Abstract
Cryoprotectants are compounds that improve the quality and extend the shelf life of frozen foods. The term cryoprotectant includes all compounds that help to prevent deleterious changes in foods caused by freezing and thawing processes or frozen storage. These substances may be added during processing and product formulation or produced naturally in the living organism from which the food is derived.
Keywords
- Freezing Point
- Freeze Storage
- Myofibrillar Protein
- Sodium Lactate
- Antifreeze Protein
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, access via your institution.
Buying options
Preview
Unable to display preview. Download preview PDF.
References
Acton, J.C. and Dick, R.L. 1989. Functional roles of heat induced protein gelation in processed meat. In Food Proteins. (Kinsella, J.E. and Soucie, W.G., eds.) pp. 195–209, AOCS: Protein and Coproducts Div., Champaign, 111.
Arai, S., Watanabe, M., and Tsuji, R.F. 1984. Enzymatically modified gelatin as an antifreeze protein. Agric. Biol. Chem. 48:2173–2175.
Arakawa, T. and Timasheff, S.N. 1982a. Preferential interactions of proteins with salts in concentrated solutions. Biochem. 21(25):6545–6552.
Arakawa, T. and Timasheff, S.N. 1982b. Stabilization of protein structure by sugars. Biochem. 21(25):6536–6544.
Arakawa, T. and Timasheff, S.N. 1984a. Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding. Biochem. 23 (25): 5912-5923.
Arakawa, T. and Timasheff, S.N. 1984b. Protein stabilization and destabilization by guanidinium salts. Biochem. 23 (25):5924–5929.
Arakawa, T. and Timasheff, S.N. 1985. The stabilization of proteins by osmolytes. Biophys. J. 47:411–414.
Ashburner, M. and Bonner, J.J. 1979. The induction of gene activity in Drosophila by heat shock. Cell. 17:241–254.
Ashie, I.N.A. and Lanier, T.C. 1996. Baro-and cryo-protection of proteins in pressure-assisted freezing of seafoods. Proceedings of the Joint Atlantic Fisheries Technologists and Seafood Science Americas Conference, University of Florida, Gainesville, FL. Sea Grant. In press.
Aunaas, T. 1982. Nucleating agents in the haemolymph of an intertidal mollusc tolerant to freezing. Experientia. 38:1456–1457.
Barringer, S.A. 1997. Personal communication.
Berry, E.D. 1996. Characterization of the cold shock response of Bacillus cereus. Ph.D. Thesis. North Carolina State University, Raleigh.
Budiaman, E.R. and Fennema, O. 1987a. Linear rate of water crystallization as influenced by temperature of hydrocolloid suspensions. J. Dairy Sci. 70:534–546.
Budiaman, E.R. and Fennema, O. 1987b. Linear rate of water crystallization as influenced by viscosity of hydrocolloid suspensions. J. Dairy Sci. 70:547–554.
Calvelo, A. 1981. Recent studies on meat freezing. In Developments in Meat Science, vol. 2. (Lawrie, R., ed.) pp. 125–158, Applied Science Publishers, Barking, UK.
Careche, M. and Tejada, M. 1990a. The effect of neutral and oxidized lipids on functionality in hake (Merluccius merluccius L.): a dimethylamine-and formaldehyde-forming species during frozen storage. Food Chem. 36:113–128.
Careche, M. and Tejada, M. 1990b. Effect of neutral and oxidized lipids on protein functionality in megrim (Lepidorhombus whiffiagonis W.) and sardine (Sardina pilchardus R.) during frozen storage. Food Chem. 37:275–287.
Carpenter, J.F. and Crowe, J.H. 1988. The mechanism of cryoprotection of proteins by solutes. Cryobiol. 25:244–255.
Carpenter, J.F., Crowe, L.M., and Crowe, J.H. 1987. Stabilization of phosphofructokinase with sugars during freeze-drying: characterization of enhanced protection in the presence of divalent cations. Biochim. Biophys. Acta 923:109–115.
Carpenter, J.F., Hand, S.C., Crowe, L.M., and Crowe, J.H. 1986. Cryoprotection of phosphofructokinase with organic solutes: characterization of enhanced protection in the presence of divalent cations. Arch. Biochem. Biophys. 250:505–512.
