Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page i — #1 Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page ii — #2 Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page iii — #3 Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page iv — #4 Contents Preface vii Editors ix Contributors xi Chapter Introduction to Food Chemistry Owen R Fennema, Srinivasan Damodaran, and Kirk L Parkin Part I Major Food Components 15 Chapter Water and Ice David S Reid and Owen R Fennema 17 Chapter Carbohydrates James N BeMiller and Kerry C Huber 83 Chapter Lipids 155 D Julian McClements and Eric A Decker Chapter Amino Acids, Peptides, and Proteins 217 Srinivasan Damodaran Chapter Enzymes 331 Kirk L Parkin Part II Minor Food Components 437 Chapter Vitamins 439 Jesse F Gregory III Chapter Minerals 523 Dennis D Miller Chapter Colorants 571 Steven J Schwartz, Joachim H von Elbe, and M Monica Giusti Chapter 10 Flavors 639 Robert C Lindsay Chapter 11 Food Additives 689 Robert C Lindsay Chapter 12 Bioactive Substances: Nutraceuticals and Toxicants 751 Chi-Tang Ho, Mohamed M Rafi, and Geetha Ghai Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page v — #5 Part III Food Systems 781 Chapter 13 Dispersed Systems: Basic Considerations 783 Pieter Walstra and Ton van Vliet Chapter 14 Physical and Chemical Interactions of Components in Food Systems 849 Zdzisław E Sikorski, Jan Pokorny, and Srinivasan Damodaran Chapter 15 Characteristics of Milk 885 Harold E Swaisgood Chapter 16 Physiology and Chemistry of Edible Muscle Tissues 923 Gale Strasburg, Youling L Xiong, and Wen Chiang Chapter 17 Postharvest Physiology of Edible Plant Tissues 975 Jeffrey K Brecht, Mark A Ritenour, Norman F Haard, and Grady W Chism Chapter 18 Impact of Biotechnology on Food Supply and Quality 1051 Martina Newell-McGloughlin Part IV Appendices 1103 Appendix A: International System of Units (SI): The Modernized Metric System 1105 Appendix B: Conversion Factors (Non-SI Units to SI Units) 1109 Appendix C: Greek Alphabet 1111 Appendix D: Calculating Relative Polarities of Compounds Using the Fragmental Constant Approach to Predict log P Values 1113 Index 1119 Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page vi — #6 Preface Another decade has past since the publication of the third edition of Food Chemistry, and given the rapid progress in biological research, an update is warranted However, this fourth edition marks several transitions Perhaps, most important is the recognition of Owen Fennema’s contributions to this text and to the field of food chemistry in general His timely introduction of the first edition of Food Chemistry over 30 years ago, in 1976, filled a long-standing void of a comprehensive text that could serve as both an instructional tool and a desk reference for professionals To us, it seems only fitting to now recognize this text as Fennema’s Food Chemistry, as a tribute to his long-lasting contributions to the field through the three pervious editions of this text Since professor Fennema’s “retirement” in 1996, he has remained professionally active, while engaging in more earthly pursuits of global travel, craftsmanship with wood, and stained glass artisanship While he has been active with the planning of this edition as a coeditor, he entrusted us to assume most of the day-to-day editorial responsibilities We are humbled, and needless to say that given the high standards set by professor Fennema in the previous editions, we are cognizant of the lofty expectations that likely exist for the fourth edition Professor Fennema is a hard act to follow, and we hope our effort will not disappoint This edition not only marks a transition in editorial responsibilities, but also in contributing authors, as several former authors have retired or are approaching retirement New (co)contributors appear for chapters on “Water and Ice,” “Carbohydrates,” “Lipids,” “Enzymes,” and “Colorants.” Some chapters have also evolved in terms of focus and include “Postmortem Physiology of Edible Muscle Tissues,” “Postharvest Physiology of Edible Plant Tissues,” “Bioactive Substances: Nutraceuticals and Toxicants” (formerly “Toxic Substances”), and “Physical and Chemical Interactions of Components in Food Systems” (formerly “Summary: Integrative Concepts”), all with new (co)contributors An added chapter appears on “Impact of Biotechnology on Food Supply and Quality.” We are indebted to the contributing authors of this volume for their patience and professionalism in dealing with new editors and for paying serious attention to the needs for chapter updates It is hoped that both new and faithful readers of this text will find it useful, and be constructive by directing any comments regarding the content of this book (as well as identifying inevitable printing errors) to our attention Srinivasan Damodaran and Kirk Parkin Madison, Wisconsin, USA Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page vii — #7 Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page viii — #8 Editors Owen R Fennema is a professor of food chemistry in the Department of Food Science at the University of Wisconsin-Madison He is coauthor of the books Low Temperature Foods and Living Matter (with William D Powrie and Elmer H Marth) and Principles of Food Science, Part II: Physical Principles of Food Preservation (with Marcus Karel and Daryl B Lund), both titles published by Marcel Dekker, Inc., and the author or coauthor of over 175 professional papers that reflect his research interests in food chemistry, low-temperature preservation of food and biological matter, the characteristics of water and ice, edible films and coatings, and lipid–fiber interactions A consulting editor for the Food Science and Technology series (Marcel Dekker, Inc.), he is a fellow of the Institute of Food Technologists and of the Agriculture and Food Chemistry Division of the American Chemical Society, and a member of the American Institute of Nutrition, among other organizations Dr Fennema received the BS degree (1950) in agriculture from Kansas State University, Manhattan, the MS degree (1951) in dairy science, and PhD degree (1960) in food science and biochemistry from the University of Wisconsin-Madison Sinivasan Damodaran is a professor of food chemistry and chair of the Department