutenin. Gliadin and most of the glutenin may be solubilised to a certain degree by the use of acidic conditions. Gluten may be separated into a series of fractions by successive extractions with progressively decreasing pH. Reprecipitation by pH adjustment, or by drying the acidic solutions directly, gives products, which maintain their functional properties. This can be shown by reconstituting our, which is carried out by recombining the starch, the isolated protein fractions and the water-soluble components prepared during the extraction of gluten. Doughs prepared by careful reconstitution show little change in dough strength from that of the original ours (MacRitchie, 1985). Its rheological properties are the basis of the functional uses of vital gluten. It is these properties that permit breads, cakes, biscuits and noodles to be made from wheat-our doughs. Thus, gluten can be considered to be like a dough in which the diluting effect of starch is no longer present. In the wet state, the protein molecules form a cohesive matrix which, in dough, also holds the starch granules within it. This matrix is also elastic, allowing it to stretch and expand. In aerated doughs, this elasticity permits the expansion of gas bubbles, which produce the texture of bread and cakes.

Modication of gluten Gluten is a modestly priced food protein, much cheaper than casein and soy isolates, whilst being greatly preferred to protein sources that are only suited to animal food. Its price advantage (see Table 1 for price comparison in Australia) offers signicant scope for value addition by modication. On occasions, threatened market surpluses of gluten have stimulated manufacturers to explore ways of converting gluten into products with different properties. A common example is the creation of a gluten product that is water-soluble, or at least dispersible in water. Deamidation, the most common method for this purpose, may be achieved with either acid or alkali treatment (Batey & Grass, 1981; Wu, Nakai, & Powrie, 1976). Removal of the amide group from some of the many glutamine residues (to form the corresponding carboxylic acid, glutamic acid) changes

Table 1. Current prices of food protein ingredients in Australia (September 2005, in US dollars) Ingredient Wheat gluten Soy protein isolate Whey protein isolate Caseinate Skimmed milk powder
a

Protein content (% approx.) 75 90 90 90 35

Price per tonne ($)a 4000 6000 21,500 12,000 4000

Price per tonne protein ($)a 5333 6667 23,889 13,333 11,429

Calculated based on the exchange rate: 1 AUDZ0.75 $.

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the potential charge, thus increasing solubility. In addition, acidic deamidation may cause some peptide hydrolysis, leading to the formation of lower-molecularweight polypeptides, which in turn enhances the solubility. Alkali treatment does not usually cause peptide hydrolysis, but it may break the disulde bonds of cystine and create cross-links due to the formation of lysinoalanine (Batey & Gras, 1981). Either acid or alkali deamidation requires neutralization, causing the production of signicant amounts of salts which usually need to be removed, often by iso-electric precipitation (Batey & Gras, 1983). Deamidated gluten is easily dispersible, making it suitable for use in foods for emulsication or foam stabilisation. No benets have been reported for the use of deamidated gluten in bread doughs. Treatment with sulfuric acid, phosphoric acid or chlorosulfonic acid produces products that bind greatly increased amounts of water, in some cases such modied glutens bind up to 200 times their own weight of water (Maningat, Bassi, & Hesser, 1994). Other chemical modications include treatment of gluten with succinic anhydride, thereby increasing its solubility at pH 7, close to the point of minimum solubility of native gluten (Barber & Warthesen, 1982). Solubility may also be produced by enzymic hydrolysis of the peptide bonds, thereby reducing the sizes of the polypeptide chains. Suitable commercial enzymes include papain, bromelain, subtilisin, trypsin and pronase. These enzymically solubilised preparations of gluten have many of the properties of chemically deamidated gluten, such as foam stability and emulsion formation. Unlike chemically deamidated gluten, enzyme-solubilised gluten has benecial effects on dough properties. For example, the addition at levels of 12% enzyme-solubilised gluten may reduce dough-mixing times by amounts similar to those achieved by chemicals such as cysteine and ascorbic acid, which are often added commercially to give improved loaf volumes (Asp, Batey, Erager, Marston, & Simmonds, 1986). However, enzyme solubilisation may lead to products with a bitter taste,