Carpenter, J.F. and Hansen, T.N. 1992. Antifreeze protein modulates cell survival during cryopreservation: mediation through influence on ice crystal growth. Proc. Natl. Acad. Sci. USA. 89:8953–8957.
Carpenter, J.F., Martin, B., Crowe, L.M., and Crowe, J.H. 1987. Stabilization of phosphofructokinase during air-drying with sugars and sugar/transition metal mixtures. Cryobiol. 24:455–164.
Carpenter, J.F., Martin, B., Loomis, S.H., and Crowe, J.H. 1988. Long-term preservation of dried phosphofructokinase by sugars and sugar/zinc mixtures. Cryobiol. 25:372–376.
Carpenter, J.F., Petrelski, S.I, Anchordoguy, T.I, and Arakawa, T. 1994. Interactions of stabilizers with proteins during freezing and drying. In Formulation and Delivery of Proteins and Peptides, vol. 567. (Cleland, J.L. and Langer, R., eds.) pp. 134–147, American Chemical Society, Washington, D.C.
Carvajal, P.A. and Lanier, T.C. 1997. Cryoprotection of intact muscle by carbohydrate infusion. J. Food Sci. In press.
Carvajal, P.A., Lanier, T.C., and MacDonald, G.A. 1997. Cryoprotection of Alaska pollock surimi by maltodextrins. Cryobiol. In press.
Cheung, H.C. 1969. Conformation of myosin: effects of substrates and modifiers. Biochem. Biophys. Acta 194:478–484.
Connell, J.J. 1961. The relative stabilities of the skeletal muscle myosins of some animals. Biochem. J. 80:503–509.
Costanzo, J.P., Lee, R.E., and Wright, M.F. 1991. Glucose loading prevents freezing injury in rapidly cooled wood frogs. Am. J. Physiol. 261:R1549–R1553.
Cotterill, O.J. 1986. Freezing egg products. In Egg Science and Technology, 3d ed. (Stadelman, W.J. and Cotterill, O.J., eds.) pp. 217–242, AVI Publishing, Westport, Conn.
DeValdez, G.F. and Diekmann, H. 1993. Freeze-drying conditions of starter cultures for sourdoughs. Cryobiol. 30:185–190.
DeVries, A.L. 1988. The role of antifreeze glycopeptides and peptides in the freezing avoidance of Antarctic fishes. Comp. Biochem. Physiol. 90B:611–621.
Dyer, W.J. 1971. Speed of freezing and quality of frozen fish. In Fish Inspection and Quality Control. (Kreuzer, R., ed.) pp. 75–81, Fishing News Books, London.
Dyer, W.J. and Peters, J. 1969. Factors influencing quality changes during frozen storage and distribution of frozen products, including glazing, coating, and packaging. In Freezing and Irradiation of Fish. (Kreuzer, R., ed.) Fishing News Books, London.
Eastman, J.T. and DeVries, A.L. 1986. Antarctic fishes. Sci. Am. 255:106–117.
Fahy, G.M., MacFarlane, D.R., Angell, C.A., and Meryman, H.T. 1984. Vitrification as an approach to cryopreservation. Cryobiol. 21:407–426.
Fahy, G.M., Levy, D.I., and Ali, S.E. 1987. Some emerging principles underlying the physical properties, biological actions, and utility of vitrification solutions. Cryobiol. 24:196–213.
Feeney, R.E. and Yeh, Y. 1993. Anti-freeze proteins: properties, mechanisms of action, and possible applications. Food Technol. 47:82–90.
Fennema, O. 1996. Water and ice. In Food Chemistry, 3d ed. (Fennema, O., ed.) pp. 1–94, Marcel Dekker, New York.
Franks, F. 1985a. Biophysics and Biochemistry at Low Temperatures. Cambridge University Press, UK.
Franks, F. 1985b. Complex aqueous systems at subzero temperatures. In Properties of Water in Foods. (Simantos, D. and Multon, J.L., eds.) pp. 497–509, Martinus Nijhoff Publishers, Dordrecht, The Netherlands.