of Food Science at the University of Wisconsin-Madison He is editor of the book Food Proteins and Lipids (Plenum Press) and co-editor of the book Food Proteins and Their Applications (with Alain Paraf) (Marcel Dekker, Inc.) and the author/coauthor of patents and over 125 professional papers in his research areas, which include protein chemistry, enzymology, surface and colloidal science, process technologies, and industrial biodegradable polymers He is a fellow of the Agriculture and Food Chemistry Division of the American Chemical Society and a member of the Institute of Food Science and the American Oil Chemists Society He is on the editorial board of Food Biophysics journal Dr Srinivasan Damodaran received his BSc degree (1971) in chemistry from University of Madras, Madras, India, the MSc degree (1975) in food technology from Mysore University, Mysore, India, and PhD degree (1981) from Cornell University, Ithaca, New York Kirk L Parkin is currently professor in the Department of Food Science of the University of Wisconsin (Madison, Wisconsin, USA), where he has been on the faculty for over 21 years He has been the College of Agricultural and Life Sciences Fritz Friday Chair of Vegetable Processing Research since 1998, and was elected Fellow of the Agricultural and Food Chemistry Division of the American Chemical Society in 2003 Dr Parkin’s research and teaching interests revolve around food chemistry and biochemistry, with about 80 refereed journal publications in the areas of marine food biochemistry, postharvest physiology and processing of fruit and vegetable products, fundamental and applied enzymology, and most recently in the area of characterizing health-promoting and bioactive phytochemicals from foods of botanical origin At UW-Madison, Dr Parkin has been an instructor for undergraduate courses in Food Chemistry, Discovery Food Chemistry Laboratory, as well as for graduate courses in Food Enzymes and Lipids He has supervised the completion of 10 Ph.D and 17 M.S graduate degree programs, and serves as associate editor for Journal of Food Science, and on the editorial board of Food Research International, Food Biochemistry, and the Journal of Food Processing and Preservation Parkin: “dk9272_c000” — 2007/7/28 — 11:20 — page ix — #9 Index 1131 Iodine, 544–545, 558 deficiency disorders, 545 Ion-exchange adsorption (IEA) process, 910–911 Ionic strength, 268–269 Ionizable groups in proteins, 225 Ionizing radiation, 194, 308 β-Ionone, 681 β-Ionone ring, 454, 594 Ions and ionic groups interactions of water with, 33–34 Iron, 542–544, 555–558 Irradiation, 960–961 γ –Irradiation, 961 Isinglass, 733 Isoamaranthin, 615 l-Isoascorbic acid, 467 Isobetanin, 615 Isodesmosine, 220, 306 Isoelectric pH, 243 Isoelectric points, 223 Isoflavones, 611, 758, 1085 Isoforms, 334 Isohumulone, 646 Isoionic point, 243 Isomalt® , 373, 725 Isomaltulose synthase, 373 Isomerization, 87 cis/trans Isomerization, 598–599 trans → cis Isomerization, 233 Isopeptides, 308 Isoprene, 596 Isoprenoid, 454, 664 Isothiocyanates, 422, 762–763 Isovaleric acid, 674 J Junction zones, 113 K Kaschin-Beck disease, 546 Kcat , 348, 349 Kelvin Equation, 796 Keratin, 306, 312 Keshan disease, 546 Ketohexoses, 87 Ketosamine, 313 Ketoses, 87 Kinetics, of enzyme reactions, 347 KM , 348, 349 Knockout mice, 753 “Knock-out”, 1090 Kokumi substances, 653–654 Kosmotropes, 258 KS , 348 Kunitz-type protease inhibitors, 299 Kynurenine, 311, 312 L Labeling, of foods, 1097 Laccases, 409 Parkin: α-Lactalbumin, 901, 902 Lactase, 104, 372 Lactic acid, 691 Lactic acid–ethanol fermentations, 667–670 Lactide, 691 Lactitol, 723 β-Lactoglobulin, 238, 240, 267, 899–901 Lactoperoxidase, 415 Lactose, 720, 907–908 intolerance, 104 tolerance, 915 use, in formulated foods, 911 Lanthionine, 306 Laplace pressure, 795 Laplace principle, 278 Lauric arginate, 710 LDL-cholesterol, 209 Lead, 547, 548 Least concentration endpoint (LCE), 288 Leavening acids, 694 Leaving group, 341 Lectins, 299, 303 Legumins, 277 Lenthionine, 660 Lentinic acid, 660 Leucoanthocyanidin, 612 Leucotriene synthesis, 675 Lewis acid, 526–527 Lewis base, 526–527 Ligands, 526–527 Light meromyosin, 942 Light-induced degradation, 490 Lignans, 1080 Lignification, 986 Lignin, 149 Limit dextrin, 130, 366 Limiting amino acids, 297 Limonin, 647, 648 Linamarin, 545 Linear plots, 354 Linear rates, 352 Linear transformation, 353 Lineweaver–Burke, 353 Linoleic acid, 663 β-oxidation, 663 α-Linolenic acid, 1081 Lipase, 186, 341, 1027 Lipid acyl hydrolase, 420 Lipid content and composition, 925–926 Lipid globules, 851–852, 853–854 Lipid hydroperoxides (LOOH), 315 Lipid metabolism, 1026–1028 Lipid oxidation, 186 antioxidants, 198–206 free radicals, control of, 198–204 interaction, 205–206 oxidation intermediates, 205 physical location, 206 decomposition products, formation, 195–198 cholesterol oxidation, 198 fatty acid, additional reaction, 198 β-scission reaction, 196–198 influencing factors, 206–207 “dk9272_c023” — 2007/7/20 — 21:28 — page 1131 — #13 Index 1132 Lipid oxidation (continued) measurement, 207–209 primary products, 207–208 secondary products, 208–209 sensory analysis, 207 mechanisms, 187–190 and pigment oxidation, 579 prooxidants, 190–195 control, 204 and free radicals formation, 194 and hydroperoxides decomposition, 194–195 and lipid hydroperoxides formation, 191–194 Lipid peroxidation, 563 Lipid-phase transitions physiochemical mechanism, 171 crystal growth, 175 nucleation, 172–175 postcrystallization, 176 supercooling, 172 Lipids, 314–315, 1012–1015 components, 157 acylglycerols, 159–162 fatty acids, 157 miscellaneous lipids, 164 phospholipids, 162–163 sphingolipids, 163 sterols, 163–164 waxes, 164 food lipids and health, 209 functionality of triacylglycerols in foods, 184–186 hydrolytic rancidity, 186 lipid oxidative, 186 antioxidants, 198–206 decomposition products, formation, 195–198 measurement, 207–209 mechanisms, 187–190 prooxidants, 190–195 rates, factors influence, 206–207 physicochemical properties, 164 crystal structure, 176 food lipids, crystallization and melting of, 169–171 lipid-phase transitions, 171 of triacylglycerols, 166–169 processing, 178 reactions, during food processingv 854 Lipoprotein lipasev 422 Lipoxygenase, 192, 303, 346, 675, 735, 736, 1027 and cartenoid degradation, 597 