presumably due to the release of small peptides from excessive enzyme action. A third approach to modication is the use of physical means, including heat treatment, texturisation by extrusion, high-pressure processing and UV irradiation. Extrusion technology is used widely to produce a brous structure in gluten, thus to simulate meat bres. Alignment of wheat-protein molecules during the extrusion process results in the formation of thin laments or microbrils, which assemble further to form a macroscopic brous structure. Hydration of the brous strands gives the laminated, eshy appearance of texturised wheat gluten (Maningat, DeMeritt, Chinnaswamy, & Bassi, 1999). High pressure has been found to change the gluten to either more liquid-like at relatively low pressure (200 MPa), or more solid-like as the pressure increased to 800 MPa (Apichartsrangkoon, Bell, Ledward, & Schoeld, 1999). There was evidence of the weakening of non-covalent bonds at mild treatment conditions, but further chemical cross-links occurred with increasing severity of treatment. When lms cast from ethanol solutions of gluten are irradiated, the tensile strength of the lm is enhanced (Rhim, Gennadios, Fu, Weller, & Hanna, 1999), presumably by the formation of cross-links between the protein chains. Dietary intolerance to gluten Many foods may provoke adverse reactions when ingested, the reactions varying in nature and severity, depending on the individuals susceptibility to specic foods. Coeliac disease, a well-known permanent food intolerance to wheat gluten (and related cereal proteins), is characterised by inammation of the small intestine which adversely affects the absorption of water and nutrients causing, in some cases, malnutrition (Sollid, 2000). The only treatment is a strict diet avoiding all products containing gluten. Allergenicity of gluten is not an issue when gluten is used or added to wheat grain/our-based food products since wheat proteins are likely to be present in the products already. However, there is a concern about the effects of

Table 2. Usage of gluten in different regions of the world (as percentage of total usage for the region) Uses Baking Flour fortication Meats Breakfast cereals Noodles Sausages Pet food Other
a

North America 83 1 1 1 12 2

Europe 17 66 13 4

Australia 54 9 9 12 13 3

Japan 30 25a 10 12 23

Total world 63 14 5 2 8 8

Includes gluten used for synthetic sh products.

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gluten on people with coeliac disease and others with wheatprotein allergies, particularly because there is an increasing trend towards the incorporation of gluten into foods that do not traditionally contain wheat proteins. Many researchers have been trying to understand the mechanism of coeliac disease and to reduce allergenicity of the proteins by modifying the allergen structure in such a way that the allergenic epitopes are no longer recognised by the immune system. Until now, the technological approach to decrease allergenicity has largely been empirical. The main reason for this is a lack of detailed knowledge about the integral allergen and epitope structure and their genetic background, thus hampering the design of more rational, generic strategies for processing. Scientic knowledge about coeliac disease, including knowledge about the proteins that cause the problem and the grains that contain these proteins, is still incomplete. Any consideration of new uses of gluten or of modied gluten, particularly in non-cereal based food products, should include the impact of the application on people with intolerances to gluten. Current food uses of wheat gluten The most common usage of gluten in western countries has traditionally been, and continues to be, in baked goods of various types. However, with an increasing awareness of wheat glutens unique structural and functional properties has come an expanding diversity of applications. The uses of gluten worldwide vary from country to country as shown in Table 2. In wheat-based products, gluten is used to fortify ours of lower-than-desirable protein content. Increasing the protein content of our by adding vital gluten improves the quality of the our to be equivalent to one with a higher protein content. This fortication may be necessary because the our has a naturally low protein and higher protein content is needed to make quality products, or because the addition of gluten provides a particular property sought in the food by improving the quality of the protein. This practice has become increasingly common in parts of Europe (Table 2), where gluten fortication of low-protein bread ours offers an attractive alternative to blending with expensive, imported high-protein wheats to satisfy functional performance requirements. Bakers also use gluten to fortify their basic ours at different levels to obtain desired performance for the production of specialty breads and different types of bakery goods. This minimises our inventories and avoids storage of high-protein ours. Vital Wheat Glutens unique visco-elastic properties improve dough strength, mixing tolerance, and handling properties. Its lm-foaming ability provides gas retention and controlled expansion for improved volume, uniformity, and texture; its thermosetting properties contribute necessary structural rigidity and bite characteristics; and its water absorption capacity improves baked product yield, softness, and shelf-life. The level of gluten used can be quite specic,

