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Inedible Gelatin and Glue

  • Chapter
Inedible Meat by-Products

Part of the book series: Advances in Meat Research Series ((ADMERE,volume 8))

Abstract

Gelatins are water-soluble protein substances derived by denaturing and partially hydrolyzing collagen, the fibrous protein abundant in animal connective tissues such as bone, cartilage, skin, and tendon. A variety of gelatin types are made commercially, as well as several kinds of animal glue, which is the oldest known form of gelatin. The description of a gelatin must specify which of the different collagen raw materials and different collagen-to-gelatin conversion processes were used. A useful description will also include values of certain physicochemical properties and will specify any special processing required for intended applications (such as foods, pharmaceuticals, photographic products, adhesives, etc.).

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References

  • Adhesives Age (1990). Census of Manufacturers. Adhesives Age33 (2), 34.

    Google Scholar 

  • Ammann-Brass, H. (Ed.) (1971). Restrainers in Photographic Gelatins: IAG Reports1965–69. Internationale Arbeitsgemeinschaft für Photogelatine (IAG). Fribourg, Switzerland.

    Google Scholar 

  • Ammann-Brass, H. (Ed.) (1984). Photographic Gelatin: IAG Reports1970–82. Internationale Arbeitsgemeinschaft für Photogelatine (IAG). Fribourg.

    Google Scholar 

  • Ammann-Brass, H. & Pouradier, J. (Ed.) (1985). Photographic Gelatin: IAG Reports1983. Internationale Arbeitsgemeinschaft für Photogelatine (IAG). Fribourg.

    Google Scholar 

  • Aoyogi, S., Matsumoto, T., Shima, Y. & Ishikawa, T. (1987). Usefulness of SDS minislab method in electrophoretic analysis of photographic gelatin. J. Photogr. Sci. 35, 158.

    Google Scholar 

  • Bachinger, H.P., Bruckner, P., Timpl, R. & Engel, J. (1978). The role of cis-trans isomerization of peptide bonds in the coil-triple helix conversion of collagen. Europ. J. Biochem. 90, 605.

    Article  Google Scholar 

  • Bachinger, H.P., Bruckner, P., Timpl, R., Prockop, D.J. & Engel, J. (1980). Folding mechanism of the triple helix in type-III collagen and type-III pNcollagen. Europ. J. Biochem. 106, 619.

    Article  Google Scholar 

  • Band, S.S. (Ed.) (1987). Photographic gelatin. 5th RPS Symp., Oxford, 2–6 September, 1985. The Royal Photographic Society, Bath, England, 292 pp.

    Google Scholar 

  • Barnstein, C.H. (1966). Gelatin. In Encyclopedia of Industrial Chemical Analysis, Vol.13 (F.D. Snell & L.S. Ettre, Eds.), pp. 361–75. John Wiley, New York.

    Google Scholar 

  • Beels, R. & Claes, F.H. (1977). Diffusion phenomena in gelatin sheets. Photogr. Sci. Eng. 21, 336.

    Google Scholar 

  • Beier, G. & Engel, J. (1966). The renaturation of soluble collagen. Products formed at different temperatures. Biochemistry5, 2744.

    Article  Google Scholar 

  • Blair, W.E. & Pearson, C.L. (1987). Good tack and open time help animal glue hold market share. Adhesives Age, June, pp. 32–35.

    Google Scholar 

  • Boedtker, H. & Doty, P. (1954). A study of gelatin molecules, aggregates and gels. J. Phys. Chem. 58, 968.

    Article  Google Scholar 

  • Borchard, W., Bremer, W. & Keese, A. (1980). The state diagram of the water-gelatin system. Colloid & Polym. Sci. 258, 516.

    Article  Google Scholar 

  • Borchard, W., Luft, B. & Reutner, P. (1986). Mixed crystal formation and glassy solidification in the system gelatin-water. J. Photograph. Sci. 34, 132.

    Google Scholar 

  • Borginon, H. Ketellapper, L.W. & Derouck, A. (1980). A comparison of different methods for the determination of the reducing properties of photographic gelatin. J. Photogr. Sci. 28 111.

    Google Scholar 

  • Bruckner, P. Eikenberry, E.F. & Prockop, D.J. (1981). Formation of the triple helix of type-I procollagen incellulo-A kinetic model based on cis-trans isomerization of peptide bonds. Europ. J. Biochem. 118 607.

