Abstract
There is a constant and increasing demand for high-quality protein foods for an ever-growing world population. Food scientists are interested not only in the chemical principles underlying protein structures and mechanisms but applications of the knowledge in exploring the unique characteristics of proteins that are relevant in complex food systems. The basic chemistry is always related to the functionality of the protein. Thus, the chemistry of muscle contraction is related to rigor mortis and the postmortem tenderness of meat. The chemical structure of collagen and the unfolding and refolding of the helical chains help to explain the formation of gelatin gel. The understanding of protein chemistry would provide new ideas that challenge food scientists and technologists to improve existing and formulate new food products.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Adachi M, Takenaka Y, Gidamis AB, Mikami B, Utsumi S (2001) Crystal structure of soybean proglycinin A1aB1b homotrimer. J Mol Biol 305:291–305
Adachi M, Kanamori J, Masuda T, Yagasaki K, Kitamura K, Mikami B, Utsumi S (2003) Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer. Proc Natl Acad Sci U S A 100:7395–7400
Asghar A, Henrickson RL (1982) Chemical, biochemical, functional, and nutritional chracteristics of collagen in food systems. Adv Food Res 28:231–372
Bell BM, Daniels DGH, Fisher N (1977) Physical aspects of the improvement of dough by fat. Food Chem 2:57–70
Belton PS (1999) On the elasticity of wheat gluten. J Cereal Sci 29:103–107
Belton PS (2005) New approaches to study the molecular basis of the mechanical properties of gluten. J Cereal Sci 41:203–211
Bent DV, Hayon E (1975) Excited state chemistry of aromatic amino acids and related peptides. II. Phenylalanine. J Am Chem Soc 97:2606–2611
Birktoft JJ, Blow DM (1972) Structure of crystalline α-chymotrypsin. J Mol Biol 68:187–240
Braams R (1966) Rate constants of hydrated electron reactions with amino acids. Radiat Res 27:319–329
Cherry JP, MeWatter KH (1981) Whippability and aeration. In: Cherry JP (ed) Protein functionality in foods. ACS symposium series, vol 147. American Chemical Society, Washington, D.C.
Clark KA, McElhinny AS, Beckerle MC, Gregorio CC (2002) Striated muscle cytoarchitecture: an intricate web of form and function. Annu Rev Cell Dev Biol 18:637–706
Cooke R (2004) The sliding filament model: 1972-2004. J Gen Physiol 123:643–656
Daigleish DG (1979) Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin. J Dairy Res 46:653–661
Dizdaroglu M, Simic MG (1985) Radiation-induced crosslinks between thymine and phenylalanine. Int J Radiat Biol 47:63–69
Don C, Lichtendonk WJ, Plijter JJ, Hamer RJ (2003) Understanding the link between GMP and dough from glutenin particles in flour towards developed dough. J Cereal Sci 38:157–165
D’Ovidio R, Masci S (2004) The low-molecular-weight subunits of wheat gluten. J Cereal Sci 39:321–339
England D (1975) Protein hydration – its role in stabilizing the helix conformation of the protein. In: Duckworth RB (ed) Water relations of foods. Academic, New York
Eyre DR (1980) Collagen: molecular diversity in the body’s protein scaffold. Science 207:1315–1322
Faraggi M, Bettelheim A (1977) The reaction of the hydrated electron with amino acids, peptides, and proteins in aqueous solution III. Histidyl peptides. Radiat Res 71:311–324
