Food Biochemistry and Food Processing Editor Y H Hui Associate Editors Wai-Kit Nip Leo M.L Nollet Gopinadhan Paliyath Benjamin K Simpson Food Biochemistry and Food Processing ©2006 Blackwell Publishing All rights reserved Blackwell Publishing Professional 2121 State Avenue, Ames, Iowa 50014, USA Orders: Office: Fax: Web site: 1-800-862-6657 1-515-292-0140 1-515-292-3348 www.blackwellprofessional.com Blackwell Publishing Ltd 9600 Garsington Road, Oxford OX4 2DQ, UK Tel.: ϩ44 (0)1865 776868 Blackwell Publishing Asia 550 Swanston Street, Carlton, Victoria 3053, Australia Tel.: ϩ61 (0)3 8359 1011 Authorization to photocopy items for internal or personal use, or the internal or personal use of specific clients, is granted by Blackwell Publishing, provided that the base fee of $.10 per copy is paid directly to the Copyright Clearance Center, 222 Rosewood iv Drive, Danvers, MA 01923 For those organizations that have been granted a photocopy license by CCC, a separate system of payments has been arranged The fee codes for users of the Transactional Reporting Service are ISBN-13: 978-0-8138-0378-4; ISBN-10: 0-8138-0378-0/2006 $.10 First edition, 2006 Library of Congress Cataloging-in-Publication Data Food biochemistry and food processing / editor, Y.H Hui ; associate editors, Wai-Kit Nip [et al.].— 1st ed p cm Includes index ISBN-13: 978-0-8138-0378-4 (alk paper) ISBN-10: 0-8138-0378-0 (alk paper) Food industry and trade—Research I Hui, Y H (Yiu H.) TP370.8.F66 2006 664—dc22 2005016405 The last digit is the print number: Contents Contributors vii Preface xiii Part I: Principles Food Biochemistry—An Introduction W K Nip Analytical Techniques in Food Biochemistry 25 M Marcone Recent Advances in Food Biotechnology Research 35 S Jube and D Borthakur Browning Reactions 71 M Villamiel, M D del Castillo, and N Corzo Part II: Water, Enzymology, Biotechnology, and Protein Cross-linking Water Chemistry and Biochemistry 103 C Chieh Enzyme Classification and Nomenclature 135 H Ako and W K Nip Enzyme Activities 155 D J H Shyu, J T C Tzen, and C L Jeang Enzyme Engineering and Technology 175 D Platis, G A Kotzia, I A Axarli, and N E Labrou Protein Cross-linking in Food 223 J A Gerrard 10 Chymosin in Cheese Making 241 V V Mistry 11 Starch Synthesis in the Potato Tuber 253 P Geigenberger and A R Fernie 12 Pectic Enzymes in Tomatoes 271 M S Kalamaki, N G Stoforos, and P S Taoukis Part III: Muscle Foods 13 Biochemistry of Raw Meat and Poultry 293 F Toldrá and M Reig v vi 14 15 16 17 18 Contents Biochemistry of Processing Meat and Poultry 315 F Toldrá Chemistry and Biochemistry of Color in Muscle Foods 337 J A Pérez-Alvarez and J Fernández-López Biochemistry of Seafood Processing 351 Y H Hui, N Cross, H G Kristinsson, M H Lim, W K Nip, L F Siow, and P S Stanfield Seafood Enzymes 379 M K Nielsen and H H Nielsen Proteomics: Methodology and Application in Fish Processing 401 O T Vilhelmsson, S A M Martin, B M Poli, and D F Houlihan Part IV: Milk 19 Chemistry and Biochemistry of Milk Constituents 425 P F Fox and A L Kelly 20 Biochemistry of Milk Processing 453 A L Kelly and P F Fox Part V: Fruits, Vegetables, and Cereals 21 Biochemistry of Fruits 487 G Paliyath and D P Murr 22 Biochemistry of Fruit Processing 515 M Oke and G Paliyath 23 Biochemistry of Vegetable Processing 537 M Oke and G Paliyath 24 Nonenzymatic Browning of Cookies, Crackers, and Breakfast Cereals 555 M Villamiel 25 Rye Constituents and Their Impact on Rye Processing 567 T Verwimp, C M Courtin, and J A Delcour Part VI: Fermented Foods 26 Dairy Products 595 T D Boylston 27 Bakery and Cereal Products 615 J A Narvhus and T Sørhaug 28 Biochemistry of Fermented Meat 641 F Toldrá 29 Biochemistry and Fermentation of Beer 659 R Willaert Part VII: Food Safety 30 Microbial Safety of Food and Food Products 689 J A Odumeru 31 Emerging Bacterial Foodborne Pathogens and Methods of Detection 705 R L T Churchill, H Lee, and J C Hall Index 745 Contributors Harry Ako (Chapter 6) Department of Molecular Biosciences and Bioengineering University of Hawaii at Manoa Honolulu, HI 96822, USA Phone: 808-956-2012 Fax: 808-956-3542 Email: hako@hawaii.edu I A Axarli (Chapter 8) Enzyme Technology Laboratory Department of Agricultural Biotechnology Agricultural University of Athens Iera Odos 75 11855 Athens, Greece Dulal Borthakur (Chapter 3) Department of Molecular Biosciences and Bioengineering University of Hawaii at Manoa Honolulu, Hawaii 96822, USA Phone: 808-956-6600 Fax: 808-956-3542 Email: dulal@hawaii.edu Terri D Boylston (Chapter 26) Food Science and Human Nutrition Iowa State University 2547 Food Sciences Building Ames, IA 50011, USA Phone: 515-294-0077 Fax: 515-294-8181 Email: tboylsto@iastate.edu Chung Chieh (Chapter 5) Department of Chemistry University of Waterloo Waterloo, Ontario N2L 3G1, Canada Phone (office): 519-888-4567 ext 5816 Phone (home): 519-746-5133 Fax: 519-746-0435 Email: cchieh@uwaterloo.ca Robin L.T Churchill (Chapter 31) Department of Environmental Biology University of Guelph Guelph, Ontario N1G 2W1, Canada Nieves Corzo (Chapter 4) Instituto de Fermentaciones Industriales (CSIC) c/Juan de la Cierva, 28006 Madrid, Spain Phone: 34 91 562 2900 Fax: 34 91 564 4853 Email: ifiv308@ifi.csic.es C M Courtin (Chapter 25) Department of Food and Microbial Technology Faculty of Applied Bioscience and Engineering Katholieke Universiteit Leuven Kasteelpark Arenberg 20 B-3001 Leuven, Belgium Phone: ϩ32 16 321 634 Fax: ϩ32 16 321 997 Email: christophe.courtin@agr.kuleuven.ac.be N Cross (Chapter 16) Cross Associates 4461 North Keokuk Avenue Apt Chicago, IL 60630, USA Phone: 773-545-9289 Email: n.cross@sbcglobal.net vii viii Contributors Maria Dolores del Castillo (Chapter 4) Instituto de Fermentaciones Industriales (CSIC) c/Juan de la Cierva, 28006 Madrid, Spain Phone: 34 91 562 2900 Fax: 34 91 564 4853 Email: ifiv308@ifi.csic.es J A Delcour (Chapter 25) Department of Food and Microbial Technology Faculty of Applied Bioscience and Engineering Katholieke Universiteit Leuven Kasteelpark Arenberg 20 B-3001 Leuven, Belgium Phone: ϩ32 16 321 634 Fax: ϩ32 16 321 997 Email: jan.delcour@agr.kuleuven.ac.be Juana Fernández-López (Chapter 15) Departamento de Tecnología Agroalimentaria Escuela Politécnica Superior de Orihuela Universidad Miguel Hernández Camino a Beniel s/n 03313 Desamparados Orihuela (Alicante), Spain Phone: ϩ34 674 9656 Fax: ϩ34 674 9609/674 9619 Email: j.fernandez@umh.es or juana.fernaandez@accesosis.es Alisdair R Fernie (Chapter 11) Max