Lipoxygenase-derived flavors, 661–662 Liquefaction, 130, 367 Liquid dispersions aggregation, 807–808 description, 805–806 sedimentation, 806–807 Liquid structures, in pure water systems, 26–27 Litesse, 729 LMW glutenins, 293 Locust bean gums (LBGs), 107, 138, 736 Long flow, 113 Loops, 271 Low-acyl gellan, 147 Low calorie lipids, 211–212 Low-calorie sweeteners, 715 Low-density lipoprotein, 755 Parkin: Low-methoxyl (LM) pectins, 146 Low-temperature blanching, 426 Lumichrome, 484 Lumiflavin, 484 Lupulone, 646 Lutein, 456, 594, 754 Luteolin, 612 Lyases, 361 Lycopene, 455, 456, 595, 596, 597, 752, 755, 1085 anticancer activities, 755 Lyophobic colloids, 786 Lyoszyme, 72 Lyotropic series, 34 Lysinoalanine, 306 “Lyso”, 162 Lysozyme, 239, 281, 344 M Macronutrients carbohydrates, 1079–1080 fiber, 1080 novel lipids, 1080–1082 protein, 1078 Maillard browning, 96 inhibition of, 706 reactions, 677 Maillard reaction, 74, 96, 312, 316 condition effect, 866 mechanism and products of, 860–866 nomenclature and substrates, 860 nutritional significance, 866–867 product s 775 Malonaldehyde, 314, 315 Malondialdehyde (MDA), 209 Maltitol, 103, 723 Maltodextrins, 129, 368 Maltogenic α-amylases, 366 Maltol, 98 Maltooligosaccharides, 129, 366 Malvidin, 602 Mangiferin, 615 Mannitol, 93, 723 Marangoni effect, 798 Margarine, 184 Masticatory substances, 730–731 Mature fruit vegetables, 1040 Maturity, 1031 Maximal freeze concentration, 61 Maximally freeze-concentrated glass, 51 Maximally freeze-concentrated matrix, 59 Mealiness, 127 Mean hydrophobicity, 281, 649 Mean residue hydrophobicity, 296 Meat, meaning of, 924 Meat pigments curing process, 578 stability, 578–579 Meat restructuring, 967 Meat tenderization, 382 Medium chain fatty acids, 160, 1081 Medium-chain triglycerides, 728 Melanins, 408 “dk9272_c023” — 2007/7/20 — 21:28 — page 1132 — #14 Index 1133 Melanoidin, 97, 312 Melting, of food lipids, 169–171 Melting point, 168, 171 Menaquinones, 466 Mercury, 547 occurrence and toxicity, 548–550 Metabolic engineering, 1077–1078 Metabolomics, 1063 Metallo complex commercial application of, 590–591 formation, 587 Metalloenzymes, 544 Metalloproteases, 379–380 Methional, 678 Methionine-γ -lyase, 425 Methionine sulfone, 309, 312 Methionine sulfoxide, 309, 312 Methoxy alkyl pyrazine volatiles, 660–661 Methyl mercury chloride, 548 Methylcellulose (MC), 137, 736 Methylcobalamin, 508 Methylmalonyl-CoA mutase, 509 Metmyoglobin, 574 Michaelis constant, 348 Michaelis–Menten kinetics, 348 Michaelis pH function, 396 Microarray technology, 1057–1058 Microbial transglutaminase, 965 Microcrystalline cellulose (MCC), 136–137, 737 Microcrystallites, 818 Micronutrients allergens, 1087–1088 antinutrients, 1086–1087 photochemicals, 1083, 1085–1086 toxins, 1088 vitamins and minerals, 1082–1083 Middle lamella, 1006 Mie theory, 274 Milk clotting, 381–382 Milk fat, 905 Milk lipids, 891–895 chemical composition of, 891–895 functionality in formulated foods, 911–912 Milk proteins, 889–891, 915 charge characteristics of, 898 chemical composition of, 889–891 functionality in formulated foods, 908–909 structure of caseins, 897–899 whey proteins, 899–902 Milk salts, 902–904 chemical composition of, 895–896 and protein micelle, 905–907 Milk sugar chemical composition of, 895–896 Minerals chemical and functional properties of minerals in foods calcium, 560 copper, 564 iron, 563 nickel, 564 Parkin: phosphates, 560–562 sodium chloride, 562–563 content, 102 mineral composition of foods affecting factors, 551–554 ash, definition and significance in food analysis, 550–551 effects of processing, 558–560 fortification and enrichment of foods with minerals, 555–558 individual minerals, 551 nutritional aspects bioavailability of minerals, 532–538 DRIs for mineral nutrients (United States and Canada), 530, 532 essential mineral elements, 529–530 essential minerals, overview, 538 individual minerals, 538–546 toxicology of food-borne heavy metals, 546–550 principles of mineral chemistry chelate effect, 527–529 minerals and acid/base chemistry, 525–527 solubility of minerals, in aqueous systems, 525 Miraculin, 722 Mixed crystals, 176 Mixed gels, 821 Mixture models, 26 M-line proteins, 930, 942, 946 Mobility temperature, 52 Modified atmosphere (MA), 990, 1037 benefits, 1038 Modified atmosphere, on pigment stability, 579 Modified atmosphere packaging, 579 Modified food starch, 126, 130–134 Modulus, 812 Moisture sorption isotherms (MSI) definitions and zones, 65–70 hydration sequence of protein, 72 hysteresis, 70–72 and Mm and RVP, interrelationships between, 76–77 temperature dependence, 70 Molecular aspects, of proteins, 262 Molecular flexibility, 272, 276 Molecular mobility, 54 Molecular pharming, 1088, 1097–1098 Molecular stability (Mm) and food stability history, 46 limitations of concept, 55–57 practical applications, 57–65 reaction rates in solution, influencing factors, 47–48 relationship between, 48 and RVP and MSI, interrelationships between, 76–77 state diagram, 49–55 MOLESCRIPT program, 900, 901 Molten structure, 255 Monellin, 722 Monodentate ligands, 527 Monolayer, 264 Monorefringent, 23 Monosaccharides, 84 glycosides, 90–92 isomerization, 87 “dk9272_c023” — 2007/7/20 — 21:28 — page 1133 — #15 Index 1134 Monosaccharides (continued) reactions, 92 acrylamide formation, in food, 101–103 caramelization, 100 carbonyl groups, reduction of, 92–93 hydroxyl group esters, 94–95 hydroxyl group ethers, 95–96 nonenzymic browning, 96–100 oxidized, to aldonic acids and aldonolactones, 92 uronic acids, 93–94 ring forms, 87–90 Monosodium l-glutamate, 652 Montmorillonite, 733 Morphology, 176 Multidentate ligands, 527 Muramidase, 344 Muscle fiber types, 949–950 Muscle to meat conversion, 950 postmortem degradation of muscle proteins, 951–952 Mutachrome, 458 Myofibers, 928 Myofibrillar proteins, 933, 964 Myoglobin, 252, 543, 573–578 chemistry and color discoloration, 577–578 oxidation state, 574, 577 heme compound structure, 573–574 Myomesin, 946 Myosin, 940–942 Myrosin cells, 422 Myrosinase, 422 N Naringen, 647, 648 Naringenase, 647, 648 Natamycin, 711 Natural plant toxicants, 770 Nebulin, 945 Neoflavones, 611 Neohesperidin dihydrochalcone, 722 Neotame, 717, 719 Neoxanthin, 594, 596 Nephrocytomegaly, 307 Nephrotoxicity, 307 Net protein ratio (NPR), 300 Net protein utilization (NPU), 301 Neurasthenia, 549 Neurotoxin, 548 Neutralization, 179 Neutralizing value, 694 Neutral salts, 258 Newtonian fluids, 284 Niacin, 485–486 analytical methods, 486 bioavailability, 486 in selected foods, 487 structure and general properties, 485–486 Nicotinamide, 485 Nicotinic acid, 485 Ninhydrin, 228 Nisin, 714 Parkin: Nitrate, 961–962 Nitric oxide, 962 Nitric oxide synthase, 766 Nitrihemin, 578 Nitrimyoglobin, 578 Nitrite burn, 578 Nitrites, 315–316, 706–707, 962 with secondary amines, 315 Nitrogen tetroxide, 735 Nitrosamines, 464, 706 N-Nitrosamines, 316 N-Nitrosoamine, 315 S-Nitrosocysteine, 316 Nitrosomyoglobin, 706 N-Nitrosopyrrolidone, 316 N-Nitrosotryptophan, 316 Nitrosyl chloride, 735 Nitrosylhemochrome, 578 Nitrosylmyoglobin, 578 Nitrous anhydride, 453 Nomenclature and classification, of enzymes, 361 Nonanthocyanin (NA) flavonoids copigmentation, 612 Noncompetitive inhibitor, 354 Noncovalent interactions, 240, 241 Nonenzymatic browning, 96–100, 312, 705 and black spot formation, 876 Nonfreezable water, 109 Nonheme iron, 543 Nonlinear regression, 351 Nonpolar substances interaction of water with, 36–41 clathrate hydrates, 37–39 complex molecular structures, 39–41 Nonprotein nitrogen, 1011 Nonreducing sugar, 105 bis-Norbiotin, 505, 506 Norbixin, 629 Novel lipids, 1080–1082 Nuclear magnetic resonance (NMR), 171 Nucleation, 172–173 Nucleophilic catalysis, 340 Nutrient composition, of milk and milk products, 912–914 Nutrient value, 924–927 Nutrification, 443 Nutrigenomics, 1063 Nutritional aspects, of minerals bioavailability of minerals, 532–538 enhancers, 535–536 inhibitors, 536–538 DRIs for mineral nutrients (United States and Canada), 530, 532 essential mineral elements, 529–530 essential minerals, overview, 538 individual minerals, 538–546 calcium, 539–541 chloride, 541–542 iodine, 544–545 iron, 542–544 phosphorus, 541 potassium, 541 selenium, 545–546 sodium, 541–542 zinc, 544 “dk9272_c023” — 2007/7/20 — 21:28 — page 1134 — #16 Index 1135 toxicology of food-borne heavy metals, 546–550 cadmium, 550 lead, 548 mercury, 548–550 Nutritional genomics, 1082 Nutritional quality, 297 Nutritive value, of bovine milk nutrient composition, of milk and milk products, 912–914 lactose tolerance, 915 proteins, effect on, 915 vitamins, effect on, 915–916 O Odor units (OUs), 642 Off-aromas, 207 Off-flavors, 207 Oil, 165 Oil-in-water emulsion-type food products, 868–869 Oilseed, 1039 Oil–water interface, 281 Olean, 730 Olestra, 730 Oligomeric proteins, 263 Oligosaccharides, 101 cyclodextrins, 106–107 lactose, 103–105 maltose, 103 sucrose, 105–106 Optical activity, 222–223 Optical properties of amino acids, 228 Organic acids, 1015–1016 metabolism, 1025–1026 Organic phosphates 541 Organomercury compounds, 549 Ornithoalanine, 306 Orthorhombic packing, 177 Osmolality, 55, 56 Osmoprotectants, 402 Osmotic effects, 402–403 Osteoarthritis, 546 Osteoporosis, 539 Ostwald ripening, 176, 796, 829, 836, 839–840 Ovalbumin, 281 Overbeating, 280 Overrun, 277 Ovoinhibitor, 304 Ovomucoid, 304 Ovoverdin, 596 Oxalates, 540, 774 Oxidation, 92, 131, 408 cysteine, 310 cystine, 310 methionine, 309–310 tryptophan, 310–312 tyrosine, 312 β-Oxidation, 662, 708 of linoleic acid, 663 Oxidation-sensitive vitamins, 453 Oxidative rancidity, 187 Oxidative stress, 765 Oxidoreductases, 346, 415 Parkin: Oxygen concentration, 206 β-Oxyindolylalanine, 310 Oxymyoglobin, 574 Oxytetracycline, 714 P Pale, soft, exudative meat (PSE), 953–954 Pancreatic adenoma, 303 Pancreatic hypertrophy, 303 Panthenol, 507 Pantothenic acid, 506–508 analytical methods, 508 bioavailability, 507 degradation, stability and modes of, 507 structure and general properties, 506–507 Papain, 294, 346 Paprika/paprika oleoresin, 630 Parabens, 711–712 Para-casein micelles, 288 Parallel β-sheet, 236 Parathaesia, 549 Parenchyma, 979 cis-Parinaric acid, 276 Partial coalescence, 833–835 Partial specific volume, 256 Particle gels, 809, 813–814 Paste, 120, 123–125 Pasteurization, 906 PCR, 1056–1057 Pectate lyase, 373, 374–375 Pectic acid, 731 Pectin, 146–147, 731, 1006 Pectin methyl esterases, 373, 374, 731, 1022 Pectin transformation enzymes, 373–376 application, 375–376 pectate lyase, 373, 374–375 pectin methyl esterases, 373, 374 polygalacturonases, 373–374 Pectinase, 373 Pectinic acid, 731 Pelargonidin, 602 Pellagra, 443 Penicillium roqueforti, 708 Pentadiene system, 158 Pentosans, 1008 Pepsin, 294 Peptide bonds, 231, 233 Peptide sweeteners, 717–719 Peptide unit, 232 Permeability, of gel, 816–817 Permittivity, 18, 22, 257 Peroxidases, 412, 1029 Peroxide values, 208 Peroxides, 205 Peroxyl radical, 188 Petunidin, 602 pH, 10 effects, 392 on enzyme activity, 394–399 stability, 393–394 pH “optimum”, 395, 398 Phage T4 lysozyme, 252 Phase diagram, 49 “dk9272_c023” — 2007/7/20 — 21:28 — page 1135 — #17 Index 1136 Phase inversion, 274 Phase relationships, 28 Phaseolin, 238, 297 Phenol oxidases, 407–412 Phenolase, 564 Phenolic acid, 1017 tannin, 1017–1020 Phenylalanine, 718 Pheophorbide, 581, 582, 586 Pheophytin, 581, 583, 589 formation, 585 Phloroglucinol, 609 Phorbin, 580 Phosphates, 962 in animal tissues, 700 Phosphofructokinase, 406 Phospholipases, 388 Phospholipids, 162, 1012 Phosphorus, 541 Phosphorus oxychloride, 320 Phosphorylation, 320–321 Photochemical degradation, 509 Photochemicals, 1083, 1085–1086 Photodegradation, of chlorophyll, 588–589 Photoisomerization, 458 O-Phthaldialdehyde, 231 Phylloquinones, 466 Physical and chemical interactions, of food system components chemical interactions, 860 Maillard reaction, 860–867 food flavor, interactions affecting flavor compound interactions, with main food components, 877 hydrolytic reactions, 877 oxidative reactions, 878 interactions effect, on food color anthocyanins, interactions of, 875–876 carotenoids, interactions of, 875 discoloration, due to metal ion binding, 876 hemoproteins, changes in, 874–875 nonenzymatic browning and black spot formation, 876 microstructure types in foods crystals, 858–860 fat globules, 851–853, 855 fibrils, 855 granules, 856–858 lipid globules, 851–852, 853–854 protein micelles, 855 sheets, 855, 856 water droplets, 851 polysaccharide interactions, 869–870 polysaccharide–lipid interactions, 871 polysaccharide–protein interactions, 871–874 protein–lipid interactions, 868–869 protein–protein interactions, 