    Google Scholar 

  • Bsi (1975). British Standard 757: Sampling and Testing Gelatins, p. 6. British Standards Institute, London.

    Google Scholar 

  • Burness, D.M. & Pouradier, J. (1977). Gelatin. III. The hardening of gelatin and emulsions. In The Theory of the Photographic Process,4th edn. (T.H. James, Ed.), pp. 77–87. Macmillan Publishing Co., New York.

    Google Scholar 

  • Chalepakis, G., Tanay, I. & Heidemann, E. (1985). How specific is the collagen decay in the manufacture of gelatine? Leder36, 2.

    Google Scholar 

  • Chatellier, J.Y., Durand, D. & Emery, J.R. (1985). Critical helix content in gelatin gels. Int. J. Biol. Macromol. 7, 311.

    Article  Google Scholar 

  • Chevé, J.L. (1971). Ètude de la polydispersité des gélatines au moyen des tamis moléculaires. J. Chim. Phys. Phys.-Chim. Biol. 68, 258.

    Google Scholar 

  • Clark, R.C. & Courts, A. (1977). The chemical reactivity of gelatin. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 209–47. Academic Press, New York.

    Google Scholar 

  • Courts, A. (1980). Properties and uses of gelatin. In Applied Protein Chemistry ( R.A. Grant, Ed.), pp. 1–29. Applied Science Publishers, London.

    Google Scholar 

  • Croda Inc. (1990a). Pharmaceutical Product Guide. Croda Inc., 183 Madison Avenue, New York, NY 10016.

    Google Scholar 

  • Croda Inc. (1990b). Product Guide, 2nd edn. Croda Inc., 183 Madison Avenue, New York, NY 10016.

    Google Scholar 

  • Croome, R.J. (1974). Kinetics of development of rigidity in gelatin gels. J. Photogr. Sci. 22, 239.

    Google Scholar 

  • Croome, R.J. (1982a). Some aspects of the use of high molecular weight synthetic and natural polymers as additives or replacements for gelatin in photographic emulsions. J. Photogr. Sci. 30, 181.

    Google Scholar 

  • Croome, R.J. (1982b). The susceptibility to salt flocculation of chemically modified gelatins. J. Photogr. Sci. 30, 84.

    Google Scholar 

  • Dgf Stoess (1986). Konzepte, p. 12. Deutsche Gelatine-Fabriken Stoess & Co. GmbH, Eberbach, Germany.

    Google Scholar 

  • Djabourov, M. & Papon, P. (1983). Influence of thermal treatments on the structure and stability of gelatin gels. Polymer 24, 537.

    Article  Google Scholar 

  • Djabourov, M., Maquet, H.T., Leblond, J. & Papon, P. (1985). Kinetics of gelation of aqueous gelatin solutions. Brit. Poly. J. 17, 169.

    Article  Google Scholar 

  • Durand, D., Emery, J.R. & Chatellier, J.Y. (1985). Investigation of renaturation in gelatin gels. Int. J. Biol. Macromol. 7, 315.

    Article  Google Scholar 

  • Evans, R.W. (1987). Transmission optical holographic elements in dichromated gelatin. Proc. SPIE Int. Soc. Opt. Eng. 600, 38.

    Google Scholar 

  • Field, D.S. (1988). Tyrosine in photographic gelatin. J. Photogr. Sci. 36, 23.

    Google Scholar 

  • Fietzek, P.P. & Kuhn, K. (1976). The primary structure of collagen. Int. Rev. Connect. Tissue Res. 7, 1.

    Google Scholar 

  • Finch, C.A. & Jobling, A. (1977). The physical properties of gelatin. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 249–94. Academic Press, New York.

    Google Scholar 

  • Flory, P.J. (1953). Principles of Polymer Chemistry, p. 569. Cornell University Press, Ithaca, NY.

    Google Scholar 

  • Flory, P.J. & Weaver, E.S. (1960). Helix-coil transitions in dilute aqueous collagen solutions. J. Am. Chem. Soc. 82, 4518.

