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Wang S: Food-derived Bioactive Peptides

Food-derived Bioactive Peptides

Green Preparation, Activity Mechanisms, and Health Applications

Preface xv 1 Introduction 1 2 Preparation of Bioactive Peptides 3 2.1 Introduction 3 2.2 Preparation Methods for Bioactive Peptides 4 2.2.1 Protein Hydrolysis 4 2.2.1.1 Enzymatic Hydrolysis 4 2.2.1.2 Microbial Fermentation 7 2.2.1.3 Chemical Hydrolysis 8 2.2.2 Chemical Synthesis 8 2.2.3 Recombinant Expression Technologies 8 2.2.3.1 Genetic Engineering of Fish- Derived Antifreeze Proteins or Peptides 9 2.2.3.2 Genetic Engineering of Insect- Derived Antifreeze Proteins 9 2.2.3.3 Genetic Engineering of Plant- Derived Antifreeze Proteins 9 2.2.3.4 Chemical Modification 10 2.3 Separation and Purification Techniques of Peptides 10 2.3.1 Ultrafiltration 11 2.3.2 Ion Exchange Chromatography 12 2.3.3 Gel Filtration Chromatography 12 2.3.4 Reversed- Phase High- Performance Liquid Chromatography 13 2.3.5 Capillary Electrophoresis 13 2.3.6 Immobilized Metal Affinity Chromatography 13 2.4 Computer- Aided Screening Technologies for Bioactive Peptides 13 References 15 3 Antifreeze Peptides 21 3.1 Introduction 21 3.2 Production and Purification of AFPs 22 3.2.1 Evaluation Methods of Antifreeze Activity 22 3.2.2 Nanoliter Osmometer 22 3.2.3 Differential Scanning Calorimetry (DSC) 23 3.2.4 Splat- Cooling 24 3.2.5 Low- Field Nuclear Magnetic Resonance (LF- NMR) 25 3.2.6 Bio- Valuation Model 25 3.2.7 Novel Technology in Utilization of the Evaluation of Antifreeze Activity 26 3.3 Molecular Characteristics and Structure-Function Relationships of AFPs 26 3.4 Action Mechanisms of AFPs 27 3.5 Application Advances of AFPs in Frozen Food Industry 30 3.5.1 Edible Safety of AFPs 31 3.5.2 Methods of Introducing AFPs into Food Products 31 3.5.3 Application in Frozen Dough 32 3.5.4 Application in Frozen Meat Products 33 3.5.5 Application in Frozen Fruit and Vegetable Products 34 3.5.6 Application in Dairy Products 34 3.5.7 Application in Cryobiology 35 3.6 Future Direction 36 References 37 4 Antioxidant Peptides 43 4.1 Sources 43 4.1.1 Marine Resources 43 4.1.2 Meat and By- Products 44 4.1.3 Plant Sources 47 4.1.4 Dairy Products 48 4.2 Evaluation Method of Activity 49 4.2.1 In vitro Evaluation 49 4.2.1.1 DPPH Radical Scavenging Assay 50 4.2.1.2 ABTS Radical Scavenging Assay 50 4.2.1.3 Hydroxyl Radical Scavenging Assay 51 4.2.1.4 Superoxide Anions Radical Scavenging Assay 52 4.2.1.5 Ferric- Reducing Antioxidant Power (FRAP) 52 4.2.1.6 Oxygen Radical Absorption Capacity (ORAC) Method 53 4.2.2 Cellular Antioxidant Effect 54 4.2.3 In vivo Antioxidant Effect 58 4.3 Mechanism Consideration 64 4.3.1 Mechanisms Underlying Cellular Antioxidant Effects 64 4.3.2 Mechanisms Underlying In Vivo Antioxidant Effects 65 4.3.3 Structure-Activity Relationship 66 4.3.3.1 Effect of Molecular Weight 66 4.3.3.2 Effect of Amino Acid Composition and Sequence 67 4.3.3.3 Effect of Secondary Structure 68 4.4 Security Assessment 69 4.4.1 Toxicological Assessment 70 4.4.2 Immunogenicity Assessment 70 4.4.3 Genotoxicity Studies 70 4.4.4 Bioavailability and Metabolism Studies 70 