868 reactions, due to heating in alkaline conditions, 867 texture and rheological food properties, interactions affecting biodegradable film formation, 879–880 cross-linking, in gels, 879 dough and baked loaf, interactions in, 880–881 freeze denaturation, of proteins, 878–879 Parkin: water–protein interactions ice crystal growth inhibition, by proteins, 868 water in proteinaceous structures, 867–868 Physiological disorders, 999, 1038 Physiological maturity, 986 Phytase, 1087 concentration in food, 537 Phytate, 299, 1086 Phytic acid, 544, 1010 Phytoalexins, 996 Phytochemicals, 1075, 1077 generalized protective mechanisms of, 764–767 Phytochemicals, health-promoting carnosic acid, 762 carotenoids, 753–755 curcumin, 759 flavonoids, 755–759 gingerol, 759–761 indoles, 762, 763–764 isothiocyanates, 762–763 proanthocyanidins, 759 resveratrol, 762 sulfur-containing bioactives, in Allium family, 762 Phytoestrogens, 752 Phytohemagglutinins, 303 Phytol, 580 Phytosterol, 211, 461 Pigments, 572, 573 anthocyanins, 599–610 betalains chemical properties, 616–619 physical properties, 616 structure, 615–616 carotenoids, 593–599 chemical properties, 597–599 occurrence and distribution, 596–597 physical properties, extraction and analysis, 597 stability during processing, 599 structures, 595–596 chlorophyll alterations, 582–589 color loss during thermal processing, 589 physical characteristics, 581–582 structure and derivatives, 579–581 technology of color preservation, 589–593 flavonoids, 610–613 heme compounds cured meat pigments, 578 myoglobin/hemoglobin, 573–578 packaging considerations, 579 stability of meat pigments, 578–579 metabolism, 1029–1030 of plant tissues, 1020 quinoids, 613–614 xanthones, 614–615 Pimaricin, see Natamycin Pineapple compound, 680 Piperine, 655 Plant foods, 551, 553–554 Plant hormones, 992 ethylene, 994–996 role, 992–994 Plant organs, 979–983 Plant phenolics, 202–203 “dk9272_c023” — 2007/7/20 — 21:28 — page 1136 — #18 Index 1137 Plant stress responses, 998 disorders, from environmental toxicants, 1003–1004 ionizing radiation, 1003 nutritional disorders, 1003 physical damage, 999 temperature extremes chilling injury, 1001–1002 freezing injury, 999–1001 high temperatures injury, 1002 Plant tissues chemical composition components, 1004 compositional changes, 1021 commodity descriptions, 1039–1042 extend shelf life and preserve quality, techniques, 1031–1039 fruits and vegetables, processing effects on, 1042–1045 losses of, 976–978 postharvest physiology, 979 cellular structure, 983–985 development, 985–986 gene expression and protein synthesis, 991–992 growth, 985–986 horticultural maturity, 986 plant hormones, 992–996 plant organs, 979–983 plant stress responses, 998–1004 respiration, 986–991 transpiration and water loss, 996–998 Plant transformation, 1069–1071 Plasmalemma, 984 Plasmid, 1055 Plasmin, 427 Plasmin inhibitor (PI), 304 Plasminogen activator inhibitor (PAI), 304 Plastein reaction, 322 Plasteins, 402 Plastic range, 170 Plasticity, 166 Plasticization, 53 Plasticizing water, 109 Plastids, 984 Plateau border, 838 Platelet aggregation, 762 PN-glucoside, 495 Polar paradox, 206 Polydextrose, 729 Polygalacturonase (PG), 373–374, 991 Polymerase chain reaction see PCR Polymers, 792–793 gels, 809, 813 nondigestibility, 149 Polymethoxylated flavones, 758 Polymorphism, 176–178 Polyols, 722–726 Polyphenol oxidase, 303, 315, 407, 1029 for anthocyanin oxidation, 610 Polyphenolics, 1017 Polyphenols, 309, 315, 656, 1019 Polysaccharide–lipid interactions, 871 Polysaccharide–protein interactions, 871–874 Polysaccharides, 108, 817–818 agar, 141, 144 Parkin: algins, 144–145 carrageenans, 141–144 cellulose, 135 carboxymethylcellulose, 137 hydroxypropylmethylcelluloses, 137 methylcellulose, 137 microcrystalline cellulose, 136–137 chemical structures and properties, 108 curdlan, 147–148 fructooligosaccharides, 149 furcellaran, 141, 144 gellan, 147 gels, 113–114 guar gums, 138 gum arabic, 148–149 hydrolysis, 114–120 interactions, 869–870 inulin, 149 locust bean gums, 138 pectins, 146–147 solubility, 108–109 solution viscosity and stability, 109–113 starch, 120 amylase, 120–121 amylopectin, 122–123 cold-water-soluble, 135 cold-water-swelling, 135 complex, 128 food processor, 130–134 gelatinization, within vegetable tissues, 126–127 granules, 125 hydrolysis, 128–130 retrogradation, 127–128 staling, 128 unmodified starch, uses of, 126 xanthan, 138–141 Polyunsaturated fatty acids, 158 Polyvinylpyrrolidone (PVP), 733, 734 Pome fruits, 1040–1041 Porcine stress syndrome (PSS), 953–954 Porphin, 579 Porphyrin, 574, 580 Postmortem biochemical changes, natural and induced affecting meat quality, 952–958 cold shortening, 955–957 dark, firm, and dry meat, 954–955 electrical stimulation, 957–958 pale, soft, exudative meat, 953–954 thaw rigor, 957 Postmortem degradation, of muscle proteins, 951–952 Potassium, 541 Potassium acid tartrate, 692 Potassium bromate dough improvers, 735 Potential energy function, 242 Power law, 288 Precooked starch, see Prepasted starch Pregelatinized products, 131 Pregelatinized starch, 135 Prepasted starch, 135 Pressure-induced denaturation, 256 Pressure-induced gels, 256 Pressure-shift freezing, 28, 959 Pressurization, 959–960 Pro-α chains, 936–937 “dk9272_c023” — 2007/7/20 — 21:28 — page 1137 — #19 Index 1138 Proanthocyanidins, 612–613, 759 with condensed tannins, 759 hydrolysis of, 613 Processed meats, chemistry of, 961 curing technology, 961–962 fat immobilization and stabilization, 965–967 hydration and water retention, 962–964 meat restructuring, 967 protein gel matrix formation, 964–965 Surimi, 967–968 Process-induced nutraceuticals, in foods, 767, 769 Process-induced toxicants, in foods, 774–776 Product composition, 10 Product selectivity, 360 Progel state, 286, 287 Prolamines, 266, 269 d-Proline, 305 Prolylendopeptidase, 294 Prooxidants, 190–195 control, 204 and free radicals formation, 194 and hydroperoxides decomposition, 194–195 and lipid hydroperoxides formation, 191–194 Propagation, 188 Propionic acid, 707 Propylene glycol alginates, 145 Prostate, 456 Prosthetic groups, 219 Proteases, 377 specificity of, 294 Protein, 793, 805, 827, 831, 1010–1011, 1078 chemical modification, 318–321 cross-linking, 306–309 denaturation, 247–260 agents, 251–260 thermodynamics, 249–251 