دانلود کتاب Agents of Change: Enzymes in Milk and Dairy Products (Food Engineering Series)

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Preface\nContents\nChapter 1: Enzymology of Milk and Dairy Products: Overview\n 1.1 Introduction\n 1.2 Indigenous Enzymes of Bovine Milk\n 1.3 Endogenous Enzymes in Milk\n 1.4 Exogenous Enzymes\n 1.4.1 Rennets\n 1.4.2 β-Galactosidase (Lactase)\n 1.4.3 Lipases\n 1.4.4 Lysozyme\n 1.4.5 Catalase\n 1.4.6 Glucose Oxidase\n 1.5 Exogenous Enzymes in Food Analysis\n 1.6 Conclusion\n References\n Further Reading\nChapter 2: The Plasmin System in Milk and Dairy Products\n 2.1 Introduction\n 2.2 Plasmin and Plasminogen\n 2.2.1 Proteolytic Specificity of Plasmin on Milk Proteins\n 2.2.1.1 β-casein\n 2.2.1.2 αs2-casein\n 2.2.1.3 αs1-casein\n 2.2.1.4 κ-casein\n 2.2.1.5 Whey Proteins\n 2.3 The Plasmin System in Bovine Milk\n 2.3.1 Activators of the Plasmin System\n 2.3.2 Inhibitors of the Plasmin System\n 2.4 Distribution of Plasmin System Components in Milk\n 2.4.1 Factors Affecting the Distribution of Plasmin System Components Within Milk\n 2.5 Factors Affecting Plasmin Activity and Consequent Proteolysis\n 2.5.1 Mastitis\n 2.5.2 Stage of Lactation\n 2.5.3 Age of Cow\n 2.5.4 Breed of Cow\n 2.5.5 pH of Milk\n 2.5.6 Heat Treatment\n 2.5.7 Presence of β-Lactoglobulin\n 2.5.8 Storage Temperature of Milk\n 2.5.8.1 Cold Storage\n 2.5.8.2 Warm (Room Temperature) Storage\n 2.5.9 Microbial Proteases\n 2.5.10 Membrane Filtration\n 2.5.11 High Pressure\n 2.6 Characterisation of Plasmin and Plasminogen\n 2.6.1 Assay Methods for Plasmin and Plasminogen\n 2.6.2 Assay Methods for Activators and Inhibitors of the Plasmin System\n 2.6.3 Monitoring of Plasmin-Mediated Proteolysis\n 2.6.3.1 Soluble Protein in Supernatant\n 2.6.3.2 Analysis of Free Amino Groups\n 2.6.3.3 Urea-Polyacrylamide Gel Electrophoresis\n 2.6.3.4 Reversed Phase-High Performance Liquid Chromatography\n 2.6.3.5 Mass Spectrometry\n 2.7 Applications of Plasmin and Its Significance in Various Dairy Products\n 2.7.1 Cheese\n 2.7.1.1 Cheese-making Properties\n 2.7.1.2 Cheese Ripening\n 2.7.2 Milk-Based UHT Products\n 2.7.3 High Protein Milk Products\n 2.7.3.1 Whey Protein-Containing Ingredients\n 2.7.3.2 Casein-Containing Ingredients\n 2.8 Conclusions and Areas for Additional Research\n References\nChapter 3: Lysosomal and Other Indigenous Non-plasmin Proteases in Bovine Milk\n 3.1 Introduction\n 3.2 Origin of Non-plasmin Proteolytic Enzymes in Bovine Milk\n 3.3 The Lysosomal and Other Non-plasmin Proteases in Bovine Milk\n 3.3.1 Cathepsin B\n 3.3.2 Cathepsin C: Dipeptidyl Peptidase 1\n 3.3.3 Cathepsin D\n 3.3.4 Cathepsin E\n 3.3.5 Other Lysosomal Cysteine Proteases\n 3.3.6 Cathepsin G\n 3.3.7 PMN Elastase\n 3.3.8 Kallikrein\n 3.3.9 Amino-and Carboxypeptidases\n 3.4 Measurement of Lysosomal and Other Non-plasmin Proteases in Milk\n 3.5 Thermal Inactivation\n 3.6 Impact on Dairy Products\n 3.7 Studies of Indigenous Non-plasmin Milk Proteases in Cases of Induced Mastitis\n 3.8 Biological Significance\n 3.9 Future Aspects and Missing Links\n References\nChapter 4: Phosphatases in Milk\n 4.1 Introduction\n 4.2 Alkaline Phosphatase\n 4.3 Origin, Isolation