Fukuda, Y. 1989. ATPase as an indicator of surimi quality. Paper presented at Pacifichem 1989; subsymposium:Use of fish minces and surimi products by the food industry: fish meat as raw material, Hawaii.
Fukuda, Y, Tarakita, Z., and Arai, K. 1984. Effect of freshness of chub mackerel on the freeze denaturation of myofibrillar protein. Bull. Jpn. Soc. Sci. Fish. 50(5):845–852.
Gekko, K. and Morikawa, T. 1981. Thermodynamics of polyol-induced thermal stabilization of chymotrypsinogen. J. Biochem. 90(1):51–60.
Gekko, K. and Timasheff, S.N. 1981. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochem. 20:4667–4676.
George, R.M. 1993. Freezing processes used in the food industry. Trends Food Sci.Technol. 4:134–138.
Goff, H.D., Caldwell, K.B., and Stanley, D.W. 1993. The influence of polysaccharides on the glass transition in frozen sucrose solutions and ice cream. J. Dairy Sci. 76:1268–1277.
Gordon, M. and Taylor, J.S. 1952. Ideal copolymers and the second-order transitions of synthetic rubbers. I. Non-crystalline copolymers. J.Appl. Chem. 2:493–501.
Haard, N.F. 1992. Biochemical reactions in fish muscle during frozen storage. In Seafood Science and Technology. (Bligh, E.G., ed.) pp. 176–209, Fishing News Books, Oxford.
Hartel, R.W. 1996. Ice crystallization during the manufacture of ice cream. Trends Food Sci.Technol. 7:315–321.
Hazen, K.C., Bourgeois, L.D., and Carpenter, J.F. 1988. Cryoprotection of antibody by organic solutes and organic solute/divalent cation mixtures. Arch. Biochem. Biophys. 267:363–371.
Hightower, K.E. and McCarty, R.E. 1996. Influence of nucleotides on the cold stability of chloroplast coupling factor 1. Biochem. 35:10051–10057.
Hirsh, A.G. 1987. Vitrification in plants as a natural form of cryoprotection. Cryobiol. 24:214–228.
Holten, C.H., Muller, A., and Rehbinder, D. 1971. Lactic Acid: Properties and Chemistry of Lactic Acid and Its Derivatives. Verlag Chemie GmbH, Weinheim.
Ijichi, K., Palmer, H.H., and Lineweaver, H. 1970. Frozen whole eggs for scrambling. J. Food Sci. 35:695–698.
Ishimori, H. 1996. Vitrification of mouse and bovine embryos using a mixture of ethylene glycol and dimethyl sulfoxide. Snow Brand R&D Rep. 106:115–152.
Jiang, S.T., Hwang, B.O., and Tsao, C.T. 1987. Protein denaturation and changes in nucleotides of fish muscle during frozen storage. J. Agric. Food Chem. 35:22–27.
Kalichevsky, M.T., Knorr, D., and Lillford, P.J. 1995. Potential food applications of high-pressure effects on ice-water transitions. Trends Food Sci. Technol. 6:253–259.
Knight, C.A. and Duman, J.G. 1986. Inhibition of recrystallization of ice by insect thermal hysteresis proteins: a possible cryoprotective role. Cryobiol. 23:256–262.
Knight, C.A., Wen, D., and Laursen, R.A. 1995. Nonequilibrium antifreeze peptides and the recrystallization of ice. Cryobiol. 32:23–34.
Kresin, M., Heschel, I., and Rau, G. 1994. Expectations and limitations of vitrification as a method for cryopreservation. Cryobiol. 30:573.
Kumazawa, Y., Oozaki, Y., Iwami, S., Matsumoto, I., and Arai, K. 1990. Combined protective effect of inorganic pyrophosphate and sugar on freeze-denaturation of carp myofibrillar protein. Nippon Suisan Gak. 56(1):105–113.
Lanier, T.C. and Akahane, T. 1986. Method of retarding denaturation of meat products. U.S. patent no. 4,572,838.
Lee, R. 1991. Principles of insect low temperature tolerance. In Insects at Low Temperature. (Lee, R.E. and Denlinger, D.L., eds.) pp. 17–41, Chapman & Hall, NewYork.
