WOOL AND KERATIN FROM WOOL FOR BIO-BASED VALUE-ADDED PRODUCTS
Location: Biobased and Other Animal Co-Products
Title: Keratin materials for new product development
Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: May 1, 2011
Publication Date: June 1, 2011
Citation: Cardamone, J.M. 2011. Keratin materials for new product development [abstract]. Europolymer Conference. p. 1.
Keratin from wool is a reactive, biocompatible, and biodegradable material found as pure protein in over 90% by weight of fiber. As a polymeric amide, keratin is a rich source of intermediate filament proteins (IFPs) which are being investigated for a wide range of biomaterial applications. The potential of reactive polypeptide chains through of sulfhydryl, phenolic, quanidine, imidazole, and carboxyl functions offers opportunities for niche market potential as biobased feedstock for novel products and applications for the pharmaceutical, cosmetic, and biomaterials industries. Keratin was extracted from fine and coarse U.S. domestic wool by oxidation and reduction processes under a variety of conditions for transformation into keratin hydrolysates, powders, gels, films, mats, scaffolds, sponge, and microfibers. The various physical forms retained the unique characteristics of natural keratin as documented by gel electrophoresis and scanning electron microscopy. These materials were characterized for functional group and amino acid content. The identities of peptide fractions and protein homologs were investigated by MALDI-TOF TOF with confirmation of Type II microfibrillar component 7C, Type I microfibrillar 48kDa component 8C-1, and Type I microfibrillar 47.6 kDa containing alanine, glutamine, glutamic acid, leucine, serine, leucine, and cystine with highest amounts glutamic acid and leucine amino acids for subsequent crosslinking. Extracted keratins with a broad range of molecular weights from 100 to 500 Da and from 8 kDa to 40-60 Kd were investigated by FTIR spectroscopy for microstructural conformations of alpha-helix, beta-sheet, and disordered regions. The content of alpha-helical, beta-sheet and secondary structures characterized keratin as viable starting material for chemical modification to form novel biobased materials useful in industrial formulations and compositions. An isolated keratin sponge hydrogel of high porosity and interconnected pore network, exhibiting high moisture uptake and release properties, was investigated for drug delivery in simulated gastric fluid. Physical property evaluation with differential scanning calorimetry and texture profile analysis for hardness, springiness, and cohesiveness indicated induced toughness upon compression to suggest the use of keratin sponge-hydrogel as implantable material.