This book compiles the latest research on food-derived opioid peptides, particularly those derived from milk. It describes in detail the structure, classification and, more importantly, physiological functions of these peptides. Presenting an interesting overview of the opioid receptors and receptor ligands, it examines the absorption, transport and degradation of these opioid peptides. Further, it highlights the production of β-casomorphins from only one variant of β-casein and its biological activities, and explores the generation of αb‐lactorphin from bovine αb‐lactalbumin and βb‐lactorphin. The book also includes a section on the use of advanced biochemical and pharmacological techniques to analyze opioid peptides, discussing the extraction of protein from food sources, protein purification followed by SGID, filtration of peptides and analysis using analytical HPLC. Lastly, it offers insights into the significance of these peptides in the pharmaceutical industry and their potential role as therapeutic agents.
This timely book is useful for researchers and students in the field of food sciences, dairy science, agriculture and pharmacology. It is also of interest to industry experts.
Author(s): Mohammad Raies Ul Haq
Edition: 1st ed. 2020
Publisher: Springer
Year: 2020
Language: English
Pages: 156
Preface
Acknowledgments
Contents
About the Author
Abbreviations
1: Significant Food-Derived Opioid Peptides
1.1 Introduction
1.2 Basic Structural Properties of Exorphins
1.3 Major Food-Derived Exorphins
1.3.1 Casomorphins
1.3.2 Lactorphins and Lactoferroxins
1.3.3 Casoxins
1.3.4 Gluten Exorphins
1.3.5 Rubiscolins
1.3.6 Soymorphins
1.3.7 Oryzatensin
1.4 Receptors for Food-Derived Exorphins
1.4.1 μ-Opioid Receptor (MOP)
1.4.2 δ-Opioid Receptor (DOP)
1.4.3 κ-Opioid Receptor (KOP)
1.5 Production of Food-derived Exorphins
1.5.1 Fermentation
1.5.2 Simulated Gastrointestinal Digestion (SGID)
1.6 Absorption and Fate of Exorphins
1.7 Transport to Blood and Across Blood-Brain Barrier (BBB)
References
2: Structure and Production of Casomorphins
2.1 Introduction
2.2 Structure of Casomorphins
2.3 Classification of Casomorphins
2.3.1 Based on Chain Length
2.3.2 Based on Milk Source
2.4 Production of Casomorphins
2.5 Effect of Milk Processing on Casomorphin Production
2.6 Opioid Activity of Casomorphins
References
3: Biological Activities of Casomorphins
3.1 Introduction
3.2 Gut Responses
3.2.1 Gut Inflammation
3.2.2 Gut Motility
3.2.3 Miscellaneous Gut Functions
3.3 Sudden Infant Death Syndrome (SIDS) and Heart-Related Attributes
3.4 Mucus Formation
3.5 Immunological Role
3.6 Miscellaneous Activities
References
4: Lactorphins and Lactoferroxins
4.1 Introduction
4.2 Structure of Lactorphins and Lactoferroxins
4.2.1 Structure of Lactorphins
4.2.2 Structure of Lactoferroxins
4.3 Classification of Lactorphins and Lactoferroxins
4.4 Opioid Activity of Lactorphins and Lactoferroxins
4.5 Production of Lactorphins and Lactoferroxins
4.6 Physiological Effects of Lactorphins and Lactoferroxins
4.6.1 Cardiovascular Functions
4.6.2 Miscellaneous Functions
References
5: Casoxins
5.1 Introduction
5.2 Structure of Casoxins
5.3 Classification of Casoxins
5.4 Opioid Activity of Casoxins
5.5 Production of Casoxins
5.6 Biological Activities of Casoxins
References
6: Gluten Exorphins
6.1 Introduction
6.2 Structure of Gluten Exorphins
6.3 Classification of Gluten Exorphins
6.4 Opioid Activity of Gluten Exorphins
6.5 Production of Gluten Exorphins
6.6 Biological Role of Gluten Exorphins
6.6.1 Celiac Disease
6.6.2 Prolactin Secretion
6.6.3 Behavioral and Pharmacological Effects
6.6.4 Hormonal and Gastrointestinal Functions
References
7: Rubiscolins, Soymorphins, and Oryzatensin
7.1 Introduction
7.2 Structure
7.2.1 Rubiscolins
7.2.2 Soymorphins
7.2.3 Oryzatensin
7.3 Classification
7.3.1 Rubiscolins 5 and 6
7.3.2 Soymorphins 5, 6, and 7
7.3.3 Oryzatensin
7.4 Opioid Activity
7.4.1 Rubiscolin
7.4.2 Soymorphins
7.4.3 Oryzatensin
7.5 Production
7.5.1 Rubiscolins
7.5.2 Soymorphins
7.5.3 Oryzatensin
7.6 Physiological Role
7.6.1 Rubiscolins
7.6.2 Soymorphins
7.6.3 Oryzatensin
References
8: Analysis of Food-derived Opioid Peptides
8.1 Introduction
8.2 Isolation of Proteins from Food Source
8.2.1 Isolation of Alpha, Beta, and Kappa Caseins from Cow Milk
8.2.2 Milk Alpha-lactalbumin and Beta-lactoglobulin
8.2.3 Milk Lactoferrin
8.2.4 Wheat Glutenin and Gliadin
8.2.5 Spinach RuBisCo
8.2.6 Soy Beta-conglycinin
8.2.7 Rice Albumin
8.3 Dialysis of Extracted Proteins
8.4 Protein Estimation by Folin Lowry Method
8.5 Purity Analysis by SDS-PAGE
8.6 Simulated Gastrointestinal Digestion
8.7 Ultrafiltration of Hydrolysates
8.8 Analysis of Opioid Peptides
8.8.1 Detection on Analytical HPLC
8.8.2 Peptide Fraction Collection on Preparative HPLC
8.8.3 Freeze Lyophilization
8.8.4 Opioid Activity Determination
8.8.5 Mass Spectroscopy of Peptide Fractions
8.8.6 In Silico Approach
8.8.7 Estimation of Opioid Peptides by ELISA
References
9: Conclusions and Future Perspectives
9.1 Structural Features of Food-derived Exorphins
9.2 Classification of Food-derived Exorphins
9.3 Opioid Activity of Food-Derived Exorphins
9.4 Production of Food-Derived Exorphins
9.5 Biological Activities of Food-Derived Exorphins
9.6 Overall Conclusions
9.7 Future Perspectives
References