Planck Institute of Molecular Plant Physiology Am Mühlenberg 14476 Golm, Germany Patrick F Fox (Chapter 19, 20) Food Science and Technology University College Cork Cork, Ireland Phone: 00 353 21 490 2362 Fax: 00 353 21 427 0001 Email: pff@ucc.ie Peter Geigenberger (Chapter 11) Max Planck Institute of Molecular Plant Physiology Am Mühlenberg 14476 Golm, Germany Email: geigenberger@mpimp-golm.mpg.de Juliet A Gerrard (Chapter 9) School of Biological Sciences University of Canterbury, Christchurch, New Zealand Phone: ϩ64 03 364 2987 Fax: ϩ64 03 364 2950 Email: juliet.gerrard@canterbury.ac.nz J Christopher Hall (Chapter 31) Department of Environmental Biology University of Guelph Guelph, Ontario N1G 2W1, Canada Phone: 519-824-4120 ext 52740 Fax: 519-837-0442 Email: jchall@evb.uoguelph.ca Dominic F Houlihan (Chapter 18) School of Biological Sciences University of Aberdeen, Aberdeen, UK Y H Hui (Editor, Chapter 16) Science Technology System P.O Box 1374 West Sacramento, CA 95691, USA Phone: 916-372-2655 Fax: 916-372-2690 Email: yhhui@aol.com Chii-Ling Jeang (Chapter 7) Department of Food Science National Chung Hsing University Taichung, Taiwan 40227, Republic of China Phone: 886 228 62797 Fax: 886 228 76211 Email: cljeang@nchu.edu.tw Sandro Jube (Chapter 3) Department of Molecular Biosciences and Bioengineering University of Hawaii at Manoa Honolulu, HI 96822, USA Phone: 808-956-8210 Fax: 808-956-3542 Email: sandro@hawaii.edu Mary S Kalamaki (Chapter 12) Department of Pharmaceutical Sciences Aristotle University of Thessaloniki 54124 Thessaloniki, Greece Phone: ϩ30 2310 412238 Fax: ϩ30 2310 412238 Email: mskalamaki@panafonet.gr Alan L Kelly (Chapter 19, 20) Food Science and Technology University of Cork Cork, Ireland Phone: 00 353 21 490 3405 Fax: 00 353 21 427 0001 Email: a.kelly@ucc.ie Contributors G A Kotzia (Chapter 8) Enzyme Technology Laboratory Department of Agricultural Biotechnology Agricultural University of Athens Iera Odos 75 11855 Athens, Greece H G Kristinsson (Chapter 16) University of Florida Laboratory of Aquatic Food Biomolecular Research Aquatic Food Products Program Department of Food Science and Human Nutrition Gainesville FL 32611, USA Phone: 352-392-1991 ext 500 Fax: 352-392-9467 Email: HGKristinsson@mail.ifas.ufl.edu Michael Krogsgaard Nielsen (Chapter 17) Food Biotechnology and Engineering Group Food Biotechnology BioCentrum-DTU Technical University of Denmark Phone: 45 45 25 25 92 Email: mkn@dfu.min.dk N E Labrou (Chapter 8) Enzyme Technology Laboratory Department of Agricultural Biotechnology Agricultural University of Athens Iera Odos 75 11855 Athens, Greece Phone and Fax: ϩ30 210 529 4308 Email: Lambrou@aua.gr Hung Lee (Chapter 31) Department of Environmental Biology University of Guelph Guelph, Ontario N1G 2W1, Canada M H Lim (Chapter 16) Department of Food Science University of Otago Dunedin, New Zealand Phone: 64 479 7953 Fax: 64 479 7567 miang.lim@stonebow.otago.ac.nz Massimo Marcone (Chapter 2) Department of Food Science University of Guelph Guelph, Ontario N1G 2W1, Canada Phone: 519-824-4120, ext 58334 Fax: 519-824-6631 Email: mmarcone@uoguelph.ca Samuel A M Martin (Chapter 18) School of Biological Sciences University of Aberdeen, Aberdeen, UK Vikram V Mistry (Chapter 10) Dairy Science Department South Dakota State University Brookings SD 57007, USA Phone: 605-688-5731 Fax: 605-688-6276 Email: vikram_mistry@sdstate.edu Dennis P Murr (Chapter 21) Department of Plant Agriculture University of Guelph Guelph, Ontario N1G 2W1, Canada Phone: 519-824-4120 ext 53578 Email: dmurr@uoguelph.ca Judith A Narvhus (Chapter 27) Dept of Chemistry, Biotechnology, and Food Science Norwegian University of Life Sciences Box 5003 1432 Aas, Norway Email: judith.narvhus@umb.no Henrik Hauch Nielsen (Chapter 17) Danish Institute for Fisheries Research Department of Seafood Research Søltofts Plads Technical University of Denmark, Bldg 221 DK-2800 Kgs Lyngby, Denmark Phone: ϩ45 45 25 25 93 Fax: ϩ45 45 88 47 74 Email: hhn@dfu.min.dk Michael Krogsgaard Nielsen (Chapter 17) Food Biotechnology and Engineering Group Food Biotechnology BioCentrum-DTU Technical University of Denmark, Bldg 221 DK-2800 Kgs Lyngby, Denmark Phone: ϩ45 45 25 25 92 Fax: ϩ45 45 88 47 74 Email: mkn@dfumin.dk Wai-kit Nip (Associate Editor, Chapters 1, 6, 16) Department of Molecular Biosciences and Bioengineering University of Hawaii at Manoa Honolulu, HI 96822, USA Phone: 808-956-3852 Fax: 808-955-6942 Email: wknip@hawaii.edu ix x Contributors Leo M L Nollet (Associate Editor) Hogeschool Gent Department of Engineering Sciences Schoonmeersstraat 52 B9000 Gent, Belgium Phone: 00 329 242 4242 Fax: 00 329 243 8777 Email: leo.nollet@hogent.be Joseph A Odumeru (Chapter 30) Laboratory Services Division University of Guelph 95 Stone Road West Guelph, Ontario N1H 8J7, Canada Phone: 519-767-6243 Fax Number: 519-767-6240 Email: jodumeru@lsd.uoguelph.ca Moustapha Oke (Chapters 22, 23) Ontario Ministry of Agriculture and Food Stone Road West, 2nd Floor SW Guelph, Ontario N1G 4Y2, Canada Email: Moustapha.oke@omaf.gov.on.ca Gopinadhan Paliyath (Associate Editor, Chapters 21, 22, 23) Department of Plant Agriculture University of Guelph Guelph, Ontario N1G 2W1, Canada Phone: 519-824-4120, ext 54856 Email: gpaliyat@uoguelph.ca José Angel Pérez-Alvarez (Chapter 15) Departamento de Tecnología Agroalimentaria Escuela Politécnica Superior de Orihuela Universidad Miguel Hernández Camino a Beniel s/n 03313 Desamparados Orihuela (Alicante), Spain Phone: ϩ34 06 674 9656 Fax: ϩ34 06 674 9609/674 9619 Email: ja.perez@umh.es D Platis Laboratory of Enzyme Technology Department of Agricultural Biotechnology Agricultural University of Athens Iera Odos 75 11855 Athens, Greece Bianca M Poli (Chapter 18) Department of Animal Production University of Florence Florence, Italy Milagro Reig (Chapter 13) Instituto de Agroquímica y Tecnología de Alimentos (CSIC) P.O Box 73 46100 Burjassot (Valencia), Spain Douglas J.H Shyu (Chapter 7) Graduate Institute of Biotechnology National Chung Hsing University Taichung, Taiwan 40227, Republic of China Phone: 886 228 840328 Fax: 886 228 53527 Email: dshyu@ms7.hinet.net Benjamin K Simpson (Associate Editor) Department of Food Science McGill University, MacDonald Campus 21111 Lakeshore Road St Anne Bellevue PQ H9X3V9, Canada Phone: 514-398-7737 Fax: 514-398-7977 Email: simpson@macdonald.mcgill.ca L F Siow (Chapter 16) Department of Food Science University of Otago Dunedin, New Zealand Phone: 64 479 7953 Fax: 