2005 Annual Report 1.What major problem or issue is being resolved and how are you resolving it (summarize project aims and objectives)? How serious is the problem? What does it matter? This project addresses utilization of the major byproducts--hides and wool--of cattle and sheep, animals raised domestically for their meat. The research contributes directly to National Program #306, "Quality, and Utilization of Agricultural Products," and particularly to its component on New Processes, New Uses, and Value-added Foods and Biobased Products. It addresses the following goals: * New knowledge derived from improved understanding of the structure, properties, and function of animal components, particularly proteins will generate development of a variety of new industrial products. * New technologies to convert commodities and process byproducts into important value-added products such as improved textiles will fill demonstrated needs. (a) Functional modification, leather and leather byproducts: Animal hides are high value coproducts of the meat industry, and the U.S. beef industry is the major, worldwide, source of cattle hides, valued at over $1 billion annually, for leather production. Tanning, the process of converting hides into high value, durable leather is rapidly being transferred to countries with lower environmental standards and labor costs. The result has been a major loss of jobs in the domestic leather industry, which is partially offset by the opening of tanneries associated with meat packing facilities where some chrome tanning of hides into unfinished leather ("wet blue") is now occurring. The processes used to convert two tons of "wet blue" into finished automotive upholstery leather leave the processor with a ton of solid waste, mainly a complex of collagen with chromium. We have developed a cost effective process for converting this waste, currently deposited in landfills, into high-grade technical gelatin, and collagen hydrolysate. Lack of domestic markets for this technical gelatin has hindered the adoption of this process by the U.S. leather industry. Development of high quality chrome-free leathers in response to the preferences of consumers, particularly in European markets, is hindered by a lack of understanding of tanning mechanisms. (b) Functional modification, wool: The U.S. sheep industry, a smaller but important component of the meat industry, produces 40 million pounds of raw wool per year. Domestic wool is threatened by the influx of imported wool treated for shrinkage resistance by chlorination, a process that produces large amounts of absorbable organo-halogens (AOX). Although some U.S. wool is exported for processing, the military and many law enforcement agencies are required to use domestically raised and processed wool for their uniforms and other products. Representatives of the armed forces have expressed interest in replacing synthetic materials in undergarments with comfortable wool. They are currently evaluating wool modified by an enzymatic process developed at ERRC in the predecessor project. Meeting additional needs of the military for altered wool properties—non-flame-ignitability, navy whiteness, and oil and water repellency—requires further research on the functional modification of this woolen fabric. Domestic wool has properties that limit its acceptance and competitiveness when compared to imported wool. Environmentally benign methods for adding value to U.S. wool will encourage domestic processing while reducing the reliance on imports. 2.List the milestones (indicators of progress) from your Project Plan. FY2005: 15 months (6/30/04 - 9/30/05) Objective 1 Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, (b) in expanding the range of high value biomaterial applications for solubilized proteins from leather byproducts. Objective 1a: High quality chrome-free leather. Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, and pursue the development of a general mechanism for tanning. 1a. Computational: Initiate the theoretical evaluation of the effects of collagen modifications, via tanning chemicals or natural aging, on the conformational stability of collagen microfibrils and the ultimate thermal stability of the collagen matrix. Experimental: Initiate evaluation of the effects of chemical or physical modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Objective 1b. Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (b) in expanding the range of high value biomaterial applications for solubilized proteins from leather byproducts, especially where these applications are in the manufacturing of leather. 1b. Solubilized proteins from leather byproducts: Identify chemoenzymatic modification strategies for processing proteinaceous byproducts of leather manufacturing to form biopolymers or conjugates with other surplus agricultural proteins. Initiate the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. Objective 2: Functional modification, wool: Modify wool to impart functionality for improved performance and expanded uses of domestic wool in nontraditional markets. 2. Initiate mill trials to establish optimized conditions for making “biopolished” (surface-oxidized and enzymatically polished) wool, developed and patented under the predecessor project, for minimizing shrinkage of woven or knit wool and its blends with other fibers and for improving the “handle” or feel of those textiles. FY2006: 27 months (9/30/05 - 9/30/06) 1a. Computational: Continue the evaluation of the effects of modifications to collagen on the conformation and conformational stability of collagen microfibrils. Experimental: Continue the evaluation of the effects of modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Initiate the experimental evaluation of computationally favorable modifications. 1b. Apply chemoenzymatic modification strategies identified in the previous year, for processing proteinaceous byproducts of leather manufacturing to produce biopolymers or conjugates in sufficient quantity for evaluation of chemical and physical properties. Continue the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. 