depending on the particular applications and the required texture and shelf-life of bakery products. For example, addition of about 1% gluten to our reduces pretzel breakage in the nished product, but the addition of too much gluten may result in pretzels that are too hard to eat. Gluten is used at approximately 2% in pre-sliced hamburger and hot-dog buns to improve the strength of the hinge and provide desirable crust characteristics when buns are stored in a steamer. It can also be used to strengthen pizza crust, making it possible to produce both thin and thick crusts from the same our. The incorporation of gluten provides crust body and chewiness and reduces moisture transfer from the sauce to the crust. A desired property of gluten is its ability to bind fat and water while at the same time increasing the protein content; this makes gluten attractive for various types of application in meat, sh, and poultry products. Gluten improves the utilisation of beef, pork and lamb meats by a restructuring process, which converts less desirable fresh meat cuts into more palatable steak-type products. Gluten has also proven as a satisfactory binder for turkey-meat pieces because of its ability to produce intact loaves with good slicing qualities. In processed-meat products, gluten is an excellent binder in poultry rolls, canned integral hams, and other non-specic loaf-type products, where it also improves slicing characteristics and minimises cooking losses during processing. A major use of gluten in non-bakery foods is as a meat replacement in vegetarian foods, and in the production of articial forms of expensive foods such as seafood and crab analogues, particularly in Japan (Table 2). Due to the growing concern for health and food safety, an increasing number of consumers are looking for meatless alternatives. Pure wet wheat gluten can be seasoned, shaped, and cooked into meatball and steaks. Texturised wheat gluten developed using extrusion technology can be used to mimic the mouthfeel, chew, and taste of meat. Meat products created by this process are suited to ready-to-eat entrees, as sandwich llings, or for pizza and salad toppings. Gluten also acts as a binder and provides a meat-like structure in veggie burgers. Glutens visco-elastic properties can be used in preparing synthetic cheese with the characteristic texture and eating quality of natural cheese. Gluten used alone or in combination with soy protein, has been used to replace approximately 30% of the more expensive sodium caseinate in imitation-cheese products. Wheat gluten-fortied breakfast cereals have been widely accepted by consumers because they are very avourful and nutritious, especially when consumed with milk. Kelloggs Special K cereal is perhaps the most familiar example in this product category. In extruded snacks, wheat gluten provides nutritional value, crispness, and desired texture. Gluten has also been mixed with fruit puree to be used as a fruit lling for nutritional bars. Addition of gluten to corn tortillas improves their rollability and pliability.

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Gluten is also used in the preparation of soy-sauce extenders, and the manufacture of monosodium glutamate. The high glutamine content of gluten makes it an ideal starting material for this latter product. Soy sauce made using gluten has light colour, slow browning rate, excellent avour and good body over traditional soy sauce. Due to the scare of the bovine spongiform encephalopathy (BSE) disease, replacement of gelatin by other food proteins has found applications for gluten recently in food products, such as chew candy or fruit chew (Van & Schueren, 2002), or as a clarifying agent of musts and white wines (Marchal, Marchal, Lallement, & Jeandet, 2002). Non-food uses of gluten The pet food industry is the second largest user of wheat gluten. The usage may be in preparing simulated meat for canned pet food or in both canned and intermediate moisture-type products, where its water absorption and fat-binding properties can improve yields and quality. Gluten not only binds chunks of raw and cooked meat together, but also absorbs the natural juices of meat that would otherwise be lost during the cooking process. Because of its relative low cost, gluten can also signicantly contribute to the nutritional requirements of pet food. Another increasing use of gluten is in aquaculture feed, as the farming of aquatic species is rapidly expanding. Its adhesive properties provide the binding needed for the pellet or granule forms of feed commonly used, its water insolubility reduces pellet breakdown, its visco-elastic properties can provide a chewy texture preferable to an extremely hard pellet, it lends itself to extrusion and air incorporation, depending on whether surface- or bottomfeeding is desired, and again, it provides nutritional value at low cost. Gluten and modied glutens have been also used in calf-milk replacements. Because of the variability in price of skimmed milk powder, some vegetable proteins are being considered as alternative sources of protein to provide the amino-acid requirement for young calves. Gluten has been reported to be used as feed and fat-lled powders for feeding piglets (e.g. Amytex and Solpro from Tate & Lyle). The thermoplasticity and good lm-forming properties of wheat gluten may be used to produce natural adhesives. Through the controlled hydrolysis, breaking of sulde links and the use of plasticisers, the properties of the adhesives can be modulated (Research at Institute for Agrobiotechnology, Tulln, Austria). Glutens adhesive properties make it useful in pressure-sensitive medical bandages and adhesive tapes. Its reactivity make it useful for binding heavy metals in industrial processes, removing ink from waste paper, or solidifying waste oils. Peptides from gluten are useful in cosmetics, lotions, and hair preparations such as skin-care products (for rming and moisturising skin from Rachel Perry, Croda, MGP), biodegradable resins (Polytriticumw) and