and Characterization of ALP in Milk\n 4.4 Assay Methods for ALP Activity\n 4.5 Significance of ALP in Dairy Products\n 4.6 Reactivation of ALP\n 4.7 Acid Phosphatase\n 4.8 Distribution, Isolation and Characterization of ACP\n 4.9 Significance of ACP\n 4.10 Conclusions\n References\nChapter 5: Antimicrobial Enzymes in Milk, and Their Role in Human Milk\n 5.1 Introduction\n 5.2 Antimicrobial Enzymes in Human Milk\n 5.2.1 Lysozyme\n 5.2.1.1 General Characteristics of Lysozyme\n 5.2.1.2 Mechanism of Antibacterial Activity of Lysozyme\n 5.2.1.3 Factors Affecting Antimicrobial Activity of Lysozyme\n 5.2.1.4 Assay Methods for Lysozyme Activity\n 5.2.2 Lactoperoxidase\n 5.2.2.1 General Characteristics of Lactoperoxidase\n 5.2.2.2 Mechanism of Antibacterial Activity of Lactoperoxidase\n 5.2.2.3 Factors Affecting Antimicrobial Activity of Lactoperoxidase\n 5.2.2.4 Assay Methods for Lactoperoxidase Activity\n 5.2.3 Xanthine Oxidase\n 5.2.3.1 General Characteristics of Xanthine Oxidase\n 5.2.3.2 Mechanism of Antibacterial Activity of Xanthine Oxidase\n 5.2.3.3 Factors Affecting Antimicrobial Activity of Xanthine Oxidase\n 5.2.3.4 Assay Methods for Xanthine Oxidase Activity\n 5.2.4 The XO-LPO “Oxidative Enzyme System’ in Human Milk and Its Activation by Infant Saliva\n 5.2.5 Polyamine Oxidases\n 5.2.5.1 General Characteristics of Polyamine Oxidase\n 5.2.5.2 Mechanism of Antibacterial Activity of Polyamine Oxidase\n 5.2.5.3 Factors Affecting Activity of Polyamine Oxidase\n 5.2.5.4 Assay Methods for Polyamine Oxidase\n 5.2.6 Lipases\n 5.2.6.1 General Characteristics of Lipases\n 5.2.6.2 Mechanism of Antibacterial Activity of Lipases\n 5.2.6.3 Factors Affecting Activity of Lipases\n 5.2.6.4 Assay Methods for Lipases\n 5.2.7 N-Acetyl-β-D-Glucosaminidase (NAGase)\n 5.2.7.1 General Characteristics of NAGase and Its Activity\n 5.2.7.2 Assay Method for Activity of NAGase\n 5.2.8 Platelet-Activating Factor (PAF) Acetylhydrolase\n 5.2.8.1 General Characteristics, Mechanism and Activity of PAF Acetylhydrolase\n 5.2.8.2 Assay Method for Activity of PAF Acetylhydrolase\n 5.3 Summary\n References\nChapter 6: Enzymes Associated with Milk Phospholipid Membrane Structures: Milk Fat Globule Membranes and Extracellular Vesicles\n 6.1 Introduction\n 6.2 Sulfhydryl Oxidase\n 6.2.1 Structure of Flavin-Dependent Sulfhydryl Oxidase\n 6.2.2 Biological Role of Flavin-Dependent Sulfhydryl Oxidase and Significance in Milk\n 6.3 Catalase\n 6.3.1 Structure of Catalase\n 6.3.2 Biological Role of Catalase and Significance in Milk\n 6.4 Lactoperoxidase\n 6.4.1 Structure of Lactoperoxidase\n 6.4.2 Biological Role of Lactoperoxidase and Significance in Milk\n 6.5 Xanthine Oxidoreductase\n 6.5.1 Structure of Xanthine Oxidoreductase\n 6.5.2 Biological Role of Xanthine Oxidoreductase and Significance in Milk\n 6.6 γ-Glutamyltransferase\n 6.6.1 Structure of γ-Glutamyltransferase\n 6.6.2 Biological Role and Significance of Glutamyltransferase in Milk\n 6.7 5’-Nucleotidase\n 6.7.1 Structure of 5’-Nucleotidase\n 6.7.2 Biological Role and Significance of 5’-Nucleotidase in Milk\n 6.8 Conclusion\n References\nChapter 7: Milk and Other Glycosidases\n 7.1 Introduction\n 7.2 Origin and