4.5 Application of Antioxidant Peptides 71 4.5.1 Applications in the Food Sector 71 4.5.2 Applications in the Pharmaceutical Field 73 4.5.2.1 Anti- Inflammatory and Liver- Protecting Drugs 74 4.5.2.2 Adjuvant Cancer Treatment Drugs 75 4.5.2.3 Anti- Fatigue Drug 76 4.5.2.4 Drugs for Other Diseases 77 4.5.3 Applications for Skincare 77 4.5.3.1 Anti- Aging Effect 77 4.5.3.2 Restoration and Conservation 78 4.5.3.3 Whitening and Moisturizing Effect 79 4.6 Limitation and Challenges 80 4.6.1 Preparation Method 80 4.6.2 Structural and Properties 81 References 82 5 Antimicrobial Peptides 99 5.1 Sources 100 5.1.1 Plant- Derived Antimicrobial Peptides 100 5.1.1.1 Thionins 100 5.1.1.2 Plant Defensins 101 5.1.1.3 Snakins 102 5.1.1.4 Hevein- Like Peptides 102 5.1.1.5 Knottin- Type Peptides 104 5.1.2 Animal- Derived AMPs 105 5.1.2.1 Piscidin- Like Peptides 105 5.1.2.2 Cathelicidins 106 5.1.2.3 Histone- Derived Antimicrobial Effectors 106 5.1.2.4 Hepcidin Family 106 5.1.2.5 Defensin Superfamily 106 5.1.3 Microbial- Derived Antimicrobial Peptides 106 5.1.3.1 RPs 107 5.1.3.2 NRPs 111 5.2 Evaluation Method of Activity 116 5.2.1 In Vitro Antimicrobial Activity 117 5.2.1.1 Agar Diffusion Method 117 5.2.1.2 Turbidimetric Assay Method 118 5.2.1.3 Viable Cell Count Method 119 5.2.1.4 Microdilution Method 119 5.2.2 In Vitro Antimicrobial Activity 120 5.2.2.1 Principles of Model Construction 120 5.2.2.2 Inoculation Routes 121 5.2.2.3 Model Identification 121 5.2.2.4 Common Mouse Models of Bacterial Infection and Experimental Methods 121 5.3 Mechanism Consideration of AMPs 122 5.3.1 Structure- Mechanism Relationship of AMPs 122 5.3.1.1 Constituents of AMPs 123 5.3.1.2 Molecular Length of AMPs 123 5.3.1.3 Charges of AMPs 123 5.3.1.4 Hydrophobicity of AMPs 124 5.3.1.5 Secondary Structure of AMPs 124 5.3.1.6 Curvature of AMPs 124 5.3.2 Mode of Actions of AMPs 125 5.3.2.1 Targeting Cell Wall Biosynthesis 125 5.3.2.2 Targeting Precursors of Peptidoglycan Biosynthesis 129 5.3.2.3 Blockage of Peptidoglycan Remodeling 132 5.3.3 Inhibition of DNA Gyrase 132 5.3.4 Suppression of Protein Synthesis and Breakdown 133 5.3.4.1 Interrupting Protein Translation 134 5.3.4.2 Disruption of Protein Post- Translational Modifications 136 5.3.4.3 Dysregulation of Protein Degradation 139 5.3.5 Destabilization of Cell Membranes 141 5.4 Security Assessment 145 5.4.1 Cytotoxicity of AMPs 145 5.4.2 In Vivo Toxicity of AMPs 145 5.5 Application 146 5.5.1 Food Preservation 146 5.5.2 Bioactive Food Ingredients 146 5.5.3 Agricultural Applications 148 5.5.4 Animal Feed Additives 149 5.5.5 Medical Applications 149 5.5.5.1 Antimicrobial Agent 149 5.5.5.2 Wound Healing 150 5.5.5.3 Other Applications 150 5.6 Limitations and Challenges 151 5.6.1 Chemical Modifications of AMPs 152 5.6.1.1 Lipidation of AMPs 152 5.6.1.2 Glycosylation of AMPs 153 5.6.1.3 Peptidomimetics 153 5.6.2 Delivery Systems for AMPs 153 5.6.2.1 Inorganic and Metallic Nanoparticles for AMPs 153 5.6.2.2 Polymeric Nanoparticles for AMPs 154 References 154 6 Metal- Chelating Peptides 165 6.1 Introduction 165 6.2 Preparation 166 6.2.1 Enzymatic Hydrolysis 168 6.2.2 Microbial Fermentation Method 169 6.2.3 