other personal care products (Foam Pro L for hair, facial cleansers from MGP Ingredients). Glutens hydrophobic and (in)solubility properties permit slow-release encapsulation of pest- or weed-control agents (Quimby et al., 1994). The use of gluten in lms has also been tried (Guilbert et al., 2002). Production of gluten lms with satisfactory properties could provide a new biodegradable lm for widespread use. Gluten has the ability to provide edible lms that protect food or food components from interactions with the environment as they can serve as barriers to mass transfer (e.g. oxygen, water vapour, moisture, aroma, lipids). Gluten-based lms may be cast from solutions of gluten in ammonia or alcohol. The properties of wheat gluten lm can be altered by the pH, heat treatment and solvent concentration of the lmforming solution. This will require the matching of the functionality of the gluten lm to its intended application. This requires an understanding of the relative importance of the various functionalities of lms, such as moisture and oxygen barrier properties, and its durability and cohesiveness for the target application. Recently in a completed EU FAIR project, wheat gluten was used as biopolymer for the production of renewable and biodegradable material (FAIR-CT96-1979). Biomaterials of varying mechanical properties were prepared from industrial gluten (native or deamidated) and from gliadinand glutenin-enriched fractions using either an aqueous casting procedure or thermo-moulding. The differences of mechanical properties induced by the process of lm preparation were larger than those arising from variations of protein composition and properties (except for lms cast from water dispersion) due to the wheat genotype, including durum wheat. It was therefore concluded that there is no need for specic breeding as far as uses of wheat proteins in non-food lm material are concerned. Hence, wheat unsuitable for bread- or pasta-making or low-quality gluten could be used without trouble for preparing plastic lms. New functional ingredients for the food industry The food industry is always seeking new cost-effective functional ingredients that impart desirable properties to a range of manufactured food products. Food ingredients serve a number of functions in food. These can broadly be classied as: (a) nutritional functionalitywhere the ingredient adds to the nutritive value; (b) physical functionalitywhere the ingredient contributes to textural and sensory properties; and (c) physiological functionalitywhere the ingredient has a bio-modulating function (i.e. it is bioactive). In terms of its nutritional value, gluten (or wheatprotein) is considered to be poorer than proteins from animal sources, primarily because it is slightly decient in the essential amino acids, lysine and threonine. However, gluten does contain high levels of the amino

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acid glutamine which is essential for strengthening muscle/body building. Therefore, the utilisation of gluten proteins is mainly due to its physical functionality and its relatively low cost. Functional properties of proteins are those physicochemical properties of proteins which affect their behaviour in food systems during preparation, processing, storage, and consumption, and contribute to the quality and sensory attributes of food systems. The most important functional properties of proteins in food applications are hydrophilic (i.e. protein solubility, swelling and water-retention capacity, foaming properties and gelling capacity), hydrophilichydrophobic (i.e. emulsifying, foaming) and hydrophobic (i.e. fat-binding properties). Functional properties of proteins as food components are affected by molecular weight and by the shape of protein molecules, their primary structure and diversity; the conformational structure being affected by covalent and/or non-covalent bonds, and charge distribution on the protein molecules. Functional properties of proteins also depend on the protein interactions with other proteins, lipids, carbohydrates, water, ions and avours in the food systems. The preparation and processing of proteins for use as ingredients in different food formulations inuences their functionality in foods. In exploring and developing new sources of foodingredient proteins, the functional property is a major criterion in assessing their potential utilisation. In addition to the provision of essential amino acids, the success of new protein applications relies on them possessing desirable functional properties and acceptable sensory characteristics. Therefore, the development of new processes for manufacturing protein ingredients should be carried out in order to provide protein products with improved functional and sensory properties. Functional properties of proteins, in particular food systems, are also affected by processing aids and conditions. Factors such as pH of medium, temperature of treatment, ionic strength, moisture content, oxidation/ reduction potential, shear stress and others, are critical for the proper use of food protein ingredients. On the other hand, they can also be utilised to modify and control functional properties of proteins.