    Article  Google Scholar 

  • Fujii, T. & Kusoki, Y. (1985). Non-gelatin components from lime-processed gelatins: Presence of lysinoalanine and histidinoalanine. J. Soc. Photogr. Sci. Technol. Japan48, 359.

    Google Scholar 

  • Fyson, J.R. (1984). Bleaching agents and diffusion through gelatin. J. Photogr. Sci. 32, 234.

    Google Scholar 

  • Graesser, W., Koepff, P.J. & Tomka, I. (1983). Gelatin, method for producing it and its use. US Pat., 4, 369, 069.

    Google Scholar 

  • Gmia (1982). Gelatin. Gelatin Manufacturers Institute of America, Inc., New York.

    Google Scholar 

  • Gmia (1986). Standard Methods for Sampling and Testing of Gelatins. Gelatin Manufacturers Institute of America, Inc., New York.

    Google Scholar 

  • Godard, P., Biebuyck, J.J., Daumerie, M., Naveau, H. & Mercier, J.P. (1978). Crystallization and melting of aqueous gelatin. J. Polym. Sci., Polym. Phys. Ed. 16, 1817.

    Article  Google Scholar 

  • Godard, P., Biebuyck, J.J., Barriat, P.A., Naveau, H. & Mercier, J.P. (1980). Kinetics of crystallization of aqueous gelatin solutions. Makromol. Chem. 181, 2009.

    Google Scholar 

  • Grand, R.J.A. & Stainsby, G. (1976). N-terminal amino acids and gelatin gelation. In Photographic Gelatin II ( R.J. Cox, Ed.), pp. 11–26. Academic Press, New York.

    Google Scholar 

  • Gross, S. & Rose, P.I. (1975). Nongelling components from gelatin gels: Extraction and identification. J. Photogr. Sci. 23, 33.

    Google Scholar 

  • Guest, C.C. (1987). Holography. In Encyclopedia of Physical Science and Tech-nology, Vol.6 ( R.A. Meyers, Ed.), p. 514. Academic Press Inc., New York.

    Google Scholar 

  • Halpern, M. (1990). Photographic Chemicals. In Specialty Chemicals, SRI Inter-national, Menlo Park, California, pp. 99–118.

    Google Scholar 

  • Harrington, W.F. & Karr, G.M. (1970). Collagen structure in solution. II. Analysis of refolding kinetics in terms of nucleation and growth process. Biochemistry9, 3725.

    Article  Google Scholar 

  • Harrington, W.F. & Rao, N.V. (1970). Collagen structure in solution. I. Kinetics of helix regeneration in single-chain gelatins. Biochemistry9, 3714.

    Article  Google Scholar 

  • Hauschka, P.V. & Harrington, W.F. (1970). Collagen structure in solution. V. Kinetic mechanism of refolding of cross-linked chains. Biochemistry9, 3754.

    Article  Google Scholar 

  • Hermel, H., Wetzel, R., Buder, E., Roth, C., Herbrich, H. & Legutke, H. (1991). Moisture, triple-helical content and brittleness of gelatin layers. J. Photogr. Sci. 39, 16.

    Google Scholar 

  • Hinterwaldner, R. (1977a). Raw materials. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 295–314. Academic Press, New York.

    Google Scholar 

  • Hinterwaldner, R. (1977b). Technology of gelatin manufacture. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 315–64. Academic Press, New York.

    Google Scholar 

  • Hopkins, W.J., Diefendorf, E.J. & Feairheller, S.H. (1985). A method of processing fresh butcher-hogskins. J. Amer. Leather Chem. Assoc. 80, 165.

    Google Scholar 

  • Hubbard, J.R. (1977) Animal glues. In Handbook of Adhesives ( I. Skeist, Ed.), pp. 139–51. Van Nostrand Reinhold, New York. Internationale Arbeitsgermeinschaft für Photogelatine (IAG). International Working Group for Photographic Gelatin. IAG, Bourg La Reine, France.

    Google Scholar 

  • Itoh, N. (1989). Modern manufacturing methods for photographic gelatin. J. Soc. Photogr. Sci. Tech. Japan52 (4), 329.

    Google Scholar 

  • Jacobson, R.E. (1976). The hydrolysis of gelatin by proteolytic enzymes and their use in photographic emulsion preparation. In Photographic Gelatin II(R.J. Cox, Ed.), pp. 233–51. Academic Press, New York.