64 479 7567 Terje Sørhaug (Chapter 27) Department of Chemistry, Biotechnology, and Food Science Norwegian University of Life Sciences Box 5003 1432 Aas, Norway Email: terje.sorhaug@umb.no P S Stanfield (Chapter 16) Dietetic Resources 794 Bolton St Twin Falls, ID 83301, USA Phone: 208-733-8662 Email: PStanfld@PMT.org Nikolaos G Stoforos (Chapter 12) Department of Chemical Engineering Aristotle University of Thessaloniki 54124 Thessaloniki, Greece Phone: ϩ30 2310 996450 Fax: ϩ30 2310 996259 Email: stoforos@cheng.auth.gr Index Germ, 568, 578, 581, 616, 618 Giardia, 697, 698 Gliadin, 617, 619, 629 Globulin, 617, 629, 574–575, 578 Gluconeogenesis, 500 Glucono-delta-lactone, 643 Glucan, 568, 570, 660 Glucose 80–82, 84–85, 87, 90–91, 300–302, 324, 330, 381, 382, 617, 621, 660, 664 oxidase, 629 oxidase-catalase enzyme system, 5, 77 phosphate, 382 Glucosidase, 674 Glutamic acid, 629 Glutathione, 75, 77 Glutelin, 574–575, 577 Gluten, 577, 582, 585, 619, 624–625 proteins, 617, 619 rye, 577 wheat, 577 Glutenin, 617, 619, 629 Glycation, 226, 232 Glycerol, 622 Glycerol-3-phosphate dehydrogenase, 666 Glycine 80–82, 629 Glycogen degradation, 357 antemortem exhaustion, 357 asphyxia phenomena, 357 embden-Meyerhof-Parnas pathway, 357 lactic acid accumulation, 357, 365 phosphorylase, 381, 382 rate, 357 reduction in pH, 357 Glycogen, 125, 300, 381, 382, 384 Glycolysis pathway, Glycolysis, 5, 10, 300–302, 325–326, 332, 381, 382, 496, 645, 648, 654, 656, 665 Glycosyl hydrolase family, 579 GMP, 689, 701 Golden rice, 37 Goldfish, 382 Green meat, 364 Broadbill swordfish, 364 Tuna, 364 Grilling, 82 Ground state, 159f Gruel, 624 H HACCP, 689, 700, 701, 702 Hake, 382 Halotolerant lactic acid, 391 Hanes-Wolff plot, 163 HAP See Heat stable alkaline proteinase Hard water, 121–122 755 lime treatment of, 122 permanent hard water, 122 reverse osmosis treatment, 122 temporary hard water, 121 treatment of, 121 Harvesting, 515, 520, 537, 541, 554 Hazard analysis critical control point (HACCP), 738 Health benefits, 611–612 Heat stable alkaline proteinase, 379, 389 Heat-induced markers, 83 Heat-labile, 393 Helicobacter pylori, 699 Heme group, 157 Hemoproteins autoxidation 340 blood 339, 341, 345 bone 345 carbon monoxide 340 cardiac muscle 342 concentration 342, 343, 344 coordination bonds 340 denaturation 340, 341, 344 deoxymyoglobin 340 exsanguination 339 ferric state 340 ferrous state 340 hemoglobin 339, 342, 343, 345 metmyoglobin 340 microbiota 340 myoglobin 339, 340, 344 nitrates 343 Nitrites 340 nitrosomyoglobin 341 oxygen 340, 341 oxymyoglobin 340 protoporphyrin 340, 342 pseudomonas 344 red fibers 339 reducing enzymes 341 Henderson-Hasselbalch equation, 165 Hepatitis A and E, 698, 699 Herring, 388, 390, 391, 392, 393 Heterocyclic amines, 82 Hexanal 77 Hexokinase, 381 Hexose transporters, 660 Hexylresorcinol, 75 Heyns compound, 80 HGA geranylgeranyl transferase (HGGT), 41–42 HGA phytyl transferase (HPT), 41 High activity dry yeast, 621 High fructose (corn) syrup, 8, 21 High performance liquid chromatography (HPLC), 26, 28–31, 168, 169 756 High-energy phosphate degradation, 357 adenosine triphosphate, (ATP),, 359 ammonia, 357 hypoxanthine, 357 impact on seafood flavor, 359 inosine monophosphate, 359 Higher alcohols, 666 aliphatic, 666 aromatic, 667 High-pressure, 77 Hill coefficient, 162, 164 Hill equation, 162, 164 Hill plot, 164 Histamine See Amines poisoning, 4, 17 Histidine, 382 HMF, 83–84 Holoenzyme, 185 Homogeneous nucleation, 109 Homogenization, 599, 608–609 Homogentisic acid (HGA), 41–42 Honeycombing, 358, 371 Honey, 76–77, 82–83 Hordein, 575–577 Horse mackerel, 391 Hull, 568 Humidity, 113 absolute humidity, 113 dew point, 113 measurement, 113 relative humidity, 113 vapor pressure, 111, 113 Hydrate (clathrate), 121 Hydrogen bond, 108–112, 114, 121, 125–126, 179, 180, 182 Hydrogen peroxide, 384 Hydrogen sulfide, 673, 674 Hydrolases, 176, 201 Hydrologic cycle, 131 Hydroperoxide lyase, 15 Hydroperoxides, 88, 91 Hydrophilic substance, 115, 121 hydrophilic interaction, 126 Hydrophobic effect, 121 hydrophobic interaction, 126 Hydroxyglutarate, 670 Hydroxylation, 72–73 Hydroxymethyl furfural, 558, 559 Hydroxyphenyl-pyruvate dioxygenase (HPPD), 41 Hypoxanthine, 18, 383, 384 I IAH1 gene, 669 Ice cream, 129, 474 Ice, 110–113, 128, 130 Index amorphous ice, 111 cubic ice, 111 microwave and ice, 130 other phases of ice, 110 phase transition, 109, 111, 113 triple point, 114 vapor pressure of ice, 111 IDH1 gene, 670 IDH2 gene, 670 ILV pathway, 671, 672 Imitation shark fin, 234 Immobilization, 199, 208–212 adsorption, 197, 199, 200, 208, 209 covalent coupling, 208, 209 cross linking, 208–210 encapsulation, 208, 209, 211, 212 matrix entrapment, 208, 209 procedure, 210 Immobilized cell technology, 675 enzymes, 208 sulfhydryl oxidase, 233 Immunological methods, 171 Immunomagnetic assays, 735 IMP See Inosine monophosphate Inclusion bodies, 192, 195 Indian mackerel, 390 Indicator of freshness, biochemical, 359, 365 collagen degradation, 366 degradation of myofibrillar proteins, 366 dimethylamine formation, 366 drop in pH, 365 fatty acid accumulation, 366 hypoxanthine, 359, 365 inosine monophosphate, 359 K1 value, 366 K-value, 365 lactic acid formation, 365 nucleotide catabolism, 365 textural changes, 366 Total volatile base, 359, 366 tyrosine accumulation, 366 xanthine oxidase, 365 Indirect assays, 167 Indolepyruvate, 667 Induced fit hypothesis, 184, 186 fit theory, 156, 159 strain, 159 Infant formula, 82–83, 91, 475–476 Infrared methods, 27 Inhibitors, 189, 191, 201, 574–575, 578–580 ␣-amylase, 575, 578 ␣-amylase/subtilisin, 578 cereal trypsin/␣-amylase, 578 Index defense (D-type), 578 Kunitz, 578 regulation (R-type), 578 endoxylanase, 575, 579 Secale cereale L xylanase inhibitor (SCXI), 579 Triticum aestivum L xylanase inhibitor I (TAXI I), 579 xylanase inhibiting protein (XIP), 579 enzymatic browning, 18 irreversible, 189 protease, 575, 580 serpins, 580 subtilisin inhibitor, 580 trypsin inhibitor, 580 reversible, 189, 191 competitive inhibitors, 190, 191, 209 inhibition constant ki, 189–191 noncompetitive, 190, 191 uncompetitive, 190, 191 Initial rate, 160, 161 Inorganic salts, 75 Inosine, 18, 382, 383, 384 monophosphate (IMP), 382 Instant active dry yeast, 621 Institute of Food Technologists (IFT), 3, 20 recommended Undergraduate Course Requirements, Insulin, 156 Inteins, 212 International commission on Enzymes, 135 organization for Standardization Culturing Method 11290–1, 718–719 Union of Biochemistry and