Marine Proteins and Peptides E-Book

• Herausgeber: John Wiley & Sons
• Kategorie: Fachliteratur
• Sprache: Englisch

Seitenzahl: 1698

Veröffentlichungsjahr: 2013

Beschreibung

Food proteins and bioactive peptides play a vital role in the growth and development of the body’s structural integrity and regulation, as well as having a variety of other functional properties. Land animal-derived food proteins such as collagen and gelatine carry risks of contamination (such as BSE). Marine-derived proteins, which can provide equivalents to collagen and gelatin without the associated risks, are becoming more popular among consumers because of their numerous health beneficial effects. Most marine-derived bioactive peptides are currently underutilized. While fish and shellfish are perhaps the most obvious sources of such proteins and peptides, there is also the potential for further development of proteins and peptides from sources like algae, sea cucumber and molluscs. Marine-derived proteins and peptides also have potential uses in novel products, with the possibility of wide commercialization in the food, beverage, pharmaceutical and cosmetic industries, as well as in other fields such as photography, textiles, leather, electronics, medicine and biotechnology.

Marine Proteins and Peptides: Biological Activities and Applications presents an overview of the current status, future industrial perspectives and commercial trends of bioactive marine-derived proteins and peptides. Many of the industrial perspectives are drawn from the food industry, but the book also refers to the pharmaceutical and cosmetics industries. There have recently been significant advances in isolating functional ingredients from marine bio-resources and seafood by-products for use in these industries, but little has been published, creating a knowledge gap, particularly with regard to the isolation and purification processes. This book is the first to fill that gap.

Marine Proteins and Peptides: Biological Activities and Applications is a valuable resource for researchers in marine biochemistry field as well as food industry managers interested in exploring novel techniques and knowledge on alternative food protein sources. It will become a standard reference book for researchers involved in developing marine bio-resources and seafood by-products for novel nutraceutical, cosmetics, and pharmaceutical applications. It will also appeal to managers and product developers in the food, pharmaceutical and cosmetics industries, particularly those looking to use marine-derived proteins and peptides as substitutes or replacements for unfashionable or outdated food components.

Leseprobe

Table of Contents

Title Page

Copyright

List of Contributors

Chapter 1: Marine-derived Peptides: Development and Health Prospects

1.1 Introduction

1.2 Development of Marine Peptides

1.3 Health Benefits of Marine Peptides

1.4 Conclusion

References

Chapter 2: Bioactive Proteins and Peptides from Macroalgae, Fish, Shellfish and Marine Processing Waste

2.1 Introduction

2.2 Macroalgal, Fish and Shellfish Proteins: Potential Sources of Bioactive Hydrolysates and Peptides

2.3 Enzymatic Hydrolysis of Macroalgal, Fish and Shellfish Processing Waste Proteins: Bioactive Protein Hydrolysates and Peptides

2.4 Endogenous Bioactive Peptides from Macroalgae, Fish and Shellfish

2.5 Bioactive Proteins from Macroalgae, Fish and Shellfish

2.6 Commercial Products Containing Marine-Derived Bioactive Protein Hydrolysates and Peptides

2.7 Conclusion

Acknowledgement

References

Chapter 3: Lectins with Varying Specificity and Biological Activity from Marine Bivalves

