Food-derived Bioactive Peptides

SHAO-YUN WANG is Professor and Dean at the College of Biological Science and Engineering, Fuzhou University, China. She’s an expert in bioactive substances, biotechnological processing of marine and agricultural products, functional foods and materials, and food biotechnology. XU CHEN is Associate Professor at the College of Biological Science and Engineering, Fuzhou University, China. His research is focused on bioactive proteins and peptides mining and functional mechanism analysis and applications. XIXI CAI is Associate Professor at the College of Biological Science and Engineering, Fuzhou University, China. Her research is focused on bioactive proteins and peptides mining and functional mechanism analysis and applications.

• Preface xv1 Introduction 12 Preparation of Bioactive Peptides 32.1 Introduction 32.2 Preparation Methods for Bioactive Peptides 42.2.1 Protein Hydrolysis 42.2.1.1 Enzymatic Hydrolysis 42.2.1.2 Microbial Fermentation 72.2.1.3 Chemical Hydrolysis 82.2.2 Chemical Synthesis 82.2.3 Recombinant Expression Technologies 82.2.3.1 Genetic Engineering of Fish- Derived Antifreeze Proteins or Peptides 92.2.3.2 Genetic Engineering of Insect- Derived Antifreeze Proteins 92.2.3.3 Genetic Engineering of Plant- Derived Antifreeze Proteins 92.2.3.4 Chemical Modification 102.3 Separation and Purification Techniques of Peptides 102.3.1 Ultrafiltration 112.3.2 Ion Exchange Chromatography 122.3.3 Gel Filtration Chromatography 122.3.4 Reversed- Phase High- Performance Liquid Chromatography 132.3.5 Capillary Electrophoresis 132.3.6 Immobilized Metal Affinity Chromatography 132.4 Computer- Aided Screening Technologies for Bioactive Peptides 13References 153 Antifreeze Peptides 213.1 Introduction 213.2 Production and Purification of AFPs 223.2.1 Evaluation Methods of Antifreeze Activity 223.2.2 Nanoliter Osmometer 223.2.3 Differential Scanning Calorimetry (DSC) 233.2.4 Splat- Cooling 243.2.5 Low- Field Nuclear Magnetic Resonance (LF- NMR) 253.2.6 Bio- Valuation Model 253.2.7 Novel Technology in Utilization of the Evaluation of Antifreeze Activity 263.3 Molecular Characteristics and Structure–Function Relationships of AFPs 263.4 Action Mechanisms of AFPs 273.5 Application Advances of AFPs in Frozen Food Industry 303.5.1 Edible Safety of AFPs 313.5.2 Methods of Introducing AFPs into Food Products 313.5.3 Application in Frozen Dough 323.5.4 Application in Frozen Meat Products 333.5.5 Application in Frozen Fruit and Vegetable Products 343.5.6 Application in Dairy Products 343.5.7 Application in Cryobiology 353.6 Future Direction 36References 374 Antioxidant Peptides 434.1 Sources 434.1.1 Marine Resources 434.1.2 Meat and By- Products 444.1.3 Plant Sources 474.1.4 Dairy Products 484.2 Evaluation Method of Activity 494.2.1 In vitro Evaluation 494.2.1.1 DPPH Radical Scavenging Assay 504.2.1.2 ABTS Radical Scavenging Assay 504.2.1.3 Hydroxyl Radical Scavenging Assay 514.2.1.4 Superoxide Anions Radical Scavenging Assay 524.2.1.5 Ferric- Reducing Antioxidant Power (FRAP) 524.2.1.6 Oxygen Radical Absorption Capacity (ORAC) Method 534.2.2 Cellular Antioxidant Effect 544.2.3 In vivo Antioxidant Effect 584.3 Mechanism