Molecular Biology, (IUBMB), 135 Nomenclature Committee of the IUBMB, (NC-IUBMB), 135 Union of Biochemistry, (IUB), 135 Union of Pure and Applied Chemistry, (IUOAC), 135 unit, 171 Invertase, 263 Ion exchanger, 197 carboxymethyl, 197, 199 diethylaminoethyl, 197, 199 methyl sulfonate, 197 quaternary ammonium, 197, 199 Ionic bonds, 179, 182 Ionizing groups, 165 Ion-selective electrodes, 30 Iron, 42–45, 48, 625 deficiency, 42–43 Isoamyl acetate, 669, 669 Isoamyl alcohol acetyltransferase, 669 Isoamyl alcohol, 667, 669 Isobutanol, 666, 667 Isoflavonoids, 45–47 757 genistein, 46–47 isoflavone synthase gene (IFS1/IFS2), 47 naringenin, 47 Isomerases, 176 Isoosmotic, 381 Isopentyl diphosphate, 16 Isoprenoids, 506 J Japanese anchovies, 391 Japanese flounder, 388 Journal of Food Biochemistry, 4, 21 Journal of Food Science, 21 K K value, 384 kcat, 161 kcat/Km, 161, 165 Keto acid, 667 Ketobutyrate, 671 Ketoglutarate dehydrogenase, 670 Ketoglutarate, 670 Ketoisocapric acid, 667 Ketoisovaleric acid, 667 Ketones, 624, 655–656 Keto-␣-methylvaleric acid, 667 Km, 161 Kojic acid, 75–76 Krausen, 672 Krebs cycle, 665, 670 Ks, 161 L Lactase, 4, 5, 20, 21, 73, 80–82, 84, 91–92, 596–598, 602, 604–605 See also Phospho-␤-galactosidase Lactate, 380, 381, 382, 597, 670, 677 dehydrogenase, 301, 311, 380, 382 Lactic acid bacteria, 595–599, 602, 604, 606, 624–630 heterofermentative, 597–598, 606 homofermentative, 597–598 Lactic acid, 300–302, 304, 322, 595, 597, 598, 602, 605, 610–611, 643–644, 648 Lactobacillus, 597–598, 604, 609–612, 625–630, 633 alimentarius, 629 brevis, 616, 626, 629 delbrueckii, 626 hilgardii, 629 plantarum, 626 sanfranciscensis, 625–629 Lactococci, 596–597, 604, 606, 608–609 Lactococcus lactis, 54, 629 Lactose free milk, 4, 21 intolerance, 598 Lactuloselysine, 80 758 Index L-ascorbic acid, 75 Latex agglutination assays, 737 LDH See Lactate dehydrogenase Lecithin, 91 LEU4 gene, 669 Leuconostoc, 597–598, 604, 606, 608–609 Leuconostoc citreum, 629 Lg-ATF1 gene, 669 Ligases, 176 Limonin, 15 Lineweaver-Burk plot, 162 Lipase, 304–306, 318–319, 327–330, 332, 605, 618, 629, 648 Lipids, 27, 122, 295, 298–299, 489, 596, 602, 618, 665, 668, 670 browning, 88–90 degradation in seed germination, 13 fat crystallization, 608 fatty acids, free, 606 hydrolysis of, 123 metabolism, 503 oxidation, 88, 327, 329, 331–332, 390, 403, 409, 412 total lipid content analysis, 27 infrared method, 27 organic solvent extraction, 27 Soxhlet method, 27 supercritical fluid extraction, 27 types of fatty acids analysis, 28 gas chromatography, 28 high performance liquid chromatography (HPLC), 28 IUPAC-AOC-AOAC method, 28 Lipofuscins, 88 Lipolysis, 304, 311, 327–332, 598, 605–606, 644–645 Lipophilic substance, 115 Lipoxygenase, 12, 15, 88 Liquid H2O, 109 See also Water boiling point, 113 density, 112 hard water, 121 phase transition, 109, 111, 113 properties of water, 109, 112 self-ionization of water, 115 triple point, 114 vapor pressure curve, 113 Listeria monocytogenes, 53, 292, 694, 696, 707, 715–716, 719, 722, 724, 726, 729, 732, 735, 737 listeriosis, 696 listerolysin, 715 outbreaks, 715 pathogenicity, 715 properties, 715 source, 715 Lobry de bruyn-Alberda van Ekenstein transformation, 83 Lock and key theory, 156 Long-chain polyunsaturated fatty acids, 353, 360 Lowry method, 26 Lyases, 176 Lycopene ␤-cyclase, 37 Lysine, 80–83, 88, 90, 629 Lysosome, 388, 390, 389, 390 Lysozyme, 54 M Mackerel, 388, 390, 391, 392 Maillard reaction, 78–83, 88, 458, 624 Maize, 615–636 MAL gene, 660, 661 posttranslational control, 664 posttranslational modification, 664 Malate, 670 Maltase, 661 Maltilol, 87 Malting, 660, 661, 662 germination, 662 kilning, 662 steeping, 662 Maltogenic ␣-amylase, 20 Maltose, 80, 84, 260, 555, 561, 617, 621–622, 625, 660, 664 metabolism, 660 transporter, 660 Maltotetraose, 664 Maltotriose, 660, 664 metabolism, 660 Maltulose, 560, 561 Maltuloselysine, 80 Masa madre, 626 Mashing, 662 Masre, 626 Mass transfer limitation, 675 Matrix metalloproteinases, 388 Maturation, 663, 672, 675 Meat, 82, 291, 315 pigments biological 338, 340 carotenes 338, 339 concentration 342, 343, 344 cytochromes 338,339, 340, 342 damage 338 heme 338, 340 Parma ham 342 photooxidation 345 tenderization, 9, 10, 21 Mediterranean sausages, 641 Melanins, 18 Melanoidins, 71, 80, 89, 226, 229 Melanosis, 365 Melondialdehyde, 233 Mesophilic cultures, 600–601, 604 Index MET gene, 673 Metabolic engineering, 213 Metabolism of complex carbohydrates, lactose in cheese production, organic acids in cheese production, Metal ion, 157 cofactors, 185 Metalloprotease, 575, 579–580 Methionine, 81–82, 88, 90 Methods, detecting foodborne pathogens, 717–738 culture-dependent enrichment methods, 717–718 immunoassay-based methods, 730–737 enzyme-linked immunosorbent assay (ELISA), 732 fluorescent labeled immunoassays, 735 immunomagnetic assays, 735 latex agglutination assays, 737 surface plasmon resonance (SPR), 735, 737 types of antibodies used, 730, 732 non-nucleic acid-based automated methods, 718 microbial Identification System (MIS), 718 microLog System, 718 replianaylzer system, 718 VITEK system, 718 nucleic acid-based methods, 718–726 DNA microarrays, 726 multiplex PCR, 724 nucleic acid sequence-based amplification (NASBA), 26 polymerase chain reaction (PCR), 719–726 real-time PCR, 724 reverse transcription-PCR (RT-PCR), 724 pathogen subtyping and verification methods, 726–730 amplified fragment length polymorphism (AFLP), 727 fluorescent in situ hybridization, 729–730 pulse-field gel electrophoresis, 729 randomly amplified polymorphic DNA, 727, 729 restriction fragment length polymorphism (RFLP), 727 ribotyping, 729 Methods, gene transfer, animals, 47–51 embryonic stem cell transfer, 47 microinjection, 47, 49, 50, 52 nuclear transfer, 47–48 viral vector infection, 47 plants, 36–47 Agrobacterium-mediated transformation, 36–38, 42, 45, 47 gene gun, 36 Methylbutanal, 623, 666, 667 Methylglyoxal, 85 Mevalonate, 16 Michaelis-Menten constant, 380 equation, 156, 161 plot, 162 Microarrays, 212 Microbial Identification System (MIS), 718 Microbial protease, 12 MicroLog System, 718 Microorganisms See also Starter cultures Candida See Yeasts Clostridium, 642, 651 Debaryomices See Yeasts Escherichia coli, 651 Kocuria varians, 650 lactic acid bacteria, 322, 648, 650 Lactobacillus, 648, 650 Listeria, 651 Micrococcaceae, 328, 644–645, 653 pathogenic, 595, 599, 609 Pediococcus, 648 Penicillium See Molds Safety, 687–703 salmonellae, 650–651 spoilage, 595, 599 Staphylococcus, 