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casings, collagen, dispersions, films, mechanical properties


Properties of five collagen preparations were investigated to enhance understanding of in-line co-extrusion casing formation. The first study revealed that 30% NaCl and 5 min brining provided maximum strength. The second study showed 100% difference in tensile strength between preparations; when adjusted to % protein, the difference was smaller but still existed.  Extrusion force and elastic modulus (G’) also varied; appear to be acid dependent. Denaturation temperature of raw dispersions was between 36.7 and 38.9 ?C. Upon salt brining, it substantially increased to 63.3 -65.3 ?C. Polarized light microscopy revealed numerus intact segments of connective tissue fibers and some cellulose fibers.

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ASTM. 2010. Standard test method for tensile properties of this plastic sheeting. Method D882-10, Philadelphia, PA.

Avery N. and Bailey A. 2008. Restraining cross-links responsible for the mechanical properties of collagen fibers: natural and artificial. In “Collagen Structure and Mechanics”. P. Fratzl (Ed.), p. 81. Springer Science, New York, NY.

Barbut S. 2010. Microstructure of natural, extruded and co-extruded collagen casings before and after heating. Ital. J. Food Sci. 22:126.

Barbut S. 2015. Principles of meat processing. In “The Science of Poultry and Meat Processing”, ISBN-978-088955-625-6. (free download).

Barbut S. and Ioi M. 2019. An investigation of the mechanical, microstructural and thermo-mechanical properties of collagen films cross-linked with smoke condensate and glutaraldehyde. Ital. J. Food Sci. In press.

Bernal V.M. and Stanley D.W. 1986. Changes in the melting characteristics of bovine tendon collagen induced by a bacterial collagenase. J. Food Sci.51(3):834.

Bontjer M.B.H., Kuijpers M.W.J.T. and Van den Berg K.W. 2011. Method for preparing food products by co-extrusion, in particular sausage and food products obtained with this method. European patent WO 2006 135238.

Carson F.L. 1997. “Histotechnology A Self-Instructional Text” 2nd ed. American Society of Clinical Pathology, Chicago, IL, USA.

Cranston E.D. and Gray D.G. 2008. Birefringence in spin-coated films containing cellulose nanocrystals. Colloids Surf. A Physicochem. Eng. Asp.325:44.

Friess W. and Lee G. 1996. Basic thermoanalytical studies of insoluble collagen matrices. Biomaterials 17:2289.

Gioffre M., Torricelli P., Panzavolta S., Rubini K. and Bigi A. 2011. Role of pH on stability and mechanical properties of gelatin films. J. Bioact. Compat. Polym.(27):67.

Harper B.A., Barbut S., Lim L-T. and Marcone M.F. 2012. Microstructural and textural investigation of various manufactured collagen sausage casings. Food Res. Int. 49(1):494.

Harper B.A., Barbut S., Li, L-T. and Marcone M.F. 2013. Characterization of ‘wet’ alginate and composite films containing gelatin, whey or soy protein. Food Res. Int. 52:452.

Helary C., Bataille I, Abed A., Iloul C., Angelo A., Louedec L., Letourneur D., Meddahi-Pelle A. and Giraude-Guille M.M. 2009. Concentrated collagen hydrogels as dermal substitutes. Biomaterials. 31(3):481.

Karmas E. 1974. Sausage Casing Technology, Food Technology Review No 14. Noyes Data Corporation, Park Ridge, IL, USA.

Kobussen J., Bontjer M.B.H., Van den Berg K.W. and Flores H.A. Method and Device for Dehydrating Co-Extruded Food Products, U.S. patentno. 20120073454A1.

Kobussen J., Kobussen M., Kobussen J. and Alexander D. 2000. Brine Formulation for Curing Extruded Sausage Strand,U.S. patent no. 6,054,155.

Mathew A.P., Oksman K., Pierron D. and Harmad M.F. 2012. Crosslinked fibrous composites based on cellulose nanofibers and collagen with in situ pH induced fibrillation. Cellulose 19:139.

McPherson J.M., Ledger P.W., Sawamura S., Conti A., Wade S., Reihanian H. and Wallace D.G. 1986. The preparation and physicochemical characterization of an injectable form of reconstituted, glutaraldehyde crosslinked bovine corium collagen. J. Biomed. Mater. Res. B.20:79.

Morgan T.F., Frame G. and Kobussen P.J. 1988. Process for producing a linked co-extruded edible product, US patent no. 5,795,605.

Oechsle A.M., Wittmann X., Gibis M., Kohlus R. and Weiss J. 2014. Collagen entanglement influenced by the addition of acids. Eur. Poym. J. 58:144.

Oechsle A.M., Akgün D., Krause F., Maier C., Gibis M., Kohlus R. and Weiss J. 2016. Microstructure and physical–chemical properties of chicken collagen. Food Struct. 7:29.

Olde Damink L.H.H., Dijkstra P.J., Van Luyn M.J.A., Van Wachem P.B., Nieuwenhuis P. and Feijen J. 1995. Glutaraldehyde as a crosslinking agent for collagen-based biomaterials. J. Material. Sci. -Material Med. 6:460.

Osburn W.N. 2000. Collagen casings. In “Protein-based Films and Coatings., A. Gennadios (Ed.), pp. 445-465. CRC Press, Boca Raton, FL, USA.

O’Sullivan A.O., Shaw N.B., Murphy S.C., Van de Vis J.W., Van Pelt-Heerschap H. and Kerry J.P. 2006. Extraction of collagen from fish skins and its use in the manufacture of biopolymer films. J. Aquat. Food Prod. T. 15:21.

Ratanavaraporn J., Kanokpanont S., Tabata Y. and Damrongsakkul S.. 2008. Effects of acid type on physical and biological properties of collagen scaffolds, J. BiomatSci. 19(7):945.

Reddy N. and Yang Y. 2004. Properties and potential applications of natural cellulose fibers from cornhusks. J. Green Chem.7:190.

Savic Z.and Savic I. 2016. “Sausage Casings” 2nd ed. p. 75. Victus, Inc., Vienna, AUS.

Tomihata K., Burczak K., Shiraki K. and Ikada Y. 1994. Cross-linking and biodegradation of native and denatured collagen. In “Polymers of biological and biomedical significance”. W. Shalaby Y. Ikada, R. Langer and J. Williams. (Eds.), p. 275. American Chemical Society, Washington, USA.

Visser P.R. 2012. Casings for Foodstuffs, U.S. patent no. 20120114807A1.

Wang P.Y. 1986. Meat processing. In “Encyclopedia of Food Engineering”. C.W. Hall, A.W. Frall, and A.L. Rippen (Eds.), pp. 545-550. AVI Publishing Company, Inc., Westport, CT, USA.

Williams B.R., Gelman R.A., Poppke D.C. and Piez K.A.. 1978. Collagen fibril formation optimal in vitro conditions and preliminary kinetic results. J. Biol. Chem. 253(18):6578.

Wolf K.L., Sobral P.J.A. and Telis V.R.N. 2006. Characterization of collagen fibers for biodegradable films production. IUFoST 13:801.