Consideration 644.3.1 Mechanisms Underlying Cellular Antioxidant Effects 644.3.2 Mechanisms Underlying In Vivo Antioxidant Effects 654.3.3 Structure–Activity Relationship 664.3.3.1 Effect of Molecular Weight 664.3.3.2 Effect of Amino Acid Composition and Sequence 674.3.3.3 Effect of Secondary Structure 684.4 Security Assessment 694.4.1 Toxicological Assessment 704.4.2 Immunogenicity Assessment 704.4.3 Genotoxicity Studies 704.4.4 Bioavailability and Metabolism Studies 704.5 Application of Antioxidant Peptides 714.5.1 Applications in the Food Sector 714.5.2 Applications in the Pharmaceutical Field 734.5.2.1 Anti- Inflammatory and Liver- Protecting Drugs 744.5.2.2 Adjuvant Cancer Treatment Drugs 754.5.2.3 Anti- Fatigue Drug 764.5.2.4 Drugs for Other Diseases 774.5.3 Applications for Skincare 774.5.3.1 Anti- Aging Effect 774.5.3.2 Restoration and Conservation 784.5.3.3 Whitening and Moisturizing Effect 794.6 Limitation and Challenges 804.6.1 Preparation Method 804.6.2 Structural and Properties 81References 825 Antimicrobial Peptides 995.1 Sources 1005.1.1 Plant- Derived Antimicrobial Peptides 1005.1.1.1 Thionins 1005.1.1.2 Plant Defensins 1015.1.1.3 Snakins 1025.1.1.4 Hevein- Like Peptides 1025.1.1.5 Knottin- Type Peptides 1045.1.2 Animal- Derived AMPs 1055.1.2.1 Piscidin- Like Peptides 1055.1.2.2 Cathelicidins 1065.1.2.3 Histone- Derived Antimicrobial Effectors 1065.1.2.4 Hepcidin Family 1065.1.2.5 Defensin Superfamily 1065.1.3 Microbial- Derived Antimicrobial Peptides 1065.1.3.1 RPs 1075.1.3.2 NRPs 1115.2 Evaluation Method of Activity 1165.2.1 In Vitro Antimicrobial Activity 1175.2.1.1 Agar Diffusion Method 1175.2.1.2 Turbidimetric Assay Method 1185.2.1.3 Viable Cell Count Method 1195.2.1.4 Microdilution Method 1195.2.2 In Vitro Antimicrobial Activity 1205.2.2.1 Principles of Model Construction 1205.2.2.2 Inoculation Routes 1215.2.2.3 Model Identification 1215.2.2.4 Common Mouse Models of Bacterial Infection and Experimental Methods 1215.3 Mechanism Consideration of AMPs 1225.3.1 Structure– Mechanism Relationship of AMPs 1225.3.1.1 Constituents of AMPs 1235.3.1.2 Molecular Length of AMPs 1235.3.1.3 Charges of AMPs 1235.3.1.4 Hydrophobicity of AMPs 1245.3.1.5 Secondary Structure of AMPs 1245.3.1.6 Curvature of AMPs 1245.3.2 Mode of Actions of AMPs 1255.3.2.1 Targeting Cell Wall Biosynthesis 1255.3.2.2 Targeting Precursors of Peptidoglycan Biosynthesis 1295.3.2.3 Blockage of Peptidoglycan Remodeling 1325.3.3 Inhibition of DNA Gyrase 1325.3.4 Suppression of Protein Synthesis and Breakdown 1335.3.4.1 Interrupting Protein Translation 1345.3.4.2 Disruption of Protein Post- Translational Modifications 1365.3.4.3 Dysregulation of Protein Degradation 1395.3.5 Destabilization of Cell Membranes 1415.4 Security Assessment 1455.4.1 Cytotoxicity of AMPs 1455.4.2 In Vivo Toxicity of AMPs 1455.5 Application 1465.5.1 Food Preservation 1465.5.2 Bioactive Food Ingredients 1465.5.3 Agricultural Applications 1485.5.4 Animal Feed Additives 1495.5.5 Medical Applications 1495.5.5.1 Antimicrobial Agent 1495.5.5.2 Wound Healing 1505.5.5.3 Other Applications 1505.6 Limitations and Challenges 1515.6.1 Chemical Modifications of AMPs 1525.6.1.1 Lipidation of