Lee, J.C. and Timasheff, S.N. 1981. The stabilization of proteins by sucrose. J. Biol. Chem. 256(14):7193–7201.
Leistner, L. 1978. Hurdle effect and energy saving. In Food Quality and Nutrition. (Downey, W.K., ed.) pp. 553–557, Elsevier, Essex, UK.
Levine, H. and Slade, L. 1986. A polymer physico-chemical approach to the study of commercial starch hydrolysis products (SHPs). Carbohydr. Polym. 6:213–244.
Levine, H. and Slade, L. 1988a. A food polymer science approach to the practice of cryostabilization technology. Comments Agric. Food Chem. 1:315–396.
Levine, H. and Slade, L. 1988b. Principles of “cryostabilization” technology from structure/property relationships of carbohydrate/water systems: a review. Cryo-Lett. 9:21–63.
Levine, H. and Slade, L. 1989. Response to the letter by Simatos, Blond, and Le Meste on the relation between glass transition and stability of a frozen product. Cryo-Lett. 10:347–370.
Lewis, J.G., Learmonth, R.P., and Watson, K. 1994. Cryoprotection of yeast by alcohols during rapid freezing. Cryobiol. 31:193–198.
Li, J. and Lee, T.-C. 1995. Bacterial ice nucleation and its potential application in the food industry. Trends Food Sci. Technol. 6:259–265.
Lim, M.H. 1989. Studies of reaction kinetics in relation to thermal behavior of solutes in frozen systems. Ph.D. Thesis. University of California-Davis.
Loomis, S.H., Carpenter, T.J., Anchordoguy, T.J., Crowe, J.H., and Branchini, B.R. 1989. Cryoprotective capacity of end products of anaerobic metabolism. J. Exp. Zoo. 252:9–15.
Loomis, S.H., Carpenter, T.J., and Crowe, J.H. 1988. Identification of strombine and taurine as cryoprotectants in the intertidal bivalve Mytilus edulis. Biochim. Biophys. Acta 94:113–118.
Love, R.M. 1962. New factors involved in the denaturation of frozen cod muscle protein. J. Food Sci. 27:544–550.
Love, R.M. 1988. The Food Fishes: Their Intrinsic Variation and Practical Implications. pp. 130–140, Van Nostrand Reinhold, New York.
MacDonald, G.A. and Lanier, T.C. 1991. The role of carbohydrates as cryoprotectants in meats and surimi. Food Technol. (March): 150–159.
MacDonald, G.A. and Lanier, T.C. 1994. Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts. J. Food Sci. 59(1):101–105.
MacDonald, G.A., Lanier, T.C., and Giesbrecht, F.G. 1996. Interaction of sucrose and zinc for cryoprotection of surimi. J.Agric. Food Chem. 44(1):113–118.
MacDonald, G.A., Lanier, T.C., Swaisgood, H.E., and Hamann, D.D. 1996. Mechanism for stabilization of fish actomyosin by sodium lactate. J. Agric. Food Chem. 44(1):106–112.
MacDonald, G.A., Wilson, N.D.C., and Lanier, T.C. 1990. Stabilised mince: an alternative to the traditional surimi process. In Chilling and Freezing of New Fish Products, pp. 69–76, International Institute of Refrigeration, Aberdeen, Scotland.
MacFarlane, D.R. 1987. Physical aspects of vitrification in aqueous solutions. Cryobiol. 24:181–195.
Maresca, B., Patriarca, E., Goldenberg, C., and Sacco, M. 1988. Heat shock and cold adaptation in Antarctic fishes: a molecular approach. Comp. Biochem. Physiol. 90B:623–629.
Meryman, H.T. 1971. Cryoprotective agents. Cryobiol. 8:173–183.
Mornet, D., Bonet, A., Audemard, E., and Bonicel, J. 1989. Functional sequences of the myosin head. J. Musc. Res. Cell Motility 10:10–24.
Mornet, D., DerTerrossian, E., Pradel, L.A., Kassab, R., and Barman, T.E. 1977. The reaction of myosin with bromoalkyl analog of adenosine triphosphate. FEBS Lett. 84:362–366.
Muhr, A.H. 1983. The influence of polysaccharides on ice formation in sucrose solutions. Ph.D. Thesis. Nottingham University.