Farrell HM Jr, Jimenez-Flores R, Bleck GT, Brown EM, Butler JE, Creamer LK, Hicks CL, Hollar CM, Ng-Kwai-Hang KF, Swaisgood JE (2004) Nomenclature of the proteins of cow’s milk − Sixth Edition. J Dairy Sci 87:1641–1674
Finnie SM, Jeannotte R, Faubron JM (2009) Quantitative characterization of polar lipids from wheat whole meal, flour, and starch. Cereal Chem 86:637–645
Frazer DB, MacRae TP (1973) Conformation in fibrous proteins and related synthetic polypeptides. Academic, New York, p 347
Frazier PJ, Brimblecombe FA, Daniels NWR, Eggitt PWR (1977) The effect of lipoxygenase action on the mechanical development of doughs from fat-extracted and reconstituted wheat flour. J Sci Food Agric 28:247–254
Fox PF, Hoynes MCT (1975) Heat stability of milk: influence of colloidal calcium phosphate and β-lactoglobulin. J Dairy Res 42:427–435
Fujimoto D, Moriguchi L, Ishida T, Hayashi H (1978) The structure of pyridinoline, a collagen crosslink. Biochem Biophys Res Commun 84:52–57
Geeves MA, Holmes KC (2005) The molecular mechanism of muscle contraction. Adv Protein Chem 71:161–194
Gennari G, Gauzzo G, Jori G (1974) Further studies on the crystal-crystal-violet-sensitized photooxidation of cysteine to cysteic acid. Photochem Photobiol 20:497–500
Gianibelli MC, Larroque OR, MacRitchie F, Wrigley CW (2001) Biochemical, genetic, and molecular characterization of wheat glutenin and its component subunits. Cereal Chem 78:635–646
Goll DE, Otsuka Y, Nagainis PA, Shannon JD, Sathe SK, Muguruma M (1983) Role of muscle proteinases in maintenance of muscle integrity and mass. J Food Biochem 7:137–177
Guo S-T, Ono T (2005) The role of composition and content of protein particles in soymilk on tofu curding by glucono-δ-lactone or calcium sulfate. J Food Sci 70:C252–C262
Hamer RJ, van Vliet T (2000) Understanding the structure and properties of gluten: an overview. In: Shewry PR, Tatham AS (eds) Wheat Gluten proceedings of the 7th international workshop, Gluten 2000. Royal Society of Chemistry 2000, pp 125–131
Harrington WF, Venkateswara R (1970) Collagen structure in solution. I. Kinetics of helix regeneration in single-chain gelations. Biochemistry 9:3714–3724
Hegarty GR, Bratzler LJ, Pearson AM (1963) Studies on the emulsifying properties of some intracellular beef muscle proteins. J Food Sci 28:663–668
Hermansson AM (1979) Aggregation and denaturation involved in gel formation. In: Pour-El A (ed) Functionalituy and protein structure. ACS symposium series, vol 92. American Chemical Society, Washington, D.C.
Hermansson AM (1986) Soy protein gelation. J Am Oil Chem Soc 63:658–666
Hibberd MG (1986) Relationships between chemical and mechanical events during muscular contraction. Ann Rev Biophys Chem 15:119–161
Holmes KC, Popp D, Gebhard W, Kabsch W (1990) Atomic model of the actin filament. Nature 347:44–49
Holt C, Wahlgren NM, Drakenerg T (1996) Ability of a β-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters. Biochem J 314:1035–1039
Horne DS (1998) Casein interactions: casting light on the black boxes, the structure in dairy products. Int Dairy J 8:171–177
Huff-Lonergan E, Lonergan SM (2005) Mechanisms of water-holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Sci 71:194–204