    Google Scholar 

  • Janus, J. & Lyons, C.A. (1975). The nucleic acid contents of the IAG gelatins. J. Photogr. Sci. 23, 125.

    Google Scholar 

  • Janus, J., Kenchington, A.W. & Ward, A.G. (1951). Rapid method for the determination of the isoelectric point of gelatin using mixed-bed deionization. Research (London) 4, 247.

    Google Scholar 

  • Johns, P. (1977). The structure and composition of collagen-containing tissues. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 31–72. Academic Press, New York.

    Google Scholar 

  • Jolley, J.E. (1970). The microstructure of photographic gelatin binders. J. Photogr. Sci. Eng. 14, 169.

    Google Scholar 

  • Jones, N.R. (1977). Uses of gelatin in edible products. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 365–94. Academic Press, New York.

    Google Scholar 

  • Katz, E.P. & Li, S.-T. (1973). Structure and function of bone collagen fibrils. J. Mol. Biol. 80, 1.

    Article  Google Scholar 

  • Kenchington, A.W. & Ward, A.G. (1954). The titration curve of gelatin. Biochem. J. 58, 202.

    Google Scholar 

  • King, S.A., Rose, P.I. & Maskasky, J.E. (1990). Modified peptizer twinned grain silver halide emulsions and processes for their preparation. US Patent 4 942 120.

    Google Scholar 

  • Kobayashi, H., Sugimoto, K., Ohno, T. & Mizusawa, S. (1989). Electrochemical detection of reducing sugars in photographic gelatins. J. Photogr. Sci. 37, 49.

    Google Scholar 

  • Koepff, P. (1980). Use of gel electrophoresis in the manufacture of gelatin-inert 2nd generation gelatin. Leder31 (5), 83.

    Google Scholar 

  • Kragh, A.M. (1977). Swelling, adsorption and the photographic uses of gelatin. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 439–74. Academic Press, New York.

    Google Scholar 

  • Leach, A.A. & Eastoe, J.E. (1977). The chemical examination of gelatin. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 475–506. Academic Press, New York.

    Google Scholar 

  • Levinson, G.I.P. (1977). Diffusion transfer and monobaths. In The Theory of the Photographic Process, 4th edn. ( T.H. James, Ed.), pp. 466–80. Macmillan Publishing Co., New York.

    Google Scholar 

  • Lewis, M.S. & Piez, K.A. (1964). Sedimentation-equilibrium studies of the molecular weight of single and double chains from ratskin collagen. Biochemistry3, 1126.

    Article  Google Scholar 

  • Light, N.D. & Bailey, A.J. (1982). Covalent crosslinks in collagen, In Methods in Enzymology, Part A, Extracellular Matrix, Vol.82 (L.W. Cunningham & D.W. Frederiksen, Eds.), pp. 360–72. Academic Press, New York.

    Google Scholar 

  • Lorry, D. & Vedrines, M. (1985). Determination of molecular weight distribution of gelatines by HPSEC. In Photographic Gelatin. IAG Reports1983(H. Ammann-Brass, Ed.), p. 35. IAG, Fribourg, Switzerland.

    Google Scholar 

  • Lower, E.S. (1983a). Utilising gelatin: Some applications in the coatings, adhesives and allied industries. Pigm. Resin Technol. 12 (7), 9.

    Article  Google Scholar 

  • Lower, E.S. (1983b). Utilising gelatin: Some applications in the coatings, adhesives and allied industries-2. Pigm. Resin Technol. 12 (8), 9.

    Article  Google Scholar 

  • Marshall, A.S. & Petrie, S.E.B. (1980). Thermal transitions in gelatin and aqueous gelatin solutions. J. Photogr. Sci. 28, 128.

    Google Scholar 

  • Marshall, A.S. & Petrie, S.E.B. (1981). Thermal transitions and physical aging in gelatin. Proc. N. Amer. Thermal Analysis Soc. Conf. 11, 183.

    Google Scholar 

  • Maskasky, J.E. (1989a). A comparison of oxidized and non-oxidized gelatins. I. Silver ion binding. J. Imaging Sci. 33, 10.

    Google Scholar 

  • Maskasky, J.E. (1989b). A comparison of oxidized and non-oxidized gelatins. II. Precipitation of tabular grain emulsions. J. Imaging Sci. 33, 13.