Chemical Synthesis Method 170 6.3 Evaluation Method of Activity 170 6.3.1 Chelating Capacity Assessment 173 6.3.2 Physiological Stability Assessment 174 6.3.2.1 High- Performance Liquid Chromatography 174 6.3.2.2 Mass Spectrometry 174 6.3.2.3 Zeta Potential Analysis 175 6.3.2.4 Integration of Techniques for Comprehensive Assessment 175 6.3.3 Absorption Efficiency Assessment 175 6.3.4 Biological Activity Assessment 176 6.3.4.1 Cell- Based Assays: Osteoblast- Like MC3T3- E1 Cells 176 6.3.4.2 In Vivo Studies: Animal Models 176 6.3.4.3 Comprehensive Evaluation of MCPs 177 6.4 Chelation Mechanism 178 6.4.1 Chelation Mechanism of Metal- Chelating Peptides 178 6.4.2 Key Functional Groups in Metal Binding 178 6.4.3 Advanced Techniques for Understanding Binding Modes 178 6.4.4 Specific Chelation Modes of Peptides with Metal Ions 179 6.4.4.1 Coordination Sites and Bond Formation 179 6.4.4.2 Main Chelation Modes for Marine Peptides 179 6.4.5 Factors Influencing Chelation 179 6.4.5.1 Amino Acid Composition and Sequence 179 6.4.5.2 Hydrophilicity/Hydrophobicity Balance 180 6.4.5.3 Functional Groups and Metal Ion Chelation 180 6.4.5.4 Influence of R Groups 180 6.4.5.5 Amino Acids with High Chelation Activity 180 6.4.6 Conclusion 181 6.5 Applications 182 6.5.1 The Multifaceted Applications of Metal- Chelating Peptides 182 6.5.1.1 Applications in the Food Industry 182 6.5.1.2 Applications in the Pharmaceutical Industry 182 6.5.1.3 Conclusion and Future Directions 182 References 183 7 Antiaging Peptides 189 7.1 Definition of Aging and Antiaging Peptides 189 7.1.1 Biological Basis of Aging 189 7.1.2 The Rise of Antiaging Peptides 190 7.2 Natural Sources and Synthetic Antiaging Peptides 191 7.2.1 Natural Antiaging Peptides 191 7.2.1.1 Animal- Derived Antiaging Peptides 191 7.2.1.2 Plant- Derived Antiaging Peptides 193 7.2.1.3 Microbial- Derived Antiaging Peptides 194 7.2.2 Preparation Method of Natural Antiaging Peptides 194 7.2.3 Engineering Synthetic Peptides 196 7.2.3.1 Optimization Strategy Based on Computer- Aided Design 196 7.2.3.2 Modification Techniques: Cyclization, D- Amino Acid Substitution, PEGylation 197 7.3 Structural Characteristics of Antiaging Peptides 199 7.4 Mechanism of Action of Antiaging Peptides 201 7.5 Research Methods and Evaluation System of Antiaging Peptides 208 7.5.1 The Core Method of Antiaging Peptide Research 208 7.5.1.1 Molecular Interaction Analysis 208 7.5.1.2 High- Throughput Screening Technology 209 7.5.2 Evaluation Method of Antiaging Peptides 209 7.6 Application of Antiaging Peptides 211 7.6.1 Application in Food System 212 7.6.2 Application in Pharmaceutical Industry 213 7.6.3 Application in Skin Care Industry 214 7.7 Challenges and Controversies in Antiaging Peptides 215 7.7.1 Technical Bottleneck 215 7.7.2 Stability and Half- Life of Antiaging Peptides 217 7.7.3 Blood-Brain Barrier Penetration Challenge 217 7.7.4 Security 218 7.8 Future Direction 219 7.8.1 Multi- Target Synergistic Strategy 219 7.8.2 Artificial Intelligence-Driven Design 220 7.8.3 Precision Antiaging Medicine 221 References 223 8 Antifatigue Peptides 229 8.1 Introduction of Antifatigue Peptides 229 8.2 Extraction and