328, 332, 650–651 Microwave, 129 cooking, 129 freeze dry, 130 heating, 88 interaction with ice, 130 interaction with water, 129 microwave spectroscopy See Spectroscopy Milk, constituents lactose, 426–431 crystallization, 428–429 derivatives, 430 fermentation, 431, 461 food applications, 429 heat-induced changes, 458 hydrolysis, 469 nutritional aspects, 430 production from whey, 467–468 properties, 427–429 solubility, 427–428 structure, 426–427 lipids, 431–437 conjugated linoleic acid, 432–433 creaming, 435–436 definition, 431 fat-soluble vitamins, 437 fatty acid profile, 432 globule stability, 435 homogenization, 436 hydrolysis, 471–472 milk emulsion, 434–435 oxidation, 436–437, 473 759 760 Milk, constituents (continued) products, 472–473 rancidity, 436 rheological properties, 434 triglycerides, 433–434 proteins, 437–447 acid casein, 468–469 bovine serum albumin, 444 casein micelles, 441–444 casein products, 468–469 enzymes, 446–447, 458–459 heat-induced changes 456–458 heterogeneity, 438 hydrolysates, 474–475 immunoglobulins, 444 minor proteins, 445–446 properties, 438–439 rennet casein, 468–469 transglutaminase, 470–471 whey proteins, 441, 467 salts, 447–448 vitamins, 448–449 Milk, general considerations, 82, 83, 91, 596, 611 acidophilus, 611 composition, 426, 595, 596 lipid, 596 milk fat globule, 599 powders, 460–461 products, 453–483 production, 425 variability, 426 Milk, processing, 453–483 enzymatic conversion, 469–473 evaporation, 459 heat stability, 457 high pressure treatment, 476–477 history, 454–456 membrane processing, 467, 469 pasteurisation, 455, spray-drying, 460 thermal processing, 454–459 ultra-high temperature milk, 456–457 Millet, 615 Milling, 581–582, 586, 661, 662 cleaning and tempering, 581 Europe, 581 pin milling, 581 roller milling, 581 extraction rate, 581–582 North America, 581 quality, 582 arabinoxylan, 582 protein, 582 Mineral analysis, 29 ash content, 29 Index dry ashing, 29 low temperature plasma ashing, 30 wet ashing, 29 atomic absorption spectroscopy, 30 atomic emission spectroscopy, 30 ion-selective electrodes, 30 losses in food processing, 29 macronutrients, 29 trace minerals, 29 Model systems, 80, 84, 86, 89–91 Modified-atmosphere packages, 88 Moisture, 294, 641 Molasses, 620 Molds, 328, 625, 644–645 Mole fraction, 115 Molecular flexibility, 380 Monophenol oxidase, 72 Mother sponge, 626 Mucor, 691 Mullet, 390 Multicatalytic, 389 Multiplex PCR, 724 Muscle growth, hyperplasia, 49 hypertrophy, 49 Mutagenesis, 202, 204–207 directed evolution, 202, 203, 207, 208, 213 error-prone PCR, 207 DNA shuffling, 207 ITCHY, 207 random-mutagenesis, 202, 207 RPR, 207 step, 207 Rational design, 202, 203, 207 deletion mutants, 205 domain swapping, 205 insertion/fusion mutants, 205 site-directed mutagenesis, 202, 204, 205, 207 truncation mutants, 205 Mycotoxins, 651 Myocommata, 386, 387 Myofibrillar proteins, 294–297, 316–317, 320–323, 389 Myoglobin, 296–297, 389, 652 Myosin, 382, 384, 387, 392 ATPase, 382 cross-linking, 12 Myostatin, 48–49 Myotome, 386 N Naringenin chalone biosynthesis, 16 Native gel electrophoresis, 170 Natural variation, 264 Nebulin, 388 Nitrate reductase, 645, 652–653 Index Nitrate, 324, 330, 643, 646, 650 See also Nitrite Nitric oxide myoglobin, 652 Nitrite, 324, 330, 642–643, 646, 650–652 NMR, 156 Noncompetitive inhibition, 160 Nonenzymatic browning, 71, 78–91 Nonprotein nitrogenous (NPN) compounds, 358 amount in different species, 358 amount in red meat, 358 amount in white meat, 358 components, 358 degradation, 358 total volatile base, 359 Non-starch polysaccharides, 568, 570 Northern sausages, 641 Norwalk/Norwalk-like viruses, 698,699 Nucellar epidermis, 568 Nuclease, 393 Nucleation, 109 Nucleic acid sequence-based amplification (NASBA), 26 Nucleoside phosphorylase, 383 Nucleosides, 300–304, 325–326, 653–654 Nucleotidase, 383 Nucleotides, 300–304, 310, 325–326, 381, 383, 384, 386, 653–654 Nutrition, 585 dietary fiber, 585–586 Nuts 82 N-␣-benzoylarginine-p-nitroanilide (BAPA), 579 O Octene-3-ol, 623 Oil sardine, 390 Omega-3 fatty acid, 353, 356, 360 Onion juice, 77 Onion oil, 77 Organic acids, 491 biosynthesis, 670 Organic solvent extraction, 27 Osmolyte, 381 Osmotic stress, 622 Oxalic acid, 74 Oxidation of diphenol, 72–73 Oxidation, 306–307, 655–656 Oxidative enzymes, 4, 319–320 Oxidized lipids, 88–90 Oxidoreductases, 176, 201 Oxygen, 263, 665, 673 Oxygen-scavenging film; 88 Oxygen-sensing methods, 171 Oxyresveratrol, 77 P Pacific rockfish, 388 Pacific whiting, 391, 393 761 Pancreatic elastase, 12 Pandoro, 626 Panettone, 626 Papain, 10, 12 Papaya latex extract, 77 Paper chromatography, 169 Parasite, 697 mucor, 691 Particle size distribution, 280, 281 Pasta, 82–83 Pasteurization 76, 82, 599, 606, 608–609 Pathogen detection methods, 57–61 digoxygenin-ELISA (DIG-ELISA), 59 ELISA, 58 PCR, 58 protein misfolding cyclic amplification (PMCA), 61–62 Pathogens, 651, 691 P-cyclodextrin, 75 PE, 90–91 Pectate lyase, 277 Pectic enzymes, 4, 5, 271 Pectic substances, 271, 273 Pectin network, 271 Pectinmethylesterase, 276 food processing, 279 genetic engineering, 278, 279 high pressure inactivation, 284 thermal inactivation, 283 Pelagic fish, 17, 352–353 Penicillium, 606, 691, 698 Pentanedione, 671, 675 Pentosans, 616, 625, 660 Pentose phosphate pathway, 501 Pentosidine, 226, 232 Pepsin, 392, 598 Pepsins, 10 Peptidase, 306, 317–318, 320–325, 618, 629 Peptide bond, 176–179, 212 Peptide mass fingerprinting, 403, 405–406 MALDI-TOF mass spectrometry, 405 tandem mass spectrometry, 406 Peptides, 72, 76–78, 88, 295, 297, 317–318, 322, 653– 654 See also Proteolysis bitter, 605 Perfringolysin (PLO), 716 Pericarp, 568, 571, 578 Perimysium, 386, 387 Peroxide, 651 pH, 165, 325, 598, 605 pH and pOH, 117 Phagemids, 191 Phase diagram, 109, 111, 113–114, 128 state diagram, 128 two-component system, 128 Phenol oxidase, 365 762 Phenol oxidation, 71 Phenolases, 73 Phenoloxidase, 71 Phenylethanol, 667 Phenylethyl acetate, 7, Phenylketouria (PKU), 157 Phenylpyruvate, 667 Phosphatidylethanolamine (PE), 90–92 Phosphoglucomutase, 382 Phospholipase, 390 See Lipases Phospholipids, 50, 299, 307, 318, 327–328, 389, 618 Phosphorylation, 158 Phospho-␤-galactosidase (lactase), See also Lactase pH-stat methods, 171 Phytase, 19, 625 Phytic acid, 43–44, 625 Phytoene, 37 desaturase (crtI gene), 37, 56 synthase (psy gene), 37 Phytyl diphosphate (PDP), 41 Pickled (marinated) fish, 370 Pigment analysis, 31 anthocyanins, 31 betaines, 32 carotenoids, 31 chlorophylls, 31 high performance