Gluten, a competitor with other food proteins While the insoluble nature of gluten is a desirable attribute in traditional applications of this ingredient in bread and baked products where it is essential for their structural properties, its insolubility in water limits its usefulness in many other applications. This is because solubility is often a pre-requisite for good hydration and water holding, viscosity building, gelling, foaming capacity and foam stabilisation and emulsication properties that are often needed in protein ingredients. In addition, when an ingredient is used in a liquid system

that undergoes heat processing, it is necessary for the ingredient to have adequate stability to heat to allow it to be heat-processed without coagulation or excessive thickening. The major success stories with protein ingredients are those related to the dairy-protein and soy-protein industries, where fractionation and processing modications have been the main methods used for diversifying the applications of these protein products. Milk-protein-containing products (e.g. skim milk powder with w35% protein, whole milk powder with w25% protein) have traditionally been used in a variety of dairy and other food products. Milk has also been fractioned into a range of protein products to diversify the applications of milk-based ingredients. Protein-based ingredients that are on the market for a long time include the caseinates (w90% protein) and whey-protein concentrates with varying protein contents (3580% protein). Newer protein products include whey-protein isolates (with w90% protein), milk-protein concentrates (up to w85% protein), major whey-protein fractions (e.g. betalactoglobulin) as well as minor proteins with bioactive properties (e.g. lactoferrin and lactoperoxidase). The production of these newer products has been made possible through improved fractionation technology. In addition, a range of hydrolysed whey protein and casein products with different degrees of hydrolysis are on the market. They have been produced for applications in sport-nutrition products to obtain differentiated properties. Soy proteins also offer an excellent example of how value has been added to a plant protein for use in food and non-food products. Like the importance of starch to the wheat gluten industry, the initial growth of the soybean industry was primarily driven by oil production rather than its protein products. As scientists, food technologists and consumers became increasingly aware of the high nutritional value of soy proteins as a plantprotein source and the potential for using new advances in processing technology for oil production with little or no adverse effect on soy protein, the growth of their use as food ingredients has increased steadily in the last decade or so. Nowadays, soybean-protein production, i.e. use of soybean meal, adds more value to soybeans than the oil. Commercial soy-protein products are available including defatted soy akes, soy meal, soy our and grits, soy concentrates, soy isolates, texturised soy proteins, etc. Soy ours are widely used in bakery products and cereals (to supplement the nutritional value of wheat proteins due to the high lysine content of soy protein). Soy concentrates and isolates are used in a variety of meat and dairy products, because of their high solubility and high protein content, soy isolates are also used in infant formulas, beverages, and as an amino-acid source to substitute for casein, egg white and meat. Unlike whey and soy proteins, gluten or wheat proteins are not high in biological value and have not