    Google Scholar 

  • Maxey, C.R. & Palmer, M.R. (1976). The isoelectric point distribution of gelatin. In Photographic Gelatin II ( R.J. Cox, Ed.), pp. 27–36. Academic Press, New York.

    Google Scholar 

  • Mccroskery, P.A., Wood, S. & Harris, E.D. (1973). Gelatin: A poor substrate for a mammalian collagenase. Science182, 70.

    Article  Google Scholar 

  • Miller, A.T. & Karmas, E. (1985). Age-related changes of bovine corium. J. Amer. Leather Chem. Assoc. 80, 106.

    Google Scholar 

  • Mitchell, J.R. (1976). Rheology of gels J. Texture Studies7, 313.

    Article  Google Scholar 

  • Moll, F. (1989). The oxidation of gelatin. J. Photogr. Sci. 37, 14.

    Google Scholar 

  • Moll, F.J. & Wagner, K. (1989). Determination of cysteine/cystine in gelatin. J. Photogr Sci. 37, 19.

    Google Scholar 

  • Moll, F., Mücke, B., Wagner, K., Gareis, H., Graesser, W. & Koepff, P. (1991). Production of a silver halide emulsion. US Patent 4 992 362.

    Google Scholar 

  • Nimni, M. (1988). (Ed.) Collagen: Biochemistry, Biotechnology and Molecular Biology, Vol. 3. CRC Press Inc., Boca Raton.

    Google Scholar 

  • Noel, C., Renotte, Y. & Lion, Y. (1990). The primitive emulsion as a tool for gelatin classification. J. Photogr. Sci. 38, 20.

    Google Scholar 

  • Norland, R.E. (1977). Fish glue. In Handbook of Adhesives. (I. Skeist, Ed.), Van Nostrand Reinhold, New York; General Information Bulletin 1- Photoengraving Glue. Norland Products Inc., 695 Joyce Kilmer Ave., New Brunswick, NJ, pp. 152–7.

    Google Scholar 

  • Ohno, T., Morikawa, M., Irie, H. & Muto, G. (1980a). Analysis of nucleic acid bases in photographic gelatins by high-performance liquid chromatography. J. Photogr. Sci. 28, 23.

    Google Scholar 

  • Ohno, T., Misuzawa, S., Itoh, M., & Muto, G. (1980b). Analysis of free nucleic acid bases in photographic gelatin by liquid chromatography. J. Photogr. Sci. 28, 238.

    Google Scholar 

  • Pagi (1977). Testing Methods for Photographic Gelatins, 3rd edn. Photographic and Gelatin Industries, Photo-Sensitized Materials Manufacturers’ Assoc., Tokyo, Japan.

    Google Scholar 

  • Piez, K.A. (1968). Molecular weight determination of random coil polypeptides from collagen by molecular sieve chromatography. Anal. Biochem. 26, 305.

    Article  Google Scholar 

  • Piez, K.A. (1987). Collagen. In Encyclopedia of Polymer Science and Engineering, 2nd edn., Vol.3 (J. Kroschwitz, Ed.), pp. 699–727. John Wiley & Sons, New York.

    Google Scholar 

  • Pouradier, J. (1973). Formation des gels de gélatine. C.R. Acad. Sci. 277, 1093.

    Google Scholar 

  • Pouradier, J. (1977). Gelatin. II. Properties of gelatin in relation to its use in the preparation of photographic emulsions. In The Theory of the Photographic Process, 4th edn. ( T.H. James, Ed.), pp. 67–76. Macmillan Publishing Co., New York.

    Google Scholar 

  • Pouradier, J. & Rondeau, A. (1968). On the methionine sulphoxide of gelatin. J. Photogr. Sci. 16, 68.

    Google Scholar 

  • Preston, B.N. & Meyer, F.A. (1971). Physical behavior of gelatin gels: A simple model for connective tisue. Biopolymers10, 35.

    Article  Google Scholar 

  • Riimaki, T.A. & Middleman, S. (1974). The effect of shear rate on the kinetics of gelation. Macromolecules7, 675.

    Article  Google Scholar 

  • Rose, P.I. (1987). Computer-assisted modeling of gelatin properties: Effects of peptide size and alpha-chain sequence. J. Photogr. Sci. 34, 114.

