Development of cross-linked collagen as a binding agent for restructured meat products

Collagen is added to meat products for gelling, binding and adhesion (formed meats, coatings, and batters), emulsification, water binding, and thickening properties. It also serves as an inexpensive protein filler. An innovative collagen cross-linking technique was studied with the potential to enhance and improve the functional characteristics of restructured meat products. Experiments were conducted to identify the parameters of covalently cross-linking collagen, via a horseradish peroxidase and H2O 2 catalysis mechanism, and to examine the potential for applying this technology to restructured meat products. Edible collagen was recovered from a readily available industrial by-product source (calf-hide), lyophilized, and cross-linked to form a collagen polymer. Various treatments were effectively applied to the collagen extract to characterize the polymer cross-linking technology, and this technology was applied to restructured meat products from several species as a natural binding agent. It appears that collagen polymerization, by the horseradish peroxidase and H2O2 catalysis mechanism, can increase deformation resistance in restructured meats and could potentially improve product integrity. The collagen/meat polymer matrix formed was demonstrated to by heat stable (71°C) and in creased TPA hardness and springiness values of restructured meat products in a model system. Therefore, this cross-linking technology appears to offer the potential to add value to a variety of further processed products and by-products by creating a viable and economical niche for recovered collagen. Common non-meat ingredients, specifically 1% NaCl in combination with.5% sodium tripolyphosphate (STPP), synergistically enhanced the efficacy of the collagen cross- linking reaction in restructured meat products. This synergistic effect could prove valuable for enhancing or modifying textural characteristics of restructured meat and poultry products.; It appears that specific collagen types may be more critical to the cross-linking polymerization than collagen solubility or total collagen. Thus, future application and refinement of collagen recovery techniques from by-products may provide an alternative and economically profitable outlet for an otherwise underutilized resource. In summary, this research demonstrates that cross-linking collagen with horseradish peroxidase and hydrogen peroxide has the potential to maintain or improve restructured meat product integrity, textural properties, and by-product utilization and thus warrants further investigation.