enzymatic modification, 321–323 functional properties, 260 changes in, 316 dough formation, 291–293 flavor binding, 282–284 gelation, 286–289 hydration, 262–266 interfacial properties, 269 solubility, 266–269 texturization, 289–291 viscosity, 284–286 hydrolysates, 293 allergenicity, 295–296 bitter peptides, 296 functional properties, 294–295 of muscle tissue, 933 connective tissue proteins and matrix, 934–937 contractile proteins, 940–943 proteins of sarcoplasmic reticulum and sarcolemma, 946–948 regulatory proteins, 943–944 sarcoplasmic proteins, 937, 939–940 structural proteins, 944–946 nutritional properties, 296 digestibility, 297–300 nutritive value, evaluation of, 300–302 quality, 296–297 reactions, during food processing, 852 Parkin: structure conformational stability and adaptability, 246–247 forces involved in stability of, 241–246 primary, 231–233 quaternary, 239–241 secondary, 233–237 tertiary, 237–239 Protein bodies, 984 Protein denaturation, freeze-induced, 959 Protein dispersibility index (PDI), 269 Protein efficiency ratio (PER), 300 Protein engineering, 1060–1062 Protein extraction, 267 Protein fat mimetics, 727–728 Protein–flavor interactions, 282–283 Protein gel matrix formation, 964–965 Protein hydrolysates, 381 Protein–lipid interactions, 868–869 Protein micelle, 855, 905–907 Protein–protein interactions, 868 Protein solubility index (PSI), 269, 290 Protein synthesis, 991 Proteinases see Proteases Proteinuria, 549 Proteolytic enzymes, 355–357 Proteomics, 1063 Proteosomes, 952 Protonation, of carbonyl and amine compounds, 863 Pseudobinary diagram, 50 Pseudoplastic behavior, 284 Pseudoplastic flow, 112 Psyllium, 150 Pullulanases, 367 Pulp wash, 376 Pulses, 1039 Pungency, 654–656 Pungent flavors, 422 Pure water relationships, 28 Pure water systems, structures in ice structure, 22–26 water (liquid) structure, 26–27 Pyranose ring, 88 Pyrazine, 100 Pyridoxal (PL), 488 interconversion, 491 Pyridoxamine (PM), 488 4-Pyridoxic acid, 490 Pyridoxine (PN), 487 Pyridoxine-5 -β-D-glucoside, 487, 488 Pyridoxyllysyl, 494 Pyrolysis, 305, 314 Pyropheophorbide, 581 Pyropheophytin, 581, 584, 589 formation, 585 Pyrroles, 97 Pyrroloquinoline quinone (PQQ), 512 Q Q10 , 990 Q-enzyme, 1007 Quality standards, 1031 Quercein, 315 “dk9272_c023” — 2007/7/20 — 21:28 — page 1138 — #20 Index 1139 Quercetin, 605, 1083 anti-infammatory agent, 758 Quercitrin, 605 Quinine, 309, 315, 645 Quinoids, 613–614 Q-values, 649 R Racemization, 304–305 Radiolysis, 308 Raffinose, 105 Random structure see Aperiodic structure Rate expressions, 349 RDNA technology, 1052, 1054–1056 Reaction coordinate, 334 Reactivity, of amino compounds, 863 Rebaudiosides, 721 Recommended dietary allowances (RDAs), 532 Redox cycling, 194 Reduced iron, 557 Reduced viscosity, 286 Reducible cross-links, 937 Reducing agents, 411 Reducing sugars, 92 Reductive glycosylation, 319 Reductones, 98 Reference daily intake (RDI), 446 Reference protein, 301 Refining, of lipid, 178–179 bleaching, 179 degumming, 179 deodorization, 179 neutralization, 179 Refractive index, 169 Regioselectivity, 360 Regreening, 592–593 Regulatory proteins tropomyosin, 943 troponin, 943–944 Relative vapor pressure (RVP) and food stability, 72–76 and Mm and MSI, interrelationships between, 76–77 and water activity, 41 definition and measurement, 41–43 temperature dependence, 43–46 Relative viscosity, 285 Rennet, 357 Rennin, 288 Resilin, 220, 306, 312 Resistant starch, 149, 1079 Respiration, 986 affecting factors, 988–989 storage life, 989–991 Respiratory quotient (RQ), 987 Resveratrol, 752, 1086 antimutagen, 762 platelet aggregation, 762 Retaining, 363 Retinal, 454 Retinoic acid, 454 Retinoids, 454, 595 Retinol, 454 Parkin: Retinyl acetate, 454 Retinyl palmitate, 454 Retrogradation, 112 Rheological properties, 166–167, 281 Riboflavin, 311, 630 analytical methods 485 bioavailability, 485 degradation, stability and modes of, 483–485 distribution, 484 photolysis, 484 structure and general properties, 482–483 Riboswitches, 1058, 1060 Ribozymes, 1058 Rmax , 292 RNA interference (RNAi), 1060 RNA silencing, 1060 Rosanoff method, 87 Rounding off, 127 Rubbery state, 262 Ruhemann’s purple, 228 Rutin, 612 Ryanodine receptor (RyR), 946–947 S Saccharification, 367 Saccharin, 644, 716–717 Saffron, 631 Salatrim, 728 Salt substances, 651–652 Salted-out, 279 Salting in, 34, 268, 279 Salting out, 34, 268 Salts, 255 Sandiness, 60, 908 Saporous sensations, 643 Saporous substances, 643 Saporous unit, 644 Sarcolemma, 928, 946–948 Sarcomere, 930 Sarcoplasmic proteins, 933, 937, 939–940 Sarcoplasmic reticulum, 928, 946–948 Saturated fatty acids, 157 Saturated vapor pressure (SVP), 997 Scatchard equation, 282 Scatchard plots, 283 Schiff base, 97, 313, 315, 489, 490, 618 Scissile bond, 357 β-Scission, 194 Sclerenchyma, 979 Secondary lipid oxidation products, 208 Secretin, 232 Sedimentation, 806–807 Selectivity, 339 of enzyme, 347 Selenium, 538, 545–546 Selenocysteine, 220, 545 Selenomethionine, 538, 545 Selenoproteins, 545 Senescence, 986 Sequestrants, see Chelating agents Serine proteases, 294, 377–378 Shear rate, 284 Shear stress, 166, 284 “dk9272_c023” — 2007/7/20 — 21:28 — page 1139 — #21 Index 1140 Shear-thinning behavior, 284 Sheets, 855, 856 β-Sheet structure, 236 Shiitake flavor, 660 Shiitake mushrooms, 660 Shikimic acid pathway, 664 Shogaols, 656 Shortening, 185 Short flow, 113 Simplesse, 257 Simple sugar, see Table sugar Singlet oxygen, 191–192, 458 Site-directed mutagenesis, 1062 Skeletal muscle structure, 928–932 Sliding filament theory, 930 Small-molecule surfactants, 832 Smoke point, 169 Smoluchowski’s equation, 47 Smooth muscle structure, 932–933 Sodium, 541–542 Sodium chloride (NaCl), 961 Sodium copper chlorophyllin, 628 Sodium erythorbate, 962 Soft solids food gels, 817–821 caseinate gels, 820 gelatin, 818–819 globular proteins gels, 820–821 mixed gels, 821 polysaccharides, 817–818 functional properties, 815–817 gels, characterization of modulus, 812 particle gels, 813–814 polymer gels, 813 rheological parameters, 810–812 structure, 809–810 mouthfeel of foods, 821–823 Sol state, 286 Solid-fat content (SFC), 167, 170 Solid solution, 176 Solubility, 266 and ionic strength, 268 of minerals, in aqueous systems, 525 organic solvents, 269 and pH, 267 and temperature, 269 Solutes aqueous