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L. Day et al. / Trends in Food Science & Technology 17 (2006) 8290 Guilbert, S., Gontard, N., Morel, M. H., Chalier, P., Micard, V., & Redl, A. (2002). Formulation and properties of wheat gluten lms and coatings. In A. Gennadios (Ed.), Protein-based lms and coatings (pp. 69122). Boca Raton, FL: CRC press. Kasarda, D. D. (2001). Grains in relation to celiac disease. Cereal Foods World, 46(5), 209210. Knight, J. W. (1965). The chemistry of wheat starch and gluten and their conversion products. London: Leonard Hill. Krishnakumar, V., & Gordon, I. (1995). The world wheat gluten market. International Food Ingredients, October(4), 4142 (see also p. 45). MacRitchie, F. (1985). Studies of the methodology for fractionation and reconstitution of wheat ours. Journal of Cereal Science, 3(3), 221230. Maningat, C. C., Bassi, S. D., & Hesser, J. M. (1994). Wheat gluten in food and non-food systems. American Institute of Baking Technical Bulletin, 16(6), 18. Maningat, C. C., DeMeritt, G. K., Chinnaswamy, R., & Bassi, S. D. (1999). Properties and applications of texturized wheat gluten. Cereal Foods World, 44(9), 650655. Marchal, R., Marchal, D. L., Lallement, A., & Jeandet, P. (2002). Wheat gluten used as a clarifying agent of red wines. Journal of Agricultural and Food Chemistry, 50(1), 177184. Murray, J. A. (1999). The widening spectrum of celiac disease. American Journal of Clinical Nutrition, 69(3), 354365. Patil, S. K. (2003). Corn processing industry coproducts: Issues and challenges. Part I. Cereal Foods World, 48(6), 363364. Patil, S. K. (2004). Corn processing industry coproducts: Issues and challenges part II. Cereal Foods World, 49(2), 102104. Quimby, P. R., Jr., Birdsall, J. L., Caesar, A. J., Connick, W. J., Jr., Boyette, C. D., Caesar, T. C., & Sands, D. C. (1994). Oil and absorbent coated granules containing encapsulated living organisms for controlling agricultural pests. US Patent 5,358, 863. Rhim, J. W., Gennadios, A., Fu, D. J., Weller, C. L., & Hanna, M. A. (1999). Properties of ultraviolet irradiated protein lms. Lebensmittel Wissenschaft und Technologie, 32(3), 129133. Shewry, P. R. (1999). The synthesis, processing, and deposition of gluten proteins in the developing grain. Cereal Foods World, 44(8), 587589. Shewry, P. R., & Halford, N. G. (2002). Cereal seed storage proteins: Structures, properties and role in grain utilization. Journal of Experimental Botany, 53(370), 947958. Sollid, L. M. (2000). Molecular basis of celiac disease. Annual Review of Immunology, 18, 5381. Spooner, T. F. (1995). The unsung hero of any successful baking procedure. Milling and Baking News, 74(41), 3438. Thompson, J. J., & Raymer, M. M. (1958). Production of ready-to-eat composite aked cereal products. US Patent 2,836,495. Van, D. E. R., & Schueren, F. M. L. (2002). Chew candy or fruit chew comprises wheat gluten and maltodextrin as replacement for gelatin. European Patent 979611. Wrigley, C. W. (1996). Giant proteins with our power. Nature, 381(6585), 738739. Wrigley, C. W. (2000). Contributions by Australians to grain quality research. In L. OBrien, & A. B. Blakeney (Eds.), An introduction to the Australian grains industry (pp. 268329). Melbourne: Royal Australian Chemical Institute. Wrigley, C. W. (2002). Gluten as the key to wheat qualitya brief history. Cereal Foods World, 47(7), 336338. Wu, C. H., Nakai, S., & Powrie, W. D. (1976). Preparation and properties of acid-solubilized gluten. Journal of Agricultural and Food Chemistry, 24(3), 504510.

been widely researched for nutritional advantages. Gluten, on the other hand, perhaps has been disadvantaged slightly due to its link with coeliac disease. Extensive research and education of consumers is needed to fully understand the value of gluten protein in terms of its possible or particular nutritional-health benets or defects. However, gluten does have economic benets over and above the more expensive milk- or soy-protein products (Table 1), and its functional properties, which other products cannot duplicate, give it a unique place among the various protein products. Gluten also possesses functional attributes that enhance product quality in foods beyond baked goods, thus soy protein should serve as a model for gluten utilisation in some ways, such as changing or enhancing particular physical functional properties to suit or enhance performance in a particular food system. Gluten, modied gluten and its fractions need to compete on price and tness-forpurpose with other protein ingredients, if wheat proteins are to be successful in a wider food market. This can be achieved by understanding customer needs and further exploring opportunities which may lead to enhanced nutritional and physical functionality as well as the health benets of wheat proteins.

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