Huff-Lonergan E, Mitsuhashi T, Beekman DD, Parrish FC, Dennis GO, Robson RM (1996) Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J Am Sci 74:993–1008
Hurrell RF, Carpenter KJ (1976) Mechanisms of heat damage in proteins. 7. The significance of lysine-containing isopeptides and of lanthionine in heated proteins. Br J Nutr 35:383–395
Johansson E, Malik AH, Hussain A, Rasheed F, Newson WR, Plivelic T, Hedenqvist MS, Gallstedt M, Kuktaite R (2013) Wheat gluten polymer structures: the impact of genotype, environment, and processing on their functionality in various applications. Cereal Chem 90:367–376
Karam LR, Dizdaroglu M, Simic MG (1984) OH radical-induced products of tyrosine peptides. Int J Radiat Biol 46:715–724
Kasarda DD (1999) Glutenin polymers: the in vitro to in vivo transition. Cereal Foods World 44:566–571
Kasada DD, Bernardin JE, Nimmo CC (1976) Wheat proteins. Adv Cereal Sci Technol 1:158–236
Kemp CM, Sensky PL, Bardsley RG, Buttery PJ, Parr T (2010) Tenderness – an enzymatic view. Meat Sci 84:248–256
Kohyama K, Nishinari K (1993) Rheological studies on the gelation process of soybeans 7S and 11S proteins in the presence of glucono-δ-lactone. J Agric Food Chem 41:8–14
Kohyama K, Sano Y, Doi E (1995) Rheological characteristics and gelation mechanism of tofu (soybean curd). J Agric Food Chem 43:1808–1812
Lakemond CMM, de Jongh HHJ, Hessing M, Gruppen H, Voragen AGJ (2000) Soy glycinin: influence of pH and ionic strength on solubility and molecular structure at ambient temperatures. J Agric Food Chem 48:1985–1990
Levitt M, Chothia C (1976) Structural patterns in globular proteins. Nature 261:552–538
Liardon R, Ledermann S (1986) Racemization kinetics of free and protein-bound amino acids under moderate alkaline treatment. J Agric Food Chem 34:557–565
Lindsay MP, Skerritt JH (1999) The glutenin macropolymer of wheat flour doughs: structure-function perspectives. Trends Food Sci Technol 10:247–253
Lindsay MP, Tamas L, Appels R, Skerritt JH (2000) Direct evidence that the number and location of cysteine residues affect glutenin polymer structure. J Cereal Sci 31:321–333
Lucey JA (2002) Formation and physical properties of milk protein gels. J Dairy Sci 85:281–294
Maruyama N, Adachi M, Takahashi K, Yagasaki K, Kohno M, Takenaka Y, Okuda E, Nakagawa S, Mikami B, Utsumi S (2001) Crystal structures of recombinant and native soybean β-conglycinin β homotrimers. Eur J Biochem 268:3595–3604
Maruyama N, Salleh MRM, Takanashi K, Yagasaki K, Goto H, Hontami N, Nakagawa S, Utsumi S (2002) The effect of the N-linked glycans on structural features and physicochemical functions of soybean b-conglycinin homotrimers. JAOCS 79:139–144
McMahon DJ, Oommen BS (2008) Supramolecular structure of the casein micelle. J Dairy Sci 91:1709–1721
Melander W, Horvath C (1977) Salt effects on hydrophobic interaction in precipitation and chromatography of proteins: an interpretation of the lyotropic series. Arch Biochem Biophys 183:200–215
Mo X, Zhong Z, Wang D, Sun X (2006) Soybean glycinin subunits: characterization of physicochemical and adhesion properties. J Agric Food Chem 54:7589–7593
Morr CV (1990) Current status of soy protein functionality in food systems. JAOCS 67:265–271
Otterbein LR, Graceffa P, Dominguez R (2001) The crystal structure of uncomplexed actin in the ADP state. Science 293:708–711