AMPs 1525.6.1.2 Glycosylation of AMPs 1535.6.1.3 Peptidomimetics 1535.6.2 Delivery Systems for AMPs 1535.6.2.1 Inorganic and Metallic Nanoparticles for AMPs 1535.6.2.2 Polymeric Nanoparticles for AMPs 154References 1546 Metal- Chelating Peptides 1656.1 Introduction 1656.2 Preparation 1666.2.1 Enzymatic Hydrolysis 1686.2.2 Microbial Fermentation Method 1696.2.3 Chemical Synthesis Method 1706.3 Evaluation Method of Activity 1706.3.1 Chelating Capacity Assessment 1736.3.2 Physiological Stability Assessment 1746.3.2.1 High- Performance Liquid Chromatography 1746.3.2.2 Mass Spectrometry 1746.3.2.3 Zeta Potential Analysis 1756.3.2.4 Integration of Techniques for Comprehensive Assessment 1756.3.3 Absorption Efficiency Assessment 1756.3.4 Biological Activity Assessment 1766.3.4.1 Cell- Based Assays: Osteoblast- Like MC3T3- E1 Cells 1766.3.4.2 In Vivo Studies: Animal Models 1766.3.4.3 Comprehensive Evaluation of MCPs 1776.4 Chelation Mechanism 1786.4.1 Chelation Mechanism of Metal- Chelating Peptides 1786.4.2 Key Functional Groups in Metal Binding 1786.4.3 Advanced Techniques for Understanding Binding Modes 1786.4.4 Specific Chelation Modes of Peptides with Metal Ions 1796.4.4.1 Coordination Sites and Bond Formation 1796.4.4.2 Main Chelation Modes for Marine Peptides 1796.4.5 Factors Influencing Chelation 1796.4.5.1 Amino Acid Composition and Sequence 1796.4.5.2 Hydrophilicity/Hydrophobicity Balance 1806.4.5.3 Functional Groups and Metal Ion Chelation 1806.4.5.4 Influence of R Groups 1806.4.5.5 Amino Acids with High Chelation Activity 1806.4.6 Conclusion 1816.5 Applications 1826.5.1 The Multifaceted Applications of Metal- Chelating Peptides 1826.5.1.1 Applications in the Food Industry 1826.5.1.2 Applications in the Pharmaceutical Industry 1826.5.1.3 Conclusion and Future Directions 182References 1837 Antiaging Peptides 1897.1 Definition of Aging and Antiaging Peptides 1897.1.1 Biological Basis of Aging 1897.1.2 The Rise of Antiaging Peptides 1907.2 Natural Sources and Synthetic Antiaging Peptides 1917.2.1 Natural Antiaging Peptides 1917.2.1.1 Animal- Derived Antiaging Peptides 1917.2.1.2 Plant- Derived Antiaging Peptides 1937.2.1.3 Microbial- Derived Antiaging Peptides 1947.2.2 Preparation Method of Natural Antiaging Peptides 1947.2.3 Engineering Synthetic Peptides 1967.2.3.1 Optimization Strategy Based on Computer- Aided Design 1967.2.3.2 Modification Techniques: Cyclization, D- Amino Acid Substitution, PEGylation 1977.3 Structural Characteristics of Antiaging Peptides 1997.4 Mechanism of Action of Antiaging Peptides 2017.5 Research Methods and Evaluation System of Antiaging Peptides 2087.5.1 The Core Method of Antiaging Peptide Research 2087.5.1.1 Molecular Interaction Analysis 2087.5.1.2 High- Throughput Screening Technology 2097.5.2 Evaluation Method of Antiaging Peptides 2097.6 Application of Antiaging Peptides 2117.6.1 Application in Food System 2127.6.2 Application in Pharmaceutical Industry 2137.6.3 Application in Skin Care Industry 2147.7 Challenges and Controversies in Antiaging Peptides 2157.7.1 Technical Bottleneck 2157.7.2 Stability and Half- Life of Antiaging Peptides 2177.7.3 Blood–Brain Barrier Penetration Challenge 2177.7.4 