Significance of Glycosidases in Milk\n 7.3 Cleavage Specificity and Biological Relevance in Relation to Substrates\n 7.4 Glycosidases as Indicators of Mastitis\n 7.5 Industrial Relevance and Effect of Milk Glycosidases during Processing\n 7.5.1 Effect of Processing on Milk Glycosidases\n 7.5.2 Applications of Lactases in Processing of Dairy Products\n 7.6 Detection and Methods for Analysis of Glycosidases\n 7.7 Concluding Remarks\n References\nChapter 8: The Enzymology of Non-bovine Milk\n 8.1 Introduction\n 8.2 Enzymology of Ovine and Caprine Milk\n 8.2.1 Proteolytic Enzyme Activities\n 8.2.2 Activities of Other Enzymes\n 8.2.3 Effect of Enzyme Activity on Milk and Dairy Product Quality\n 8.3 Enzymology of Buffalo Milk\n 8.4 Enzymology of Camel Milk\n 8.5 Enzymology of Non-ruminant Milk\n 8.6 Conclusion\n References\nChapter 9: The Enzymology of Human Milk\n 9.1 Introduction\n 9.2 Proteases\n 9.2.1 Protease Activators\n 9.2.2 Antiproteases\n 9.2.3 Protease Activity in the Mammary Gland\n 9.2.4 Protein Digestion in Human Neonates\n 9.2.5 Proteolytic Systems and Peptides\n 9.2.6 Specific Protease Systems\n 9.2.6.1 Plasmin System\n 9.2.6.2 Cathepsin System\n 9.2.6.3 Elastase System\n 9.2.6.4 Trypsin System\n 9.2.6.5 Chymotrypsin\n 9.2.6.6 Thrombin\n 9.2.6.7 Kallikrein\n 9.2.6.8 Amino- and Carboxypeptidase Systems\n 9.2.6.9 Matrix Metalloproteinase System\n 9.3 Lipases\n 9.3.1 Lipoprotein Lipase\n 9.3.2 Bile Salt-Stimulated Lipase\n 9.4 Glycosidases\n 9.4.1 α-L-Fucosidase\n 9.4.2 α-1,3/4-Fucosyltransferase\n 9.4.3 N-Acetyl-β-D-hexosaminidase\n 9.4.4 Neuraminidase\n 9.4.5 α-Amylase\n 9.4.6 Pro- and Anti-Glycosidases\n 9.5 Other Enzymes in Human Milk\n 9.5.1 Phosphatases\n 9.5.2 Xanthine Oxidase\n 9.5.3 Antioxidant Enzymes\n 9.5.4 Additional Enzymes\n 9.6 Conclusion\n References\nChapter 10: Lipases from Milk and Other Sources\n 10.1 Introduction\n 10.2 The Milk Enzymes\n 10.2.1 Lipoprotein Lipase\n 10.2.2 Somatic Cell Lipase\n 10.2.3 Colostral Lipase\n 10.2.4 Milk Esterases\n 10.3 Lipolysis Due to Milk Lipase in Milk\n 10.3.1 Spontaneous Lipolysis\n 10.3.2 Induced Lipolysis\n 10.4 Lipase-Catalysed Acyl-Transfer Reactions on Milk Fat\n 10.4.1 Interesterification\n 10.4.2 Acidolysis\n 10.4.3 Alcoholysis\n 10.5 Conclusion\n References\nChapter 11: Heat-Stable Microbial Peptidases Associated with the Microbiota of Raw Milk\n 11.1 The Microbiota of Raw Milk\n 11.1.1 The Genus Pseudomonas\n 11.2 Microbial Peptidase from Raw Milk Isolates\n 11.2.1 Peptidases Secreted by Pseudomonas Species\n 11.2.2 Interactions of Plasmin and Microbial Peptidases in Milk\n 11.3 Destabilization of Milk by Peptidases\n 11.4 Determination of Peptidase Activity in Milk\n 11.5 Thermal Inactivation of Peptidases\n 11.6 Conclusion and Outlook\n References\nChapter 12: The Heat Stability of Indigenous and Bacterial Enzymes in Milk\n 12.1 Enzyme Sources and Problems Encountered in Milk Products\n 12.2 Inactivation Methods\n 12.3 Basics of Heat Inactivation Kinetics\n 12.4 Heat Stability of Enzymes\n 12.4.1 Heat Stability of Indigenous Enzymes\n 12.5 Heat Stability of Bacterial Enzymes\n 12.6 Conclusion\n References\nChapter 13: The Role of Proteases in the Stability