Muhr, A.H. and Blanshard, J.M.V 1982. Diffusion in gels. Polymer. 23:1012–1026.
Muhr, A.H. and Blanshard, J.M.V 1986. Effect of polysaccharide stabilizers on the rate of growth of ice. J. Food Technol. 21:683–710.
Muhr, A.H., Blanshard, J.M.V., and Sheard, S. 1986. Effects of polysaccharide stabilizers on the nucleation of ice. J. Food Technol. 21:587–604.
Noguchi, S. 1974. The control of denaturation of fish muscle proteins during frozen storage. D.Sc. Thesis. Sophia University, Tokyo, Japan.
Obuchi, K., Iwahashi, H., Kaul, S.C., Ishimura, M, Fujii, S., Satoh, A., and Komatsu, Y. 1993. In High Pressure Bioscience and Food Science. (Hayashi, R., ed.) pp. 147–156, San-E Publishing, Kyoto, Japan.
Park, J.W. and Lanier, T.C. 1987. Combined effects of phosphates and sugar or polyol on protein stabilization of fish myofibrils. J. Food Sci. 52:1509–1513.
Park, J.W., Lanier, T.C., and Green, D.P. 1988. Cryoprotective effects of sugar, polyols, and/or phosphates on Alaska pollock surimi. J. Food Sci. 53:1–3.
Park, J.W., Lanier, T.C., Hamann, D.D., and Keeton, J.T. 1987. Use of cryoprotectants to stabilize functional properties of prerigor salted beef during frozen storage. J. Food Sci. 52:537–542.
Park, J.W., Lanier, T.C., and Pilkington, D.H. 1993. Cryostabilization of functional properties of pre-rigor and post-rigor beef by dextrose polymer and/or phosphates. J. Food Sci. 58:467–472.
Park, J.W., Lanier, T.C., Swaisgood, H.E., Hamann, D.D., and Keeton, J.T. 1987. Effects of cryoprotectants in minimizing physicochemical changes of bovine natural actomyosin during frozen storage. J. Food Biochem. 11:143–161.
Parker, R. and Ring, S.G. 1995. A theoretical analysis of diffusion-controlled reactions in frozen solutions. Cryo-Lett. 16:197–208.
Pauling, L. 1953. General Chemistry, 2d ed. pp. 344–347, W.H. Freeman, San Francisco.
Payne, S.R. and Young, O.A. 1995. Effects of pre-slaughter administration of antifreeze proteins on frozen meat quality. Meat Sci. 41:147–155.
Pittz, E.P. and Timasheff, S.N. 1978. Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8. Biochem. 17:615–623.
Privalov, P.L. 1990. Cold denaturation of proteins. Crit. Rev. Biochem. Mol. Biol. 25:281–305.
Rawn, J.D. 1989. Biochemistry. Neil Patterson Publishers, Burlington, N.C. Roos, Y.H. 1995. Phase Transitions in Foods. Academic Press, San Diego.
Roos, Y.H. and Karel, M. 1991. Water and molecular weight effects on glass transitions in amorphous carbohydrates and carbohydrate solutions. J. Food Sci. 56:1676–1681.
Rosen, M.J. 1978. Surfactants and interfacial phenomena. John Wiley & Sons, New York.
Rubinsky, B., Arav, A., and DeVries, A.L. 1992. The cryoprotective effect of antifreeze glycopeptides from Antarctic fishes. Cryobiol. 29:69–79.
Saeki, H. 1996. Gel-forming ability and cryostability of frozen surimi processed with CaCl2-washing. Fish. Sci. 62:252–256.
Samejima, K., Oka, Y, Yamamoto, K., Asghar, A., and Yasui, T. 1988. Effects of SH groups, ∈NH2 groups, ATP, and myosin subfragments on heat-induced gelling of cardiac myosin and comparison with skeletal myosin and actomyosin gelling capacity. Agric. Biol. Chem. 52:63.
Schlesinger, M.J., Ashbumer, M., and Tisseries, A. (eds.) 1982. Heat Shock from Bacteria to Man. CSH, New York.