liquid chromatography, 31 lipid soluble pigments, 31 reverse-phase chromatography, 31 water soluble pigments, 31 pKa, 165 Plant promoters, 35S CaMV promoter, 37–39, 41–42, 45, 47 maize ubiquitin (Ub) promoter, 39 rice glutelin (GluB-1) promoter, 43 rice glutelin (Gt1) promoter, 37, 45 shrunken (Sh2) promoter, 39 starch synthase promoter, 45 Plasmids, 191, 195, 196, 206 Plasmin, 10, 605–606 Poikilotherme, 380 Polar molecule, 106, 121 hydrophilic substance, 121 Polarographic methods, 171 Polygalacturonase, 275, 493 food processing, 278 genetic engineering, 277, 278 high pressure inactivation, 284 thermal inactivation, 283 Polymerase chain reaction (PCR), 719–726 Polypeptide, 157 Polyphenol oxidase, 18, 71–78, 85, 87 browning, 18 Polyunsaturated fatty acids, 88 Porridge, 624 Index Post-translational modifications, 192, 193, 195 Potato, 72, 75, 82, 85, 253 Potrykus, I., 37 Poultry, 291, 315 PPO See Polyphenol oxidase Prawn, 390 Pressing, 604 Primary sequence, 156 Prion proteins (PrP), 60–61 PrPc, 60–61 PrPSc, 60–61 Probiotic bacteria, 612, 635–636 Processing, 537, 539, 540, 541, 542, 543, 544, 545, 547, 549, 550, 551, 552, 553, 554 blanching, 537, 539,541, 542, 543 canning, 537, 539, 541, 543, 544, 553 comminution, 537, 545, 546 cutting, 537, 541, 542, 544, 552 deaeration, 537, 545, 546 exhausting, 537, 541, 544 extraction, 537, 545, 546 filling, 537, 541, 544 grading, 537, 541, 542, 544, 551 homogenization, 537, 545, 546 inspection, 537, 544 operations, 537, 541, 544, 551 peeling, 537, 541, 542, 544, 550, 551 preprocessing, 537, 541 procedure, 537, 543 salting, 537, 545, 546 sorting, 537, 541, 542, 544, 545, 550, 551 trimming, 537, 539, 542, 544, 545 washing, 537, 539, 541, 542, 544, 545, 550, 551 Production of ammonia from trimethylamine and its N-oxide, 17 ammonia from urea, 18 biogenic amines, 17 formaldehyde from trimethylamine and its N-oxide, 17 starch sugars, starch syrups, Prolamin, 574, 577 Proline, 629 Propanol, 666, 667 Propionibacteria, 606 Prosthetic groups, 157, 185 Protease, 575, 577, 579–580 aminopeptidase, 579 aspartic protease, 575, 579–580 carboxypeptidase, 579 cysteine protease, 575, 579–580 endoprotease, 579 exoprotease, 579 inhibitor, 575, 579–580 serpins, 580 subtilisin inhibitor, 580 Index trypsin inhibitor, 580 metalloprotease, 575, 579–580 N-␣-benzoylarginine-p-nitroanilide (BAPA), 579 serine protease, 575, 579–580 Proteases, 4, 10, 599, 605 See also Proteinases Proteasome, 317, 379, 389 Protein analysis, 25–27 by detecting or quantifying specific protein component, 26 electrophoresis, 26 high performance liquid chromatography, 26 reverse-phase chromatography, 26 size-exclusion chromatography, 26–27 by determining nitrogen content, 25 biuret procedure, 25 Lowry method, 26 Protein cross-links (cross-linking), 223–235 AGE protein cross-links, 226 covalent links, 225 cross-links derived from dehydration, 225 cross-links derived from the Maillard reaction, 225– 226 cross-links derived from tyrosine, 225 cross-links formed via transglutaminase catalysis, 229– 230 disulfide cross-links, 225, 232–233 effect on food quality, 226 in foods, 224 intramolecular cross-links, 224 intramolecular cross-links, 224 isopeptide cross-links, 230 lysine-lysine cross-links, 226, 229 maillard-related cross-links, 229 manipulation during food processing, 230–235 chemical methods, 231–232 cross-linking agents, 231 enzymatic methods, 232–233 on food quality, 233 on food texture, 233 on functional properties of food, 232 relation to food deterioration, 233 Protein, 119, 122, 124, 357, 491, 568, 574–580, 582, 585, 596, 616–618, 624 amino acid, 118 antifreeze protein, 116 arrays, 212 bread-making, 585 coagulation, 598, 602 data bank (PDB), 156 degradation, 357 denaturation, 609 denature of, 121 disulfide isomerase (PDI), 232–233 emulsifying capacity, 580 foam-forming capacity, 580 763 folding of, 121 hydrolysis of, 124 hydrophilic protein, 121 hydrophobic protein, 121 membranes bond protein, 116 milling, 582 myofibrillar proteins, 357, 358 loss of firm texture, 358 loss of functional characteristics, 358 loss of integrity, 358 nonstorage, 574–575 osborne fractionation, 574–575 proteolysis, 598, 605–606, 610 salting in, 122 salting out, 122 sarcoplasmic proteins, 357 quality degradation, 357 solubility, 122 storage, 574–575, 577 stroma (muscle) proteins, 357, 358 collagen degradation, 358 textural changes, 358 synthesis of, 124 Proteinases, 304–306, 316–317, 358, 618, 629, 650 Protein-glutamine ␥-glutamyltransferase (transglutaminase), 12 Proteolysis, 304, 311, 320–325, 332, 629, 644–645, 650, 654 during cheese fermentation, 12 in cheese, 248 in animal tissues, in germinating seeds, 12 Proteomics, 401–16 allergen characterization, 416 antemortem metabolism, 409–10, 414 methodology, 401, 403–5 post mortem metabolism, 410 quality involution, 409 species authentication, 414–16 Prusiner, S., 60 PSE meat, 302, 304–305, 311 pork, 642 Pulsed electric field processing, 88, 729 Putrescine, 18 See Amines Pyroglutamate, 670 Pyrraline, 80 Pyrroles, 80, 89–91 Pyruvate, 665, 666, 670 Q QTL analyses, 265 Quality, 537, 539, 540, 541, 542, 543, 544, 545, 546, 551, 552, 553, 554 attributes, 537, 545, 546, 552, 554 764 Quality, (continued) consumption, 537, 538, 551 control, 546, 547, 552, 553, 554 definitions, 537, 550 index of seafood acceptability, 18 kinetic, 546, 548 minimally processed, 537, 550, 552, 553, 554 physical, 537, 546, 547, 548 physicochemical, 537, 546, 547, 549, 552 stability, 537, 546, 547, 548, 549, 550 Quantum yield (Q), 168 Quenching, 168, 169 R Radioactivity, 169 Radioisotopes, 169 Radiometric methods, 169 Rainbow trout, 388, 390 Randomly amplified polymorphic DNA, 727, 729 Rate-limiting state, 158 Rayfish, 390 Real-time PCR, 724 Recombinant bovine growth hormone (rBGH), 50 Recombinant DNA technologies, 599 Red muscle, 381, 389, 390 Redox potential, 323, 329 regulation 257, 263 Reduced glutathione, 75 Reducing pentoses, 80 Reducing sugar, 78, 80–82, 555, 556, 557 Reduction of phytate in cereals, 19 Reductones, 85–86 Reinheidsgebot, 677 Reinzuchtsauerteig, 626 Rennet, 242, 598–599, 602, 605 manufacture, 242 genetic technology, 242 paste, 243 substitutes, 244, 393 Replianaylzer system, 718 Resonance energy transfer (RET), 169 Rested harvest, 382, 384 Restriction fragment length plymorphism (RFLP), 727 Reveratrol (resveratrol), 16, 77 Reversephase chromatography, 26, 30–31 staining, 171 transcription-pcr (rt-pcr), 724 zymography, 171 Rhizopus, 691 Ribose, 81, 89 Ribotyping, 