Security 2187.8 Future Direction 2197.8.1 Multi- Target Synergistic Strategy 2197.8.2 Artificial Intelligence-Driven Design 2207.8.3 Precision Antiaging Medicine 221References 2238 Antifatigue Peptides 2298.1 Introduction of Antifatigue Peptides 2298.2 Extraction and Purification of Antifatigue Peptides 2298.2.1 Sources of Antifatigue Peptides 2298.2.2 Preparation of Antifatigue Peptides 2318.2.2.1 Chemical Hydrolysis Method 2318.2.2.2 Chemical Synthesis 2318.2.2.3 Enzyme Synthesis Method 2328.2.2.4 Microbial Fermentation Method 2328.2.2.5 Enzymatic Hydrolysis Method 2338.2.3 Isolation and Purification of Antifatigue Peptides 2358.2.3.1 Electrophoresis Technology 2358.2.3.2 Chromatography Technology 2358.2.3.3 Membrane Separation Technology 2368.2.3.4 Multiple Methods Combined 2368.2.4 Sequence Identification of Antifatigue Peptides 2378.2.5 Correlation Between Structural Features and Antifatigue Function 2388.2.5.1 Amino Acid Composition 2388.2.5.2 Sequence Features 2398.2.5.3 Molecular Weight Size 2408.2.5.4 Peptide Chain Length 2408.3 Detection and Evaluation of the Activity of Antifatigue Peptides 2418.3.1 Mice Pole- Climbing Test 2418.3.2 Mice Swimming Test 2428.3.3 Mice Tail- Hanging Test 2438.3.4 Mice Rotameter Test 2438.3.5 Common Antifatigue Biochemical Indexes 2448.4 Mechanisms of Antifatigue Peptides in Relieving Exercise Fatigue 2458.4.1 Regulation of Energy Metabolism 2458.4.2 Regulation of Inflammation 2478.4.3 Antioxidant Effect 2488.4.4 Regulation of Neurotransmitters 2498.4.5 Improvement of Exercise Endurance 2508.5 Current Status of Research and Its Applications 2528.5.1 Animal- Derived Peptides 2528.5.1.1 Oyster Peptides 2538.5.1.2 Jellyfish Peptides 2548.5.1.3 Sea Cucumber Peptides 2558.5.1.4 Freshwater Fish Peptides 2568.5.1.5 Marine Fish Peptides 2578.5.1.6 Livestock- Derived Peptides 2588.5.2 Plant- Derived Peptides 2598.5.3 Yeast- Derived Peptides 2608.5.4 Productions 261References 2629 Immune Regulatory Peptides 2699.1 Introduction 2699.1.1 Molecular Basis of Immunomodulation and Host Defense Mechanisms 2699.2 Introduction to Immunomodulatory Peptides 2709.3 Immunomodulatory Peptides 2719.3.1 Mechanisms and Biological Roles 2719.4 Applications in Disease Management 2719.4.1 Inflammatory and Autoimmune Disorders 2719.4.2 Cancer Immunotherapy 2729.4.3 Infectious Diseases and Antimicrobial Resistance 2729.4.4 Challenges and Innovations in Peptide Therapeutics 2729.4.5 Future Perspectives 2729.5 Conclusion 2739.6 Preparation 2739.6.1 Preparation Method of Immunomodulatory Peptide 2739.6.1.1 Organic Solvent Extraction 2739.6.1.2 Tissue Homogenization Extraction 2749.6.1.3 Enzymatic Hydrolysis 2749.6.1.4 Chemical Synthesis 2759.6.1.5 Microbial Fermentation 2779.6.1.6 Genetic Engineering 2779.6.2 Isolation and Purification Method of Immunomodulatory Peptides 2789.6.2.1 Ultrafiltration 2789.6.2.2 Chromatography 2799.6.2.3 Solvent Extraction 2809.6.2.4 Membrane Separation Continuous Coupling Technology 2809.7 Evaluation Method of Activity 2819.7.1 In Vitro Cell Models 2819.7.2 In Vivo Animal Models 2849.8 Mechanism Consideration 2869.8.1 Direct Regulation of Immune Cell Function 2879.8.2 Modulation of Cytokine Networks 