Schmitt, J.M., Sieg, F., and Hincha, D.K. 1994. Noncolligative cryoprotection by proteins. Cryobiol. 31:560.
Sharp, A. and Offer, G. 1992. The mechanism of formation of gels from myosin molecules. J. Sci. Food Agric. 58:63–73.
Shenouda, S.Y. 1980. Theories of protein denaturation during frozen storage of fish flesh. Adv. Food Res. 26:275–311.
Shimizu, Y. and Fujita, T. 1985. Stability of unwashed and washed fish mince during frozen storage. Bull. Jpn. Soc. Sci. Fish. 51:1187–1194.
Slade, L. and Levine, H. 1995. Glass transitions and water-food structure interactions. Adv. Food Nutr. Res. 38:103–269.
Slade, L., Levine, H., Ievolella, J., and Wang, M. 1993. The glassy state phenomenon in applications for the food industry: application of the food polymer science approach to structure-function relationships of sucrose in cookie and cracker systems. J. Sci. Food Agric. 63:133–176.
Stadelman, W.J., Olson, VM., Shemwell, G.A., and Pasch, S. 1988. Nutritional value of eggs. In Egg and Poultry-Meat. (Morton, I.D., Scott, R., Watson, D.H., and Lewis, M., eds.) pp. 20–39, Ellis Horwood, Chichester, England.
Storey, K.B. 1990. Life in a frozen state: adaptive strategies for natural freeze tolerance in amphibians and reptiles. Am. J. Physiol. 258:R559–R568.
Storey, K.B., Baust, J.G., and Wolanczyk, J.P. 1992. Biochemical modification of plasma ice nucleating activity in a freeze-tolerant frog. Cryobiol. 29:374–384.
Timasheff, S.N. and Arakawa, T. 1989. Stabilization of protein structure by solvents. In Protein Structure: A Practical Approach. (Creighton, T.E., ed.) pp. 331–346, IRL Press, Oxford.
Tinoco, I., Sauer, K., and Wang, J.C. 1985. Physical Chemistry: Principles and Applications in Biological Sciences, 2d ed. Prentice-Hall, Englewood Cliffs, N.J.
Treloar, L.R.G. 1970. Introduction to Polymer Science. Springer-Verlag, New York.
van Holde, K.E. 1985. Physical Biochemistry, 2d ed. Prentice-Hall, Englewood Cliffs, N.J.
Volkin, D.B. and Klibanov, A.M. 1989. Minimizing protein inactivation. In Protein Function: A Practical Approach. (Creighton, T.E., ed.) pp. 1–23, IRL Press, New York.
Wagner, J.R. and Añón, M.C. 1985. Effect of freezing rate on the denaturation of myofibrillar proteins. J. Food Technol. 20:735–744.
Warren, C.J., Mueller, G.M., and McKown, R.L. 1992. Ice crystal growth suppression polypeptides and methods of preparation. U.S. patent no. 5, 118,792.
Wasylyk, J.M., Tice, A.R., and Baust, J.G. 1988. Partial glass formation: a novel mechanism of insect cryoprotection. Cryobiol. 25:451–458.
Watanabe, T., Kitabatake, N., and Doi, E. 1988. Protective effects of non-ionic surfactants against denaturation of rabbit skeletal myosin by freezing and thawing. Agric. Biol. Chem., 25(10):2517–2523.
Wessels, J.P.H., Simmonds, C.K., Seaman, P.D., and Avery, L.W.J. 1981. Annual Report, Fishing Industry Research Institute, Capetown, South Africa.
Wyman, J. 1964. Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19:223–286.
Yamamoto, K. 1990. Electron microscopy of thermal aggregation of myosin. J. Biochem. 108(6):896–898.
Zachariassen, K.E. 1985. Physiology of cold tolerance in insects. Physiol. Rev. 65:799–832.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
MacDonald, G.A., Lanier, T.C. (1997). Cryoprotectants for Improving Frozen-Food Quality. In: Erickson, M.C., Hung, YC. (eds) Quality in Frozen Food. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5975-7_11
Download citation
DOI: https://doi.org/10.1007/978-1-4615-5975-7_11
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7738-2
Online ISBN: 978-1-4615-5975-7
eBook Packages: Springer Book Archive