729 Ribozymes, 156, 175 Rice, 615–636 Index transgenic iron, 43–44 lysine, 45 vitamin A, 37 Rigor mortis, 384, 385, 387 Ripening, 379, 390, 391, 602, 605–606, 642, 648–651 accelerated, 606 hormone, RNA catalysts, 175 See also Ribozymes Roasting, 82–83 Roe, 370, 379, 392 aminopeptidase activity, 370 cathepsin-D-like activity, 370 Rohu, 390 Rye, 567–586, 615, 625 classification, 567 constituents, 568, 582, 583 non-starch polysaccharides, 568, 570 proteins, 568, 574–580 starch, 568–570 kernel, 568 processing, 581 bread-making, 582–585 feed, 585 food products, 585 fractionation, 585 industrial uses, 585 milling, 581–582 production, 567 S Saccharomyces, 691 Saccharomyces cerevisiae, 620–623 Safety, 651–652 Salmon, 388, 389, 390, 392 canned salmon, 371 pigments in, 365 Salmonella, 692, 694, 699, 708–713, 724, 729 infections, 713 S enterica subspecies enterica, 708 S enteriditus, 713 S typhi, 707, 713 S typhimurium, 708, 724, 735 salmonellosis, 696 symptoms, 713 Salt, 324, 329–330, 332, 642–643, 653–654 Salt-cured fish, 379, 391 Salting, 379, 386, 390–391, 605 San Francisco sourdough, 626 Sarcocystis, 697, 698 Sarcolemma, 387 Sarcomere, 387 Sarcoplasmic proteinases, 389 Sarcoplasmic proteins, 297, 310, 322–323 Saturation-type model, 156 Index Sausages, types of French saucisson, 642 German teewurst, 642 Hungarian salami, 642 Italian salami, 642 Lebanon Bologna, 642 pepperoni, 642 Spanish salchichón, 642 summer sausage, 642 Scalding, 604 Schiff’s base, 80, 91 Scombroid poisoning, 4, 17 Seafood, 351–378 consumption recommendations, 357 enzymes, 379–400 freezing and frozen storage, 366–370 degradation of trimenthylamine oxide, 369 dehydration effect, 367 ice crystal effect, 367 lipid oxidation and hydrolysis, 368–369 protein denaturation, 367 reaction of protein with intact lipids, 368 reaction of proteins with oxidized lipids, 368 solute concentration effect, 368 glycogen in, 352 health attributes, 352–353, 356–357 lipids in, 371 fatty species, 359 lean species, 359 low fat species, 359 medium fat species, 359 nitrogenous compounds in, 371 nutritive composition of major groups, 352–356 effect of processing, 353 macronutrients, 352, 353 micronutrients, 353, 356 pigments in, 371 processing methods for, 371 quality indices in, 371 quality problems, 361–363 minimization of lipid-derived problems, 362–363 novel processing methods, 361–362 related to lipids in fish, 361–363 Secale cereale L xylanase inhibitor (SCXI), 579 Secalin, 574–577, 580 aggregation behavior, 576, 577 amino acid composition, 574–576, 580 conformation, 575, 577 high molecular weight (HMW), 574–575, 577 low molecular weight (LMW), 575 molecular weight, 575–577 S-poor, 574, 576 S-rich, 574, 575 ␥-secalin, 575 40k ␥-secalin, 575–577 765 75k ␥-secalin, 575–577 ␥-secalin, 575–577 Secondary plant products, 506 Seed lipids, 13 Semidry-fermented sausages See Fermented sausages Sepharose, 199 Sequential model for allosteric enzymes, 156 Serine protease, 575, 579–580 SFA1 gene, 667 Shaping, 604 Shark, 358 ammonia, 358 urease, 358, 359 Shelf life, 690, 691 Shellfish, 380, 381, 386, 390, 391 Shiga disentiriae shiga toxin, 714 Shiga toxin (Stx), 57, 60, 714 Shigella, 695, 729 Shortening, 624 Shorts, 570, 580 Shrimp, 365 canned, 371 dried, 371 SI unit, 171 Sigmoid curve, 162 Size exclusion chromatography, 26–27 Smoke-cured seafood, 371 cold-smoked fish, 370 Smoking, 643, 651 SNF1, 257 Sodium chloride, 75–76 See also Salt Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), 170 Sorbitol, 87 Sorghum, 615 Sour cream, 598, 608–609 Sourdough, 582–583 acetic acid, 582 bread, 624–630 heterofermentative lactic acid fermentation, 582 homofermentative lactic acid fermentation, 582 lactic acid, 582 microbiology, 625 one-stage process, 582 processes, 626–627 starters, 625–626 three-stage process, 582 two-stage process, 582 Soxhlet extraction, 27 Spacer, 199 Spawning, 379, 389 Specific activity, 171 Specificity, 175, 176, 199, 201, 202, 212 regiospecificity, 175 stereospecificity, 175 766 Spectrofluorometric methods, 167, 168 Spectroscopy, 106 electromagnetic radiation, 106 energy level, 106 IR, infrared, 106 microwave, 107, 129 Planck, Max, 106 UV, ultraviolet, 107 visible light, 107 Spent grains, 661 Spiced sugar-salted, 390 Spices, 328, 643 Spoilage, 379, 383, 384, 385, 389, 690, 691 spoilage organisms, 691 Squid, 364, 393 Stability, 176, 179, 192, 194, 197, 199, 204, 208, 210 Staling, 624–625 Staphylococcus aureus, 692, 695, 697, 716–717, 732 enterotoxin A, 717 S aureus enterotoxins, 717 Alpha-hemolysin, 717 sources, 716 symptoms, 717 Starch, 125, 568–570, 578, 582–584, 616, 622, 625, 660 amorphous, 569 amylopectin, 125 amylose, 125 animal starch See Glycogen blocklets, 569 bread-making, 583 crystalline, 569 degradation, 258, 259, 494 gelatinization, 569–570, 583, 624 differential scanning calorimetry (DSC), 569 enthalpy, 569 temperature, 569–570, 583 gelation, 570 growth rings, 569 importance, 253 industrial uses, 254 lamellae, 569 modification, 265 optical birefringence, 569 particle size distribution, 569 pasting, 570 retrogradation, 570 structure, 254 synthesis, 255, 256 X-ray diffraction, 569 yield, 260 Starch-sugar interconversions, 495 Starter cultures, 322, 328, 643–646, 648 State diagram, 128 See Phase diagram equilibrium solubility curve, 128 Index eutectic point, 128 glass transition temperature, Tg, 129 Steady state, 128 model, 161 rate, 160 Sterilization, 82 Sterol esters, 618 Sterols, 665 Stilbenes, 16 Stokes shift, 168 Storage 78, 82–84, 87–88, 90 Strawberry flavor, 15 Streptococci, 596–598, 604, 609–611 Stress, 382 Structure 176–179, 181–183, 187, 188, 190, 201, 204, 207 motifs, 179, 181, 204 primary, 176–179 quaternary, 181 secondary, 178, 179, 181 super secondary, 179 See also motifs tertiary, 179 three-dimensional (3d), 178, 179, 182, 202, 204, 205 Stuffing, 647 Subcritical water, 113 Subcutaneous yellowing of flesh, 364 Substrate binding site, 182, 185 Subunit, 181 Succinate, 622 Succinate dehydrogenase, 670 Sucrose, 104, 255, 622, 660, 664 enthalpy of combustion, 104 Sugar signal, 258 Sugars 76, 80, 82–85, 87 Sugar-salted herring, 389 Sulfate, 673, 674 Sulfhydryl amino acids, 75 (thiol) oxidase, 233 Sulfites, 75, 87, 673, 674 agents, 18 dioxide, 671, 673 reductase, 673 Sulfurous odor of cruciferous vegetables, 15 Supercritical fluid extraction, 27 Supercritical water, 113, 114 Surface plasmon resonance (SPR), 735, 737 Surfactant, 624 Surimi, 12, 379, 391, 392, 393 Surrogate marker living test, 61 Swiss-MODEL sever, 