2. Modify the patented wool process as needed, based on the results of mill trials. Initiate the development of environmentally acceptable methods for functionalizing wool for improved performance characteristics. FY2007 39 months (9/30/06- 9/30/07): 1a. Computational: Continue the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Initiate the theoretical evaluation of the interactions of potential enzymatic or other chromium-free tanning reagents with microfibrillar collagen. Experimental: Continue the evaluation of the effects of computationally favorable modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. 1b. Continue the evaluation of chemical, physical and functional properties of those products that show promise for applications in leather manufacturing. Initiate pilot scale application of identified products to pieces of hide or partially processed leather. Initiate the quality evaluation of leather manufactured with the identified products. 2. Select the most promising functionalized substrates as starting products for the engineering of new as well as improved conventional textile products. Initiate the optimization of processes for improving selected functionality. FY2008: 51 months (9/30/07 - 9/30/08) 1a. Computational: Complete the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Continue the estimation of the potential for enzymatic or other chromium-free tannages. Experimental: See previous periods. Transfer methods developed on isolated collagen to hide powder or intact hide. 1b. Continue the evaluation of leather produced at the pilot scale using the identified products. Identify an industrial partner for full scale testing of the identified products in leather manufacturing. Initiate full-scale tests of the use of feasible products in leather manufacturing. 2. Initiate pilot scale processing and evaluation of functionalized textile products using substrates identified in previous year. Initiate cost analysis of technically feasible processes. FY2009: 60 months (9/30/08 - 6/30/09) 1a. Computational: Complete the theoretical evaluation of the potential for enzymatic or other chromium-free tannages. Contribute concepts developed in previous periods to the development of a fundamental understanding of tanning. Experimental: Continue transfer of methods from collagen to intact hide. Formulate a set of options based on technical and economic factors for selecting or designing a high quality chrome-free tannage. 1b. Continue full-scale tests of promising processes. Perform cost analysis for promising processes. Initiate transfer of technology to industry. 2. Complete cost analysis for technically feasible processes. Document performance aspects of products and modify functionality and/or textile substrate to optimize identified end-uses. Transfer technology to industry as appropriate. 4a.What was the single most significant accomplishment this past year? Leather byproduct utilization: CWU researchers demonstrated that biopolymers can be produced by enzymatically crosslinking gelatin, recovered from cattle hides as a byproduct of tanning, with other surplus agricultural proteins. Sodium caseinate and ovalbumin, both proteins historically used in leather processing, were individually combined with gelatin and then treated with enzyme to form conjugates that had unique physical properties. Sodium caseinate is highly soluble and reactive under conditions favorable for enzymatic crosslinking with gelatin to form high molecular weight complexes. High viscosity biopolymers are formed by enzymatic crosslinking of ovalbumin, which is less soluble than sodium caseinate and forms colloidal suspensions, with gelatin. The degree of crosslinking was enhanced by addition of even small amounts of the secondary protein. Economically, the current costs of sodium caseinate ($1.95/lb) and ovalbumin ($1.80/lb), while not insignificant, are less than that of lowest grade gelatin ($2.60-2.75/lb). These protein conjugates are anticipated to replace petroleum derived resins in leather fillers and finishing agents. (NP306, Component II; Milestone: Objective 1a) 4b.List other significant accomplishments, if any. None. 4c.List any significant activities that support special target populations. None. 4d.Progress report. 1935-41440-014-01T-This report serves to document research conducted under Trust Fund Cooperative Agreement between ARS and the American Sheep Industry Association (ASI). Although the consumer recognizes wool for its unique properties of resiliency and warmth, its apparent discomfort and lack of dimensional stability limit apparel production and consumer acceptance. Foreign imports of wool treated by chlorination (not permitted in the United States) threaten markets for domestic wool. ARS Research under the previous project 1935-41440-011-01T resulted in an aqueous enzymatic process that whitens, biopolishes, and prevents wool from shrinking. The American Sheep Industry Association (ASI), the military, and the domestic wool industry now indicate particular attention should be given to flame retardation or prevention to meet the needs of the military. Wool will ignite and burn with a self-extinguishing flame. To meet the needs of the military for itch-free, machine washable wool with improved burn-prevention behavior, we have developed a heat resistant polymer to apply to ARS-processed wool fabric. The burning resistance of the treated fabric equals that of a wool/ Nomex fabric blend intended for military attire. The ARS product is preferred because it produces a soft crushable ash whereas the blend produces an intractable residue that can lodge in open wounds. ARS is introducing the military to comfortable, machine washable wool fabrics with improved flame retardancy (FR). This product will increase the demand for domestic wool fabrics that are processed entirely by textile mills in this country. This research concerns the apparel needs of the military in wartime and the textile industry recognizes that these developments will create novel commercial markets for wool. 1935-41440-014-02S-This report serves to document research conducted under a Specific Cooperative Agreement between ARS and the University of Georgia, which facilitated the work underwritten by base funds and Trust Fund Cooperative Agreement #58-1935-1-143 between ARS and the American Sheep Industry Association (ASI; see report for 1935-41440-014-01T).Wool fibers are flammable but the propagating flame self-extinguishes and produces a soft ash residue unlike the melt-drip behavior of synthetic fibers that form a