solutions, water–solute interactions in hydrogen bonding, 34–36 ions and ionic groups, 33–34 macroscopic level, 31–32 molecular level, 32–33 nonpolar substances, 36–41 ice in the presence of, 28–31 Sorbamic acid, 474 Sorbic acid, 691, 707–709, 725 Sorbitan, 96 Sorbitan monostearate, 724 Sorbitol, 93, 723 Sorption hysteresis, 70 Sour substances, 652 Soy proteins, 280 Spans, 724 Parkin: Specific heat capacity, 168 Specific viscosity, 285, 286 Specificity constant, 350 Spherosil QMA process, 910, 911 Spherosil S process, 910, 911 Sphingolipids, 163 Spreadability, 184 Spun-fiber process, 290 Spun-fiber texturization, 289–290 Stability constant, 527 Stabilized starches, 131 Stabilizers, 726–727 Stachyose, 105, 1079 Staling, 127–128 Staphylococcus aureus, 42, 304 Starch, 120, 1006 amylase, 120–121 amylopectin, 122–123 cold-water-soluble, 135 cold-water-swelling, 135 complex, 128 food processor, 130–134 gelatinization, within vegetable tissues, 126–127 granules, 125 hydrolysis, 128–130 retrogradation, 127–128 staling, 128 unmodified starch, uses of, 126 Starch degrading enzymes, 1023 Starch hydrolysis, 368–39 Starch liquefaction, 366 Starch paste, 124 Starch–sugar transformations, 1023–1025 Starch-transforming enzymes, 364–370 α-amylase, 364–366 β-amylase, 366 baked goods, 369–370 brewery, 370 cyclomaltodextrin glucanotransferase, 367–368 glucoamylase, 367 pullulanases, 367 starch hydrolysis, 368–369 State diagram, 49–55, 76 assumptions, identifying, 53–55 complex food systems, 53 developing, 57–59 equilibrium and kinetics, interplay of, 51–52 interpretation, 50–51 Steady-state approach, 348 Steady-state relative humidity (SSRH), 42–43 Stereochemisty of amino acids, 221–222 Steric repulsion, 803 Steric strains, 241 Sterols, 163–164 Stevioside, 721 Still-freezing, 959 Stokes–Einstein equation, 48 Stomata, 980 Stone fruits, 1041 Storage organs, 1039 Storage proteins, 1010 Strain, 345 “dk9272_c023” — 2007/7/20 — 21:28 — page 1140 — #22 Index 1141 Strecker degradation, 98, 312, 313, 474, 663, 678, 775, 866 of amino acids with oxidizing agents, 862 Stress metabolites, 999 Stromal proteins, 933 Structural organization, of bovine milk components casein micelles, 902–904 fat globule, 904 proteins, structure of caseins, 897–899 whey proteins, 899–902 salts, 902–904 Structural proteins, 944–946 Structure breaking ions, 34 Structured lipids, 212, 387 Structure forming ions, 34 Struvite, 590 “Substantial equivalence”, 1095 Substrate binding, 394 Substrate recognition, 357 Substrate transformation, 394 Subtilisin, 377, 1065 Subtilisin A, 294 Subtropical fruits, 1041 Succinic acid, 653 Succinic anhydride, 319 Sucralose, 719–721 Sucrase, 106 Sucrose, 93, 720, 1006 Sucrose diacetate hexaisobutyrate, 732 Sucrose polyesters, 729–730 Sugar transformation glucose isomerization, 370–371 glucose oxidase, 371 glucosidases, 372–373 invertase, 371 lactose hydrolysis, 372 Sugar wall defect, 428 Sugars, 255 Sulfated galactans, 141 Sulfhydryl–disulfide interchange reaction, 245, 287 Sulfhydryl oxidase, 389 Sulfhydryl protease, 346 Sulfides, 762 Sulfites, 411, 453, 704–706 Sulfiting agents, 453 Sulfitocobalamin, 509 Sulfitolysis, 321 Sulfoamide sweeteners, 716–717 Sulfomyoglobin, 578 Sulforaphane, 763 Sulfur, browning by, 706 Sulfur-containing bioactives, in Allium family, 762 Sulfur dioxide, 99, 704–706 Supercooling, 172 Superoxide, 472 Superoxide anion, 195, 205 Supertasters, 650 Supplemeted phase diagramsv 49 Surface-active properties, 269 Surface activity, 162 Surface area, 206 Surface dilational modulus, 797 Surface energy, 18 Parkin: Surface equation of state, 790 Surface hydrophobicity, 276, 281 Surface load, 790, 827–828 Surface phenomena contact angles, 793–795 curved interfaces, 795–797 interfacial rheology, 797–798 interfacial tension and adsorption, 788–790 surface tension gradients, 798–799 surfactants, 790–793 Surface pressure, 790 Surface tension gradients, 798–799 Surfactants, 789, 790–793, 837 amphiphiles, 791–792 functions, 799 polymers, 792–793 Surimi, 967–968 Sweet substances, 643–645 tripartite structure theory, 645 Sweetener production, 370 Syneresis, 113, 817 Synergism, 205 Synthase, 361 Synthetase, 361 Synthetic phenolics, 202 Synzymes, 1069 T Table sugar, 105 Tails, 271 Talin, 722 Tannic acid, 734 Tannins, 299, 478, 613, 656, 1017–1020 Tapioca starch, 120 Tea cream, 1018 Telopeptide, 937 Temperature, 8, 389 Termination, 190 Terpenes, 664 Terpenoids, 664–665 Tetrahedral intermediate, 341 Tetrahedral structure, 19 Tetrahedron, 21 Tetrahydrofolates, 496, 498 Texture, 184–185 Texture and rheological food properties, interactions affecting biodegradable film formation, 879–880 cross-linking, in gels, 879 dough and baked loaf, interactions in, 880–881 freeze denaturation, of proteins, 878–879 Thaumatin, 722 Thaw rigor, 957 Theaflavins, 613 Thearubigins, 613 Theobromine, 646 Thermal conductivity, 18, 168 Thermal denaturation, 255 Thermal diffusivities, 18 Thermal stability, of proteins, 252 Thermolysin, 294, 379 Thermophilic enzymes, 1066 Thermoplastic melt, 290 “dk9272_c023” — 2007/7/20 — 21:28 — page 1141 — #23 Index 1142 Thermostability, 366 Thermostable proteins, 253 Thiamin, 476–482 analytical methods, 482 bioavailability, 482 degradation, 478–482 rates, 479 energy of activation, 479 structure and general properties, 476–478 thermal stability, 478 unusual acid–base behavior, 476 Thiamin disulfide, 478 Thiamin hydrochloride, 477 Thiamin mononitrate, 477 Thiamin pyrophosphate, 476 Thiaminases, 478 Thick films, 841 Thickeners, 726–727 Thin-boiling starch, 129 Thin films, 841 Thiobarbituric acid (TBA), 209 Thiodipropionic, 703 Thiols, 203 Thixotropic flow, 113, 284 Thyroid hormones, 544 Time, Time scale, 787 Titanium oxide, 631 Titin, 232, 944–945 TMAO demethylase, 428 Tocopherols, 187, 199, 461, 463 α-Tocopheryl acetate, 463 Tocopheryl hydroquinone, 464 Tocopheryl quinone, 465 Tocotrienols, 463 Tofu manufacture, 289 Tolerable upper intake level, 532 Toxic compound nutritional quality and formation, 302 Toxicology, of food-borne heavy metals, 546–550 cadmium, 550 lead, 548 mercury, 548–550 Toxins, 1088 Trace element, 524 Trains, 271 trans fatty acids, 210 Transamidation, 308 Transgenes, 1060 Transgenic animals, 1088 Transgenic plants, 991 Transglutaminase, 288, 323, 384 Transition metals, 194 Transition-state theory, 