of UHT-Treated Milk\n 13.1 Introduction\n 13.2 Principles of UHT Processing\n 13.2.1 Definition of UHT Treatment\n 13.3 Chemical Changes Occurring in Milk During UHT Processing\n 13.4 Physico-Chemical Changes in Ultra-High-Temperature (UHT) Treated Milk During Storage\n 13.4.1 Gelation of UHT Milk\n 13.5 Strategies to Control Destabilisation of UHT Treated Milk During Storage\n 13.5.1 Raw Milk Quality\n 13.5.2 Accelerated Shelf-Life Testing of UHT Milk\n 13.6 Conclusions\n References\nChapter 14: Milk-Clotting Enzymes\n 14.1 Historical Background\n 14.2 Different Types of Rennets and Coagulants\n 14.2.1 Bovine Rennets\n 14.2.2 Ovine and Caprine Rennets\n 14.2.3 Porcine and Chicken Pepsin\n 14.2.4 Microbial Coagulants\n 14.2.5 Plant Coagulants\n 14.2.6 Fermentation Produced Chymosin (FPC)\n 14.2.7 General Considerations Around Rennets and Coagulants\n 14.3 Production of Rennets and Coagulants\n 14.4 Market Shares of Different Rennets and Coagulants\n 14.5 Molecular and Catalytic Properties of Milk-Clotting Enzymes\n 14.6 Analysis of Rennets and Coagulants\n 14.7 Interpretation of the Strength of Rennets\n References\nChapter 15: Enzymes in Cheese Ripening\n 15.1 Introduction\n 15.2 Lactose Metabolism\n 15.2.1 Starter Cultures\n 15.2.2 Glycolysis and Regeneration of NADH\n 15.2.3 Lactic Acid Metabolism\n 15.3 Citrate Catabolism\n 15.4 Milk Fat Catabolism\n 15.4.1 Milk Fat Hydrolysis\n 15.4.2 Fatty Acid Metabolism\n 15.4.3 Methods to Accelerate Lipolysis\n 15.5 Proteolysis\n 15.5.1 Proteolytic Activities in Cheese\n 15.5.2 Indigenous Milk Proteases\n 15.5.3 Coagulants\n 15.5.4 Lactic Acid Bacterial Protease: Lactocepin\n 15.5.5 Bacterial Cell Membrane Transport Systems\n 15.5.6 Peptidases\n 15.5.7 Phosphatases\n 15.5.8 Synthesis of Specific Glu-Peptides\n 15.5.9 Acceleration of Proteolysis in Cheese\n 15.6 Amino Acid Catabolism\n 15.6.1 Lyases\n 15.6.2 Dehydratases\n 15.6.3 Aminotransferases\n 15.6.4 Deaminases\n 15.6.5 Decarboxylases\n 15.7 Breakdown of Microbial Cell Membranes and Cell Lysis\n 15.8 Nucleic Acid Catabolism\n 15.9 Catabolism of Vitamins and Other Compounds\n 15.10 Conclusions\n References\nChapter 16: Enzyme Modified Cheese\n 16.1 Introduction\n 16.2 General Principles\n 16.3 The Application and Advantages of EMC as a Cheese Flavor Ingredient\n 16.4 Production Methods of EMC\n 16.4.1 Emulsification of the Substrate\n 16.4.2 Enzyme Addition and Incubation\n 16.4.3 Termination of Enzyme Activity/Standardization of the Final Product\n 16.4.4 Blue Cheese Flavor\n 16.5 Enzymes in EMC Production\n 16.5.1 Proteolytic Enzymes\n 16.5.2 Lipolytic Enzymes\n 16.5.3 Use of Starter Cultures in EMC Production\n 16.6 Health Effects and Functional Properties of EMCs\n 16.7 Conclusion and Future Trends\n References\nChapter 17: Enzymatic Protein Cross-Linking in Dairy Science and Technology\n 17.1 Introduction\n 17.2 Chemical Aspects and Production of Enzymes for Protein Cross-Linking\n 17.2.1 Transglutaminase\n 17.2.2 Oxidoreductases\n 17.3 Analysis of Cross-Linking Reactions\n 17.3.1 Quantification of Enzymatically Induced Covalent Cross-Links\n 17.3.1.1 N-ε-(γ-Glutamyl)-Lysine Isopeptide Content\n 17.3.1.2 Cross-Links from