Papiz MZ, Sawyer L, Eliopoulos EE, North ACT, Findley JBC, Siraprasadarao R, Jone TA, Newcomer ME, Kraulis PJ (1986) The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324:383–385
Pareyt B, Finnie SM, Putreys JA, Delcour JA (2011) Lipids in bread making: sources, interactions, and impact on bread quality. J Cereal Sci 54:266–279
Payens TAJ (1979) Casein micelles: the colloid-chemical approach. J Dairy Res 46:291–306
Pearce KL, Rosenvoid K, Andersen HJ, Hopkins DL (2011) Water distribution and mobility in meat during the conversion of muscle to meat and aging and the impacts on fresh meat quality attributes – a review. Meat Sci 89:111–124
Philips MC (1981) Protein conformation at liquid interfaces and its role in stabilizing emulsions and foams. Food Technol 35(1):50–57
Pomeranz Y, Chung OK (1978) Interaction of lipids with proteins and carbohydrates in breadmaking. J Am Oil Chem Soc 55:285–289
Privalov PL, Khechinashvilli NN (1974) A thermodynamic approach to the problems of stabilization of globular protein structure: a calorimetric study. J Mol Biol 86:665–684
Qi PF, Wei YM, Yue YW, Yan ZH, Zheng YL (2006) Biochemical and molecular characterization of gliadins. Mol Biol 40:713–723
Rao PS, Hayon E (1975) Reaction of hydroxyl radicals with oligopeptides in aqueous solutions. A pulse radiolysis study. J Phys Chem 79:109–115
Rayment I, Rypniewski WR, Schmidt-Base K, Smith R, Tomchick DR, Benning MW, Winkelmann DA, Wesenberg G, Holden HM (1993) Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261:50–58
Rayment I, Holden HM (1994) The three-dimensional structure of a molecular motor. TIBS 19:129–134
Renkema JMS, van Vliet T (2002) Heat-induced gel formation by soy proteins at neutral pH. J Agric Food Chem 50:1569–1573
Richardson JS (1976) Handedness of crossover connections in β sheets. Proc Natl Acad Sci U S A 73:2619–2623
Richardson JS (1977) β-Sheet topology and the relatedness of proteins. Nature 268:495–500
Saito I, Matsuura T (1977) Peroxidic intermediates in photosensitized oxygenation of tryptophan derivatives. Acc Chem Res 10:346–352
Saito I, Matsuura T (1985) Chemical aspects of UV-induced cross-linking of proteins to nucleic aicd. Photoreaction with lysine and tryptophan. Acc Chem Res 18:134–141
Saio K, Watanabe T (1978) Differences in functional properties of 7S and 11S soybean proteins. J. Texture Stud 9:135–157
Samejima KJ, Ishioroshi M, Yasui T (1981) Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J Food Sci 46:1412–1418
Schaich KM (1980) Free radical initiation in proteins and amino acids by ionizing and ultraviolet. CRC Crit Rev Food Sci Nutr 13:89–129
Schaich KM (1980) Free radical initiation in proteins and amino acids by ionizing and ultraviolent radiations and lipid oxidation – part II: ultraviolet radiation and photolysis. CRC Crit Rev Food Sci Nutr 13:131–159
Schaich KM (1980) Free radical initiation in protein and amino acids by ionizing and ultraviolet radiation and lipid oxidation – part III: free radical transfer from oxidizing lipids. CRC Crit Rev Food Sci Nutr 13:189–244
Schmidt DG (1980) Colloidal aspects of casein. Neth Milk Dairy J 34:42–
Schmidt DG (1981) Gelation and coagulation. In: Cherry JP (ed) Protein functionality in foods. ACS symposium series, vol 147. American Chemical Society, Washington, D.C.