Purification of Antifatigue Peptides 229 8.2.1 Sources of Antifatigue Peptides 229 8.2.2 Preparation of Antifatigue Peptides 231 8.2.2.1 Chemical Hydrolysis Method 231 8.2.2.2 Chemical Synthesis 231 8.2.2.3 Enzyme Synthesis Method 232 8.2.2.4 Microbial Fermentation Method 232 8.2.2.5 Enzymatic Hydrolysis Method 233 8.2.3 Isolation and Purification of Antifatigue Peptides 235 8.2.3.1 Electrophoresis Technology 235 8.2.3.2 Chromatography Technology 235 8.2.3.3 Membrane Separation Technology 236 8.2.3.4 Multiple Methods Combined 236 8.2.4 Sequence Identification of Antifatigue Peptides 237 8.2.5 Correlation Between Structural Features and Antifatigue Function 238 8.2.5.1 Amino Acid Composition 238 8.2.5.2 Sequence Features 239 8.2.5.3 Molecular Weight Size 240 8.2.5.4 Peptide Chain Length 240 8.3 Detection and Evaluation of the Activity of Antifatigue Peptides 241 8.3.1 Mice Pole- Climbing Test 241 8.3.2 Mice Swimming Test 242 8.3.3 Mice Tail- Hanging Test 243 8.3.4 Mice Rotameter Test 243 8.3.5 Common Antifatigue Biochemical Indexes 244 8.4 Mechanisms of Antifatigue Peptides in Relieving Exercise Fatigue 245 8.4.1 Regulation of Energy Metabolism 245 8.4.2 Regulation of Inflammation 247 8.4.3 Antioxidant Effect 248 8.4.4 Regulation of Neurotransmitters 249 8.4.5 Improvement of Exercise Endurance 250 8.5 Current Status of Research and Its Applications 252 8.5.1 Animal- Derived Peptides 252 8.5.1.1 Oyster Peptides 253 8.5.1.2 Jellyfish Peptides 254 8.5.1.3 Sea Cucumber Peptides 255 8.5.1.4 Freshwater Fish Peptides 256 8.5.1.5 Marine Fish Peptides 257 8.5.1.6 Livestock- Derived Peptides 258 8.5.2 Plant- Derived Peptides 259 8.5.3 Yeast- Derived Peptides 260 8.5.4 Productions 261 References 262 9 Immune Regulatory Peptides 269 9.1 Introduction 269 9.1.1 Molecular Basis of Immunomodulation and Host Defense Mechanisms 269 9.2 Introduction to Immunomodulatory Peptides 270 9.3 Immunomodulatory Peptides 271 9.3.1 Mechanisms and Biological Roles 271 9.4 Applications in Disease Management 271 9.4.1 Inflammatory and Autoimmune Disorders 271 9.4.2 Cancer Immunotherapy 272 9.4.3 Infectious Diseases and Antimicrobial Resistance 272 9.4.4 Challenges and Innovations in Peptide Therapeutics 272 9.4.5 Future Perspectives 272 9.5 Conclusion 273 9.6 Preparation 273 9.6.1 Preparation Method of Immunomodulatory Peptide 273 9.6.1.1 Organic Solvent Extraction 273 9.6.1.2 Tissue Homogenization Extraction 274 9.6.1.3 Enzymatic Hydrolysis 274 9.6.1.4 Chemical Synthesis 275 9.6.1.5 Microbial Fermentation 277 9.6.1.6 Genetic Engineering 277 9.6.2 Isolation and Purification Method of Immunomodulatory Peptides 278 9.6.2.1 Ultrafiltration 278 9.6.2.2 Chromatography 279 9.6.2.3 Solvent Extraction 280 9.6.2.4 Membrane Separation Continuous Coupling Technology 280 9.7 Evaluation Method of Activity 281 9.7.1 In Vitro Cell Models 281 9.7.2 In Vivo Animal Models 284 9.8 Mechanism Consideration 286 9.8.1 Direct Regulation of Immune Cell Function 287 9.8.2 Modulation of Cytokine Networks 287 9.8.3 Regulation of Signal Transduction Pathways 287 9.8.4 Regulation of Gut Immune Homeostasis 288 9.8.5 Direct Regulation of Immune Cells by Functional Peptides 