156 Swiss-PDB Viewer, 156 Syneresis, 599, 602, 609, 611 Syrups, 661 Index T Tagatose, 82 Taste, 320, 645, 650, 653–654 TCA cycle, 665, 670 Tea, 71, 75, 82 Technological processes, 88 Teleost, 381 Temperature, 80–85, 87, 89–91, 165 Testa, 568, 571, 616 Texture of tomato products, 277, 280, 284, 286 Texture, 305, 309, 320, 606, 608, 643, 653 Thawing, 384 Therapeutic enzymes, 191, 197, 208, 212 Thermal stability, 380 Thermal-processed seafood, 370 changes in tissue structure, 370 crabmeat extraction, 370 mild heating, 371 oxidation of myoglobin, 370 oxidation of oxymyoglobin, 370 protein coagulation, 370 Thermophilic cultures, 600–601, 604 Thin-layer chromatography (TLC), 169 Thiol compounds, 75, 77, 87 Threonine, 81 Ti plasmid (T-DNA), 36 disarmed ti plasmid, 36 engineered T-DNA, 36 vir gene, 36 Tilapia, 388, 389 Tissue degradation/spoilage, macro-structure, microstructure, Titin, 388 Titration, 118 equivalence point, 118 half equivalence point, 118 titration curve, 118 TMA/TMAO See Trimethylamine Tocopherol, 40–42 Tomato, 546, 547, 551, 553, 554 canned, 537, 543, 544, 545, 551, 553 genetically modified, high pressure inactivation, 284 juice processing, 537, 544, 545, 546, 547, 548, 549, 550, 551 thermal inactivation, 283 transgenic tomatoes, 21 Total volatile base, 359, 366 Toxoplasma, 697, 698, 707 Trans-2-nonenal, 373 Transaminase, 12, 176, 187, 201, 606 Transamination, 667 767 Transgenic approaches 253, 260, 265 detection, 56–57 DNA artificial coding, 57, 58 real-time quantitative PCR (RT-PCR), 57 TaqMan probes, 57 organisms cattle, 48–49 fish, 51–53 microorganisms, 53–56 plants, 36–47 poultry, 50–51 swine, 49–50 Transglutaminase (Protein-glutamine ␥-glutamyltransferase), 12, 229–230, 233, 392 activity in seafood processing, 12 cross-linking occurrence`, 234 microbial transglutaminase, 233 operation pH and temperature ranges, 233 Streptoverticillium mobaraense, 233 uses in food, 233–235 Transition state, 158, 159, 181, 183, 184 Transmissible spongiform encephalopathies (TSEs), 60 Creutzfeldt-Jakob disease (CJD), 60 mad cow disease (BSE), 60 Tri-acylglycerols, 298–299, 307–308, 318–319, 327–330 Triazine dyes, 201 Triglyceride, 389, 618 Trigycerides in fish, 360 Trimethylamine, (TMA), 358, 364, 385 -N-oxide aldolase, 385 (TMAOase) -N-oxide, 379, 385 oxidase, (tmaoase), 366 oxide, (TMAO), 358, 364, 369, 380 reductase, 379, 385 Triticum aestivum L xylanase inhibitor I (TAXI I), 579 Trub, 661 Trypsin, 389, 391, 393 Tryptophol, 667 Tuna, 358, 382, 388, 389, 390 burnt tissue, 371 honeycombing, 358, 371 Turnover number, 380 Two-dimensional electrophoresis, 403–405, 409, 415 alkaline proteins, 404–405 hydrophobic proteins, 404 Tyramine See Amines Tyrosinase, 72, 86–87 Tyrosine, 73 Tyrosol, 667 U Ultrasound assisted thermal packaging, 88 Uracil-DNA N-glycolase, 393 768 Urease, 4, 18, 358–359 dried, 371 epithelial discoloration, 364 ommochromes, 364 Uric acid, 383 V Van der Waals, 179, 182, 208 Vectors, 191, 192 ori, 191 polylinker, 191, 192 promoter, 191, 192, 195, 196 selection marker, 191–193 terminator, 192 Vegetables, processing, 527–554 Vibrio, 695 cholerae, 695 cholerae, 707 paraheamolyticus, 697 vulnificus, 699 vulnifus, 707 Vicinal diketones, 670, 671, 672, 673, 675 biosynthesis, 670 Viruses, 698, 699 Viscera, 392, 393 Viscosity, 570, 572, 573, 574, 583, 584 tomato products, 278, 279, 280, 282, 286 Vitamin analysis, 30 AOAC International Official Methods, 31 bioassays, 30 calorimetric assays, 30 colorimetric assays, 30 fat soluble vitamins, 30 fluorescent assays, 30 gas chromatography, 31 high performance liquid chromatography, 30–31 reverse-phase chromatography, 30 water soluble vitamins, 30 Vitamin, 125 fat-soluble vitamin, 126 vitamin B complex, 126 vitamin C, 126 vitamin E, 307 water-soluble vitamin, 126 VITEK system, 718 Vmax, 161 Volatile compounds, 78, 80, 629–630 See also Flavor W Water activity (aw), 80–81, 111, 126–127, 130, 323, 329, 332, 643, 648–651, 656 absorption and desorption of water, 127 drying food, 130 growth of microorganism, 127 Index of dry food, 127 relative vapor pressure, 126 Water, 103 bond water, 126, 127 chemical bonding, 105 cluster, 108 compound water, 104 critical pressure, 113 critical temperature, 109, 113 density, 112 dimer, 108 food chemistry of, 126 free water, 126 hard water, 121 heat of formation, 104 holding capacity, 300, 310–311 hydrogen bond, 108, 112 ice Ih, 110 interaction with microwave, 129 liquid, 109 loosely bond water, 127 molecular structure, 105 origin of life, 104 phase transition, 109, 111, 113 polarity, 104 properties of liquid H2O, 109, 112 resources, 131 self ionization of water, 115 solid, 109 subcritical water, 113 supercritical water, 113–114 triple point, 109, 114 vapor, 106 Wheat gliadin, 575–577 Wheat glutenin, 576–577 HMW-glutenin subunits, 576–577 LMW-glutenin subunits, 576–577 Wheat, 615–36 Whey, 602, 604 processing, 466–468 proteins, 596, 609 White croaker, 389 White muscle, 381, 382, 385, 386, 389, 390 Whole-meal, 571, 580, 581, 582, 585 Woodchips, 678 Wort, 660, 661, 662 aeration, 661, 662 aldehydes, 676 boiling, 661, 662 carbohydrates, 660, 664 clarification, 661, 662 cooling, 661, 662 fermentation, 665 high-gravity, 661 Index lipids, 665 separation, 661, 662 X Xanthine oxidase, 384 Xanthine, 383, 384 X-ray crystallography, 156 Xylanase inhibiting protein (XIP), 579 Xylitol, 55 Xylose isomerase, Xylose, 570–574, 579 Xylosidase, 575, 579 Xylosone, 86 Y Yeast, 328, 620–623, 625–626, 644–645 alloploid, 665 aneuploid, 665 Candida utilis, 55 cell membrane, 665 growth kinetics, 660 immobilized, 672, 676, 678 lipid vesicles, 667 plasma membrane, 668 polyploid, 665 Saccharomyces cerevisiae, 53 sedimentation, 672 Yellowfin tuna, 364 Yellowtail, 388 Yersinia enterocolitica, 697, 714–715 outbreak, 714 pathogenicity, 714 properties, 714–715 Y-ST enterotoxin, 715 Yogurt, 598–599, 609–612 Y-ST enterotoxin, 715 Z Zinc, 668 Zymography, 170 769 ... Principles of food biochemistry, • Advances in selected areas of food biochemistry, • Food biochemistry and the processing of muscle foods and milk, • Food biochemistry and the processing of... tomatoes, and food hydration chemistry and biochemistry • The chemistry and biochemistry of muscle foods and milk are covered under the color of muscle foods, raw meat and poultry, processed meat and. . .Food Biochemistry and Food Processing Editor Y H Hui Associate Editors Wai-Kit Nip Leo M.L Nollet Gopinadhan Paliyath Benjamin K Simpson Food Biochemistry and Food Processing ©2006