Schmidt DG (1982) Association of caseins and casein micelle structure. In: Fox PF (ed) Developments in dairy chemistry. Applied Science Publishers, Ltd., London/New York
Shewry PR, Popineau Y, Lafiandra D, Belton P (2001) Wheat glutenin subunits and dough elasticity: findings of the EUROWHEAT project. Trends Food Sci Technol 11:433–441
Singh H (2004) Heat stability of milk. Int J Dairy Technol 57:111–119
Slattery CW, Evard R (1973) A model for the formation and structure of casein micelles from subunits of variable composition. Biochim Biophys Acta 317:529–538
Squire JM, Al-Khayat HA, Knup C, Luther PK (2005) Molecular architecture in muscle contractile assemblies. Adv Protein Chem 71:17–87
Sroan BS, Bean SR, MacRitche F (2009) Mechanism of gas cell stabilization in bread making. I. The primary gluten-starch matrix. J Cereal Sci 49:32–40
Tamas L, Gras PW, Solomon RG, Morell MK, Appels R, Bekes F (2002) Chain extension and termination as a function of cysteine content and the length of the central repetitive domain in storage proteins. J Cereal Sci 36:313–325
Tatham AS, Shewy PR (1985) The conformation of wheat gluten proteins. The secondary structures and thermal stabilities of α, β, and γ-gliadins. J Cereal Sci 3:103–113
Thomson NH, Miles MJ, Popineau Y, Harris J, Shewry P, Tatham AS (1999) Small angle X-ray scattering of wheat seed storage proteins α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin. Biochim Biophys Acta Protein Struct Mol Enzymol 1430:359–366
Utsumi S, Maruyama N, Satoh R, Adachi M (2002) Structure-function relationships of soybean proteins revealed by using recombinant systems. Enzyme Microb Technol 30:284–288
Wall JS (1979) The role of wheat proteins in determining baking quality. In: Laidman DL, Jones RGW (eds) Recent advances in the biochemistry of cereals. Academic, New York
Watanabe A, Yokomizo K, Eliasson A-C (2003) Effect of physical states of nonpolar lipids in rheology, ultracentrifugation, and microstructure of wheat flour dough. Cereal Chem 80:281–284
Whitaker JR, Feeney RE (1983) Chemical and physical modification of proteins by the hydroxide ion. CRC Crit Rev Food Sci Nutr 19:173–212
Wikening VG, Lai M, Arends M, Armstrong DA (1968) The cobalt-60 γ-radiolysis of cysteine in deaerated aqueous solutions at pH values between 5 and 6. J Phys Chem 72:185–190
de Wit JN (2009) Thermal behavior of bovine b-lactoglobulin at temperatures up to 150 °C, a review. Trends Food Sci Technol 20:27–34
Wolf WJ, Rackis JJ, Smith AK, Sasame HA, Babcock GE (1958) Behavior of the 11S protein of soybeans in acid solutions. I. Effects of pH, ionic strength and time in ultracentrifugal and optical rotatory properties. J Am Chem Soc 80:5730–5735
Yamamoto O (1972) Radiation-induced binding of methionine with serum albumin, tryptophan or phenylalanine in aqueous solution. Int J Radiat Phys Chem 4:335–345
Yamamoto O (1975) Radiation-induced binding of OH-substituted aromatic amino acids, tyrosine and dopa, mutually and with albumin in aqueous solution. Radiat Res 61:251–260
Yamauchi F, Yamagishi T, Iwabuchi S (1991) Molecular understanding of heat-induced phenomena of soybean protein. Food Rev Intl 7:283–322
Yang SF, Ku HS, Pratt HK (1967) Photochemical production of ethylene from methionine and its analogues in the presence of flavin mononucleotide. J Biol Chem 242:5274–5280
Yong SH, Karel M (1978) Reaction of histidine with methyl linoleate: characterization of the histidine degradation products. J Am Oil Chem Soc 55:352–357
Yong SH, Lau S, Hsieh Y, Karel M (1980) Degradation products of L-tryptophan reacted with peroxidizing methyl linoleate. In: Simic MG, Karel M (eds) Autoxidation in food and biological systems. Phenum Press, New York
Zheng H-G, Yang X-Q, Ahmad I, Min W, Zhu J-H, Yuan D-B (2009) Soybean β-conglycinin constituent subunits: isolation, solubility and amino acid composition. Food Res Int 42:998–1003
Ziegler GR, Acton JC (1984) Mechanisms of gas formation by proteins of muscle tissue. Food Technol 38(5):77–82
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG
About this chapter
Cite this chapter
Wong, D.W.S. (2018). Proteins. In: Mechanism and Theory in Food Chemistry, Second Edition. Springer, Cham. https://doi.org/10.1007/978-3-319-50766-8_2
Download citation
DOI: https://doi.org/10.1007/978-3-319-50766-8_2
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-50765-1
Online ISBN: 978-3-319-50766-8
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)