288 9.8.5.1 Regulation of T Cells 288 9.8.5.2 Regulation of B Cells 289 9.8.5.3 Regulation of Macrophage Polarization 289 9.8.5.4 Regulation of Natural Killer Cells 289 9.8.6 Modulation of Cytokine Networks 290 9.8.6.1 Regulation of Proinflammatory Cytokines 290 9.8.6.2 Regulation of Anti- Inflammatory Cytokines 290 9.8.6.3 Modulation of Cytokine Network Balance by Functional Peptides 290 9.8.7 Regulation of Signaling Pathways by Functional Peptides 291 9.8.7.1 NF- ¿B Signaling Pathway 291 9.8.7.2 MAPK and JAK-STAT Pathways 291 9.8.8 Role of Functional Peptides in Intestinal Immune Regulation 291 9.9 Applications 292 9.9.1 Application of Functional Peptides in Pulp Therapy 292 9.9.1.1 Synergistic Antibacterial Effects and Dentin Regeneration 292 9.9.1.2 Immunomodulatory Mechanisms 292 9.9.2 Application of Functional Peptides in Tissue Engineering 293 9.9.2.1 Serum- Free Expansion of Artificial Mesenchymal Stem Cells 293 9.9.2.2 Tissue Repair and Regeneration 293 9.9.3 Application of Functional Peptides in Immune Enhancement 293 9.9.3.1 Peptide Nanofibers as Adjuvants 293 9.9.3.2 Effects of Peptide Hydrolysates on Immune Function 294 9.9.4 Application of Functional Peptides in Immune Suppression 294 9.9.4.1 Peptides in Systemic Lupus Erythematosus 294 9.9.4.2 Immunosuppressive Effects of VIP Peptide 294 References 295 10 Flavor Peptides 299 10.1 Introduction 299 10.2 Preparation of Flavor Peptides 303 10.2.1 Methods for Hydrolysis and Microbial Fermentation 303 10.2.2 Methods for Direct Extraction and Synthesis 304 10.3 Taste Characteristics of Flavor Peptides 305 10.3.1 The Effect of Amino Acids 305 10.3.2 The Effect of Flavor and Matrix Interactions 307 10.4 Taste Mechanism of Flavor Peptides 308 10.4.1 Release and Migration of Flavor Peptides 308 10.4.2 Taste Buds and Taste Cells 308 10.4.3 Taste Receptors and Conductive Pathway 308 10.5 Applications in the Food Industry 312 10.5.1 Compound Condiments 312 10.5.2 Functional Foods 314 Abbreviations 315 References 315 11 Self- Assembling Peptides 323 11.1 Sources 323 11.1.1 Food- Derived SAPs 323 11.1.2 Artificially Designed SAPs 325 11.2 Supramolecular Structure of SAPs 326 11.2.1 Nanotube 327 11.2.2 Nanofiber 327 11.2.3 Nanosheets/Ribbons 327 11.2.4 Other Supramolecular Structures 328 11.3 Mechanism Consideration 329 11.3.1 Thermodynamics of Self- Assembly 329 11.3.2 Dynamics of Self- Assembly 330 11.3.3 Effects of Kinetic/Thermodynamic Interactions 332 11.4 Function Properties of SAPs 332 11.4.1 Amphiphilicity 333 11.4.2 Gelation Ability 333 11.4.3 Assembly Reversibility 334 11.4.4 Photoelectric Properties 335 11.5 Security Assessment 335 11.5.1 Biocompatibility 336 11.5.2 Immunogenicity 336 11.5.3 Degradation Product Toxicity 336 11.6 Applications 337 11.6.1 Food Industry 337 11.6.1.1 Nutrient Delivery Systems 337 11.6.1.2 Food Detection 337 11.6.1.3 Other Applications 337 11.6.2 Biomedical Fields 338 11.6.2.1 Pharmaceutical Effect 338 11.6.2.2 Antibacterial Nanomaterials 338 11.6.2.3 Tissue Engineering 339 11.6.3 Other Applications 339 11.7 Limitations and Challenges 340 References 340 Index 347

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