molten, hard bead upon cooling. Because of its self-extinguishing property, wool is used in airplane interiors and ARS-processed wool fabrics that overcome the itch-factor are preferred by the military to replace synthetic polypropylene underwear. To fully meet the flame retardant requirements for military attire, wool fiber is currently blended with Nomex or Kevlar (synthetic fibers known to resist burning). To improve the flame retardant properties of ARS-processed wool, a temperature-resistant, high-performance polymer that can be applied to wool fabric was synthesized. The burning resistance of the treated fabric equals that of a wool/ Nomex fabric blend intended for military attire. The polymer incorporates the highly ordered structure of polyimide with soft segments of siloxanes to form nonignitable polyimidesiloxanes that are easy to process and exhibit thermal and radiation stability, stain and water resistance, and stability to UV light. Successful completion of this research will introduce the military to comfortable, machine-washable wool fabrics that will resist burning. To meet the military demand for these fabrics, participating wool mills are anticipated to include ERRC technology in their existing product lines, thereby increasing the demand for domestic wool fiber and apparel for traditional and new end uses. 5.Describe the major accomplishments over the life of the project, including their predicted or actual impact. This is the first annual report for this project. A major accomplishment is reported under question 4. 6.What science and/or technologies have been transferred and to whom? When is the science and/or technology likely to become available to the end-user (industry, farmer, other scientists)? What are the constraints, if known, to the adoption and durability of the technology products? Functional modification of collagen: • The collagen microfibril molecular model developed under previous projects is now providing a basis for research into the interactions of collagen with tannin-like molecules, and the effects of changes in ionic strength and pH on collagen by researchers in Europe. Functional modification of leather byproducts: • Continued MOU with Dr. Karel Kolomaznik, Professor, Tomas Bata University, Zlin, Czech Republic in which the utilization of protein hydrolysate from waste leather products will be used to lower the formaldehyde content in resins. • Developed a new MOU with Dr. Jaume Cot, Professor, Departamento de Ecotecnologías, CSIC, Barcelona, Spain for research on enzymatic modification of collagen by-products. Functional modification of wool: • Mill trials of the process, patent pending, developed under Trust Fund Agreement 58-1935-1-143 with the American Sheep Industry Association (ASI), are being conducted under more than 20 individual confidentiality agreements with American wool mills. More than 20,000 pounds of wool fabric have been ARS-processed in finishing and dyeing plants throughout the country with plans to treat to treat raw wool fiber and wool yarns for commercial and handcrafter markets. One particular mill has applied the process continuously over the past year and is now petitioning to license with the intention to supply the military with itch-free, machine-washable wool for underwear. They are supplying the military with 10,000 ARS-processed undershirts for the first and second stages of wear trials by troops in the field. They plan to use the technology for private-sector products, for which the license is required. 7.List your most important publications in the popular press and presentations to organizations and articles written about your work. (NOTE: List your peer reviewed publications below). Reports on the hides and leather phases of this project were presented to customers at the annual meeting of the Research Liaison Committee of the American Leather Chemists Association, ERRC, Wyndmoor, PA, April 26-27, 2005 (industry, academic, government representatives of the hides, leather, and tannery supplier industries). Progress reports on collaborative wool research with the American Sheep Industry Association (ASI) were prepared monthly for ASI review and presented in quarterly meetings at ERRC to an ASI representative. Collagen networks. In Leather Science and Engineering 15(1) 26-30 (in Chinese) Review Publications Gembeh, S.V., Farrell Jr, H.M., Taylor, M.M., Brown, E.M., Marmer, W.N. 2004. Application of transglutaminase to derivatize proteins. 1. studies on soluble proteins and preliminary results on wool. Journal of the Science of Food and Agriculture. 85:418-424. Taylor, M.M., Marmer, W.N., Brown, E.M. 2005. Characterization of biopolymers prepared from gelatin and sodium caseinate for potential use in leather processing. Journal of American Leather Chemists Association. 100(3):149-159. Taylor, M.M., Cabeza, L., Marmer, W.N., Brown, E.M. 2005. Preparation of high molecular weight products by crosslinking protein isolated from the enzymatic processing of chromium-containing collagenous waste i. extraction of gelatin. Leather Science and Engineering. 15(2):3-7. Brown, E.M. 2004. Potential interactions of the c-terminal telopeptides of bovine type i collagen. Journal of American Leather Chemists Association. 99(9):376-385. Lastowka, A.M., Brown, E.M., Maffia, G.J. 2005. A comparison of chemical, physical and enzymatic cross-linking of bovine type i collagen fibrils. Journal of American Leather Chemists Association. 100(5):196-202. Cardamone, J.M., Yao, J., Nunez, A. 2004. Controlling shrinkage in wool fabrics: effective hydrogen peroxide systems. Textile Research Journal. 74(10):887-898. Cardamone, J.M., Yao, J., Phillips, J.G. 2005. Combined bleaching, shrinkage prevention, and biopolishing of wool fabrics. Textile Research Journal. 75(2):169-174. Taylor, M.M., Bumanlag, L.P., Marmer, W.N., Brown, E.M. 2005. Preparation of fillers for leather from enzymatically modified collagen by-products [abstract]. American Leather Chemists Association. Paper No. 13. Kasala, J., Taylor, M.M., Raschik, P., Kolomaznik, K. 2005. Engineering study of collagen grafting [abstract]. American Leather Chemists Association. Paper No. 12. Brown, E.M., Stauffer, D.M., Cooke, P.H., Maffia, G.J. 2005. The effect of ultrasound on bovine hide collagen structure [abstract]. American Leather Chemists Association. Paper No. 14.