336 Translucent gels, 287 Transpeptidase, 425 Transpeptidation, 402 Transpiration, 996 Transportation, 1036–1307 Triacylglycerols, 159, 858–859, 1013 functionality in foods appearance, 185–186 flavor, 186 texture, 184–185 Parkin: physicochemical properties, 164 density, 167–169 rheological properties, 166–167 Trichloroethylene, 315 Triclinic packing, 177 Trigonelline, 486 Trimethylamine, 675 Trimethylamine oxide, 676 2,4,6-Trinitrobenzene sufonic acid (TNBS), 313 Tropical fruits, 1041–1042 Tropocollagen, 935, 937 Tropomodulin, 945 Tropomyosin, 943 Troponin, 943–944 True protein digestibility, 300 Trypsin, 294, 1065 Trypsin inhibitors, 299 Trypsin inhibitory activity, 303 T-Tubules, 928 Tuning-fork, 164 Tunneling, 346 Turgor pressure, 984 Turmeric/turmeric oleoresin, 631 Tweens, 724 Two-state transition, 250 Tyrosinase, 408 U Ubiquinol, 512 Ubiquitous calpains, 952 UHT processing, 906 Umami substances, 652–653 Unfreezable water, 264 Unsaturated fatty acids, 157–159 Urease, 389 Urethane, 715 Uronic acid, 93–94 U.S RDA value, 446 V V-8 protease, 294, 295 Vacuole, 984 van der Waals attraction, 164, 800 van der Waals interaction, 241 van der Waals radii, 20 Vanillin, 654 Vaporization, 18 Vapor pressure (VP), 30, 997 Vapor pressure difference (VPD), 997 Vector, 1055 Vegetative organs, 1039 Veri-Green process, 592 Vicillins, 277 Violaxanthin, 595, 596 Viscosity, 284–286, 402 Vistec process, 910, 911 Vitamin A analytical methods, 459–460 bioavailability, 459 degradation, stability and modes of, 456–459 structure and general properties, 454–456 Vitamin B2 see Riboflavin “dk9272_c023” — 2007/7/20 — 21:28 — page 1142 — #24 Index 1143 Vitamin B6 , 487–496 bioavailability, 495–496 degradation, stability and modes of, 490–495 energy of activation, 494 interconversion, 490 ionization, 488 measurement, 496 potential neurotoxicity, 488 rate constants, 494 structure and general properties, 487–490 zwitterionic form, 488 Vitamin B12 , 508–510 analytical methods, 510 bioavailability, 510 degradation, stability and modes of, 509 structure and general properties, 508 Vitamin D analytical methods, 461 structure and general properties, 460–461 Vitamin E analytical methods, 466 bioavailability, 465 degradation, stability and modes of, 464–465 scavenging singlet oxygen, 465 structure and general properties, 461–464 Vitamin K analytical methods, 467 structure and general properties, 466–467 Vitamins, 441, 915–916, 1020–1021 analytical methods, 446 bioavailability, 446–448 dietary recommendations, 444–446 essential vitamin-like compounds, 510–513 fat-soluble vitamin, 454 and minerals, 1082–1083 nutrients foods, addition of, 443–444 oxidation-sensitive, 453 retention, optimization, 513–514 sources, 442–443 stability, 441–442, 445 water activity, 452 toxicity, 442 variation/losses, causes blanching effects and thermal processing, 450–451 chemical composition, influence, 453 inherent variation, 448–449 postharvest changes, 449 preliminary treatment, 449–450 during thermal processing, losses, 451–453 water-soluble vitamins, 467 V max /KM , 350 W Warner–Bratzler shear test, 955 Water, 1004–1006 Water activity, 10, 206–207, 452, 482, 726 effects, 400 Water and ice, 18 aqueous solutions, water–solute interactions in hydrogen bonding, 34–36 ions and ionic groups, 33–34 Parkin: macroscopic level, 31–32 molecular level, 32–33 nonpolar substances, 36–41 Mm and food stability history, 46 limitations of concept, 55–57 practical applications, 57–65 reaction rates in solution, influencing factors, 47–48 relationship between, 48 state diagram, 49–55 MSI definitions and zones, 65–70 hydration sequence of protein, 72 hysteresis, 70–72 temperature dependence, 70 physical properties, 18 pure water systems, structures, in ice structure, 22–26 water (liquid) structure, 26–27 pure water, phase relationships of, 28 RVP and food stability, 72–76 RVP and water activity, 41 definition and measurement, 41–43 temperature dependence, 43–46 RVP, Mm and MSI, interrelationships between, 76–77 solutes, ice in the presence of, 28–31 water molecule, 18–22 association, 20–22 dissociation, 22 Water binding, 31 in animal tissues, 700 Water binding capacity, 262, 265, 317 Water binding potential, 31 Water content, 255 Water holding capacity, 31–32, 265, 287, 700 Water-in-oil emulsion-type foods, 869 Water loss, 996–998 Water molecule, 18–22 association, 20–22 dissociation, 22 Water–protein interactions ice crystal growth inhibition, by proteins, 868 water in proteinaceous structures, 867–868 Water-soluble vitamins, 467 ascorbic acid, 467–475 biotin, 505–506 folate, 496–504 niacin, 485–486 pantothenic acid, 506–508 riboflavin, 482–485 thiamin, 476–482 vitamin B12 , 508–510 vitamin B6 , 487–496 Water–solute interactions, in aqueous solutions hydrogen bonding, 34–36 ions and ionic groups, 33–34 macroscopic level, 31–32 molecular level, 32–33 nonpolar substances, 36–41 Waxes, 164, 1014 Waxiness, 127 Waxy maize, 120, 123 “dk9272_c023” — 2007/7/20 — 21:28 — page 1143 — #25 Index 1144 Weak gels, 815 Wheat dough, viscoelasticity of, 292 Whey protein concentrates (WPC), 280, 910, 911 Whey protein isolate (WPI), 267, 910, 911 Whey proteins, 899–902, 907, 917–918 use, in formulated foods, 910–911 Williams–Landel–Ferry (WLF) equation, 47, 52, 55 Winterization, 180 Wood rosin, 730 Wound physiology, 999 X Xanthan, 112 Xanthones, 614–615 Xanthophylls, 595 Xylanases, 376 Xylans, 376 Xylitol, 93, 723 Y Yielding, 811 Yield stress, 166, 285 Young equation, 793–795 Z Zeaxanthin, 456, 594, 596, 754 Z-disc, 930, 931, 945, 952 Zein, 296 Zinc, 544, 558 Zinc metallo enzymes, 544 Zinc pheophytin a, 587 Zn-protoporphyrin, 578 Zn-pyropheophytin, 587 Parkin: “dk9272_c023” — 2007/7/20 — 21:28 — page 1144 — #26 ... agricultural and food chemistry came largely through his books on agricultural chemistry, of which the first (1813) was Elements of Agriculture Chemistry, in a Course of Lectures for the Board... flavor, nutritive value Texture, flavor, color, nutritive value Texture, flavor, color, nutritive value; toxic substances can be generated Texture, flavor, color, nutritive value Texture, flavor,... Nutrition Department University of Florida Gainesville, Florida Jeffrey K Brecht Horticultural Sciences Department University of Florida Gainesville, Florida Norman F Haard Department of Food