Other Enzymatic Reactions\n 17.3.2 Static and Dynamic Light Scattering\n 17.3.3 Size Separation of Polymerised Milk Proteins\n 17.3.3.1 Gel Electrophoresis\n 17.3.3.2 Size-Exclusion Chromatography\n 17.3.3.3 Field Flow Fractionation\n 17.4 Application of Cross-Linking Enzymes in Dairy Science and Technology\n 17.4.1 Overview of Review Articles and Book Chapters\n 17.4.2 Limitations of Transglutaminase Application for Acid-Induced Milk Gels\n 17.4.3 Application of Laccase in Stirred Yoghurt Manufacture\n 17.4.4 Enzymatic Protein Cross-Linking in Cheese Making\n 17.4.5 Creation of Well-Defined Micro- and Nanostructures\n 17.4.5.1 Preparation of Microgel Particles by Cross-Linking of Casein Micelles\n 17.4.5.2 Cross-Linking of Casein Nanoparticles: Molecular Aspects and Gelation Properties\n 17.4.5.3 Formation and Physical Properties of Nanoparticles from Cross-Linked α-Lactalbumin\n 17.5 Conclusions and Outlook\n References\nChapter 18: The Production of Bioactive Peptides from Milk Proteins\n 18.1 Introduction: Milk Proteins and Bioactive Peptides\n 18.2 Production of Milk Protein-Derived BAPs\n 18.2.1 In Vitro Enzymatic Hydrolysis\n 18.2.1.1 Enzymatic Hydrolysis for the Generation of Anti-Diabetic Peptides\n 18.2.1.2 Enzymatic Hydrolysis for the Generation of Antihypertensive Peptides\n 18.2.1.3 Enzymatic Hydrolysis for the Generation of Antioxidant Peptides\n 18.2.1.4 Enzymatic Hydrolysis for the Generation of Immunomodulatory Peptides\n 18.2.1.5 Enzymatic Hydrolysis for the Generation of Anticancer Peptides\n 18.2.1.6 Enzymatic Hydrolysis for the Generation of Antimicrobial Peptides\n 18.2.1.7 Enzymatic Hydrolysis for the Generation of Opioid-Like Peptides\n 18.2.1.8 Enzymatic Hydrolysis for the Generation of Other Bioactive Peptides\n 18.2.2 Microbial Fermentation\n 18.2.2.1 Bacteria\n 18.2.2.2 Yeasts and Moulds\n 18.2.3 Production of BAPs During Gastrointestinal Digestion\n 18.2.4 In silico Approaches for Peptide Generation\n 18.3 Fractionation and Enrichment of BAPs\n 18.3.1 Membrane Filtration\n 18.3.2 Chromatography\n 18.4 Conclusion\n References\nChapter 19: Reducing Allergenicity by Proteolysis\n 19.1 Cow’s Milk Allergy\n 19.1.1 Bovine Milk Proteins\n 19.1.2 Bovine Milk Epitopes\n 19.1.3 Bovine Milk Proteolysis\n 19.2 Digestion\n 19.2.1 Digestion Process\n 19.2.2 Digestibility of Bovine Milk Proteins\n 19.2.3 Digestion Parameters Affecting the Digestibility of Bovine Milk Proteins\n 19.2.4 Evaluation of Digestibility\n 19.2.5 Evaluation of Residual Allergenicity of Digestion Products\n 19.3 Infant Formulas\n 19.3.1 Hypoallergenic Infant Formulas\n 19.3.2 Production Process\n 19.3.3 Clinical Use of eHF and pHF\n 19.3.4 Allergenicity Evaluation\n 19.4 Conclusions\n References\nChapter 20: Future Opportunities and Challenges in Dairy Enzymology\n 20.1 Introduction\n 20.2 Future Challenges in Indigenous and Endogenous Milk Enzymology\n 20.3 Processing and Milk Enzymes\n 20.4 Emerging Enzymes\n 20.4.1 Protein Glutaminase\n 20.4.2 Glutaminase\n 20.4.3 Lactose Oxidase\n 20.4.4 Phospholipase\n 20.5 Application of Molecular Methods: Omics\n 20.6 Conclusion: Remaining Gaps in Our Knowledge and Future Outlook\n References\nIndex