    Google Scholar 

  • Rose, P.I. (1977). Gelatin. I. General properties. In The Theory of the Photographic Process, 4th edn. ( T.H. James, Ed.), pp. 51–67. MacMillan Publishing Co., New York.

    Google Scholar 

  • Rose, P. & Gross, S. (1975). Non-gelling components from gelatin gels: Extraction and identification. J. Photogr. Sci. 23, 59.

    Google Scholar 

  • Rose, P.I. & Kaplan, C.J. (1985). Analysis for methionine in gelatin and evidence of its involvement in reduction of gold (III). In Photographic Gelatin. IAG Reports1983 ( H. Ammann-Brass, Ed.), pp. 168–79. IAG, Fribourg, Switzerland.

    Google Scholar 

  • Rose, P.I. & Suarez, S.S. (1984). Hexose sugars in photographic gelatins. In Photographic Gelatin. IAG Reports1970–1982 ( H. Ammann-Brass, Ed.), pp. 134–41. IAG, Fribourg, Switzerland.

    Google Scholar 

  • Rose, P.I., Suarez, S.S. & Bronson, J.L. (1979). Gelatin molecular weight distribution by gel filtration and high pressure liquid chromatography. Paper presented at The Royal Photographic Society Fourth Conference on Photographic Gelatin, Oxford, September 1979.

    Google Scholar 

  • Saunders, P.R. & Ward, A.G. (1954). An absolute method for the rigidity modulus of gelatin gels. In Proc. 2nd Int. Congr. Rheol. ( V.G.W. Harrison, Ed.), p. 284. Academic Press, New York.

    Google Scholar 

  • Saunders, P.R. & Ward, A.G. (1955). Mechanical properties of degraded gelatins. Nature176, 26.

    Article  Google Scholar 

  • Scholtan, W., Lange, H., Rosenkranz, H. & Moll, F. (1974). Bestimmung des Molekulargewichts and der Molekulargewichtsverteilung von Gelatine mit Hilfe der Gelchromatographie and der Ultrazentrifuge. Coll. Polym. Sci. 252, 949.

    Article  Google Scholar 

  • Silver, F.H. & Trelstad, R.L. (1981). Physical properties of type I collagen in solution: Structure of a-chains and ß-and y-components and two-component mixtures. Biopolymers20, 359.

    Article  Google Scholar 

  • Sjolinder, S. (1986). Dichromated gelatin and light sensitivity. J. Imaging Sci. 30, 151.

    Google Scholar 

  • Sri International (1987). Water soluble polymers. Chemical Economic Handbook, July. SRI International, Menlo Park, California.

    Google Scholar 

  • Stainsby, G. (1977). The physical chemistry of gelatin in solution. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, EDS.), pp. 109–36. Academic Press, New York.

    Google Scholar 

  • Stainsby, G. (1987). Gelatin gels. In Collagen as a Food (A.M. Pearson, T.R. Dutson & A.J. Bailey, Eds.) Adv. Meat Res. 4, 209.

    Google Scholar 

  • Sterman, M.D., Faust, M.A., Genova, D.J., Curme, H.G. & Johnson, M.F. (1972). Effect of chemical crosslinks on the thermal stability of conformation in swollen gelatin films In Photographic Gelatin (R.J. Cox, Ed.), pp 113–120. Academic Press, New York.

    Google Scholar 

  • Stickley, F.L. (1986). The biodegradation of gelatin and its problems in the photographic industry. J. Photogr. Sci. 34, 111.

    Google Scholar 

  • Stryer, L. (1982). Biochemistry, 2nd edn., pp. 185–204. W.H. Freeman and Co., San Francisco.

    Google Scholar 

  • Te Nijenhuis, K. (1981). Investigation into the ageing process in gels of gelatin/ water systems by the meaurement of their dynamic moduli. Part I. Phenomenology. Colloid & Polymer Sci. 259, 522.

    Article  Google Scholar 

  • Todd, A. (1961). Rigidity factor of gelatin gels. Nature191, 567.

    Article  Google Scholar 

  • Tomka, I. (1979). Electrophoresis as a routine tool to investigate photographic gelatins. Paper presented at The Royal Photographic Society Fourth Conference on Photographic Gelatin, Oxford, September 1979.