2879.8.3 Regulation of Signal Transduction Pathways 2879.8.4 Regulation of Gut Immune Homeostasis 2889.8.5 Direct Regulation of Immune Cells by Functional Peptides 2889.8.5.1 Regulation of T Cells 2889.8.5.2 Regulation of B Cells 2899.8.5.3 Regulation of Macrophage Polarization 2899.8.5.4 Regulation of Natural Killer Cells 2899.8.6 Modulation of Cytokine Networks 2909.8.6.1 Regulation of Proinflammatory Cytokines 2909.8.6.2 Regulation of Anti- Inflammatory Cytokines 2909.8.6.3 Modulation of Cytokine Network Balance by Functional Peptides 2909.8.7 Regulation of Signaling Pathways by Functional Peptides 2919.8.7.1 NF- κB Signaling Pathway 2919.8.7.2 MAPK and JAK–STAT Pathways 2919.8.8 Role of Functional Peptides in Intestinal Immune Regulation 2919.9 Applications 2929.9.1 Application of Functional Peptides in Pulp Therapy 2929.9.1.1 Synergistic Antibacterial Effects and Dentin Regeneration 2929.9.1.2 Immunomodulatory Mechanisms 2929.9.2 Application of Functional Peptides in Tissue Engineering 2939.9.2.1 Serum- Free Expansion of Artificial Mesenchymal Stem Cells 2939.9.2.2 Tissue Repair and Regeneration 2939.9.3 Application of Functional Peptides in Immune Enhancement 2939.9.3.1 Peptide Nanofibers as Adjuvants 2939.9.3.2 Effects of Peptide Hydrolysates on Immune Function 2949.9.4 Application of Functional Peptides in Immune Suppression 2949.9.4.1 Peptides in Systemic Lupus Erythematosus 2949.9.4.2 Immunosuppressive Effects of VIP Peptide 294References 29510 Flavor Peptides 29910.1 Introduction 29910.2 Preparation of Flavor Peptides 30310.2.1 Methods for Hydrolysis and Microbial Fermentation 30310.2.2 Methods for Direct Extraction and Synthesis 30410.3 Taste Characteristics of Flavor Peptides 30510.3.1 The Effect of Amino Acids 30510.3.2 The Effect of Flavor and Matrix Interactions 30710.4 Taste Mechanism of Flavor Peptides 30810.4.1 Release and Migration of Flavor Peptides 30810.4.2 Taste Buds and Taste Cells 30810.4.3 Taste Receptors and Conductive Pathway 30810.5 Applications in the Food Industry 31210.5.1 Compound Condiments 31210.5.2 Functional Foods 314Abbreviations 315References 31511 Self- Assembling Peptides 32311.1 Sources 32311.1.1 Food- Derived SAPs 32311.1.2 Artificially Designed SAPs 32511.2 Supramolecular Structure of SAPs 32611.2.1 Nanotube 32711.2.2 Nanofiber 32711.2.3 Nanosheets/Ribbons 32711.2.4 Other Supramolecular Structures 32811.3 Mechanism Consideration 32911.3.1 Thermodynamics of Self- Assembly 32911.3.2 Dynamics of Self- Assembly 33011.3.3 Effects of Kinetic/Thermodynamic Interactions 33211.4 Function Properties of SAPs 33211.4.1 Amphiphilicity 33311.4.2 Gelation Ability 33311.4.3 Assembly Reversibility 33411.4.4 Photoelectric Properties 33511.5 Security Assessment 33511.5.1 Biocompatibility 33611.5.2 Immunogenicity 33611.5.3 Degradation Product Toxicity 33611.6 Applications 33711.6.1 Food Industry 33711.6.1.1 Nutrient Delivery Systems 33711.6.1.2 Food Detection 33711.6.1.3 Other Applications 33711.6.2 Biomedical Fields 33811.6.2.1 Pharmaceutical Effect 33811.6.2.2 Antibacterial Nanomaterials 33811.6.2.3 Tissue Engineering 33911.6.3 Other Applications 33911.7 Limitations and Challenges 340References 340Index 347