    Google Scholar 

  • Tomka, I. (1982). Photographic material. US Patent 4 360 590.

    Google Scholar 

  • Tomka, I. (1983). Die Makromolekulare Charakterisierung der Gelatine. Chimia37, 33.

    Google Scholar 

  • Tomka, I., Bohonek, J., Spuhler, A. & Ribeaud, M. (1975). Structure and formation of gelatin gel. J Photogr. Sci. 23, 97.

    Google Scholar 

  • Torchia, D.A., Hiyama, Y., Sarkar, S.K., Sullivan, C.E. & Young, P.E. (1985). Multinuclear magnetic resonance studies of collagen molecular structure and dynamics. Biopolymers24, 65.

    Article  Google Scholar 

  • Traub, W. & Piez, K.A. (1971). Chemistry and structure of collagen. In Advances in Protein Chemistry, Vol.25 (C.B. Anfinsen, J.T. Edsall & F.M. Richards, Eds.), pp. 243–352. Academic Press, New York.

    Google Scholar 

  • Umberger, J.Q. (1967). Solution and gelation of gelatin as related to solvent structure. Photogr. Sci. Eng. 11, 385.

    Google Scholar 

  • Us Department pf Commerce & Bureau of The Census (1987). Census of Manufacturers, Adhesives and Sealants, Industry 2891. US Government Printing Office, Washington DC.

    Google Scholar 

  • Usp (1980). The United States Pharmacopeia, 20th Rev. The United States Pharmacopeial Convention, Inc., Rockville, MD.

    Google Scholar 

  • Veis, A. (1964). The Macromolecular Chemistry of Gelatin. Academic Press, New York.

    Google Scholar 

  • Veis, A. (1970). In Biological Polyelectrolytes (A. Veis, Ed.), pp. 211–73. Marcel Dekker, New York.

    Google Scholar 

  • Vera, V.D., Gratacos, E. & Cot, J. (1977). The effect of hydrogen peroxide on collagen. Part II. The use of hydrogen peroxide as a sole decomposition agent in a two-stage process for gelatin manufacture. Leder28 (10), 161.

    Google Scholar 

  • Viro, F. (1980). Gelatin. In Kirk-Othmer Encyclopedia of Chemical Technology, 3rd edn., Vol.11, p. 714. John Wiley & Sons, New York.

    Google Scholar 

  • Wainewright, F.W. (1977). Physical tests for gelatin and gelatin products. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 507–34. Academic Press, New York.

    Google Scholar 

  • Wetzel, R., Buder, E., Hermel, H. & Huttner, A. (1987). Conformations of different gelatins in solutions and in films. An analysis of circular dichroism (CD) measurements. Coll. & Polym. Sci. 265, 1036.

    Google Scholar 

  • Wood, P.D. (1977). Technical and pharmaceutical uses of gelatin. In The Science and Technology of Gelatin (A.G. Ward & A. Courts, Eds.), pp. 413–37. Academic Press, New York.

    Google Scholar 

  • Xu, K., Zhang, L. & Sun, L. (1989). Identification and quality control of Ejiao (donkey-skin) gelatin. Yaowu Fenxi Zazhi9 (6), 332.

    Google Scholar 

  • Yannas, I.V. (1972). Collagen and gelatin in the solid state. J. Macromol. Sci. Revs. Macromol. Chem. C7(1), 49.

    Google Scholar 

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  1. Photographic Research Laboratories, Eastman Kodak Company, Rochester, NY, 14650, USA

    Philip I. Rose

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  1. Philip I. Rose
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  1. Department of Animal Science, Oregon State University, Oregon, USA

    A. M. Pearson

  2. Agricultural Experiment Station, Oregon State University, Oregon, USA

    T. R. Dutson

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© 1992 Elsevier Science Publishers Ltd

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Rose, P.I. (1992). Inedible Gelatin and Glue. In: Pearson, A.M., Dutson, T.R. (eds) Inedible Meat by-Products. Advances in Meat Research Series, vol 8. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-7933-1_10

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  • DOI: https://doi.org/10.1007/978-94-011-7933-1_10

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-011-7935-5

  • Online ISBN: 978-94-011-7933-1

  • eBook Packages: Springer Book Archive

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