3.1 Introduction

3.2 Lectins

3.3 Isolation, Molecular Characterization and Carbohydrate Specificity of Bivalve Lectins

3.4 Biological Functions of Bivalve Lectins

Acknowledgements

References

Chapter 4: Digestive Enzymes from Marine Sources

4.1 Introduction

4.2 Biodiversity and Availability

4.3 Marine Biocatalysts

4.4 Digestive Enzymes

4.5 Lipases

4.6 Industrial Applications

References

Chapter 5: Kamaboko Proteins as a Potential Source of Bioactive Substances

5.1 Introduction

5.2 Creation of Healthier and Safer Foods

5.3 Enzymatic Modification of Food Proteins

5.4 Kamaboko

5.5 Chemical Properties of Kamaboko

5.6 Expression of Health the Function of Kamaboko Proteins

5.7 Antioxidative Activities of Kamaboko Proteins

5.8 Angiotensin I-Converting Enzyme-Inhibitory Activities of Kamaboko Proteins

5.9 Conclusion

References

Chapter 6: Biological Activities of Fish-protein Hydrolysates

6.1 Introduction

6.2 Angiotensin I-Converting Enzyme Inhibitors

6.3 Antioxidative Properties

6.4 Anticancer Activity

6.5 Antimicrobial and Antiviral Activity

6.6 Calcium-Binding Peptides

6.7 Appetite Suppression

6.8 Anticoagulant Activity

6.9 Immunostimulant Activity

6.10 Hypocholesterolemic Activity

6.11 Hormone-Regulating Properties

6.12 Other Biological Activities

References

Chapter 7: Biological Activities of Proteins and Marine-derived Peptides from Byproducts and Seaweeds

7.1 Introduction

7.2 Bioactive Peptides

7.3 Marine-derived Bioactive Peptides

7.4 Isolation and Characterisation of Marine-derived Bioactive Peptides

7.5 Lectins

7.6 Phycobiliproteins

7.7 Other Amino Acids and Peptides Present in and Derived from Macroalgae

7.8 Membrane Processing

7.9 Bioactivities of Marine-derived Peptides—inhibiting Proteases for Health

7.10 Heart-health Bioactive Peptides

7.11 Commercially Available Bioactive Peptides

7.12 Conclusion

References

Chapter 8: Ability of Diverse Marine Invertebrate Lectins to Regulate Cell Functions

8.1 Introduction

8.2 Does a Feather Star Lectin have a Role in Regenerative Biology?

8.3 A Novel Lectin from the Mediterranean Mussel Induces Apoptosis and Glycosphingolipid Interaction

8.4 Downregulation of the Gene Expression of an ABC Transporter by a Novel Lectin-glycosphingolipid Pathway Involving a Suel-type Lectin Domain

8.5 Perspectives on Studies of Invertebrate Lectins and Their Diverse Properties

References

Chapter 9: Routes in Innate Immunity Evolution: Galectins and Rhamnose-binding Lectins in Ascidians

9.1 Animal Lectins

9.2 Ascidians

9.3 Galectins

9.4 Rhamnose-binding Lectins

9.5 Conclusion

Acknowledgements

References

Chapter 10: Production of Lactobacilli Proteinases for the Manufacture of Bioactive Peptides: Part I—Upstream Processes

10.1 Introduction: Bioactive Peptides—Production And Functionalities

10.2 Lactobacilli Metabolism

10.3 The Proteolytic System of The Lactobacilli

10.4 Sources of Proteases and Advantages of Microbial Proteases

10.5 Marine Lactobacilli

10.6 Proteinase Production Requirements

10.7 Effect of Fermentation Modes on Cell Growth and Proteinase Production

10.8 Cell Systems for Proteinase Production

10.9 Statistical Methods and Mathematical Models

10.10 Conclusion

Acknowledgements

References

Chapter 11: Production of Lactobacilli Proteinases for the Manufacture of Bioactive Peptides: Part II—Downstream Processes

11.1 Introduction: Cell Recovery

11.2 Isolation: Proteinase-extraction Methodologies

11.3 Purification of Enzymes

11.4 Enzyme Concentration and Storage

11.5 Characterisation of Proteinase

11.6 Solvent and Enzyme Engineering for Enhanced Stability and Specificity

11.7 Conclusion

References

Chapter 12: Recovery of Proteins and their Biofunctionalities from Marine Algae

12.1 Introduction

12.2 Importance of Proteolytic Enzyme-assisted Extractions

12.3 Marine-algal Functional Proteins and Peptides with Bioactivity

12.4 Marine-algal Proteins: Potential Sources for Future Applications

12.5 Conclusion

References

Chapter 13: Fish Gelatin: A Versatile Ingredient for the Food and Pharmaceutical Industries

13.1 Introduction

13.2 Structural Features of Fish Gelatin

13.3 Improvement of Functional Properties

13.4 Applications in the Food Industry

13.5 Applications in the Pharmaceutical Industry

13.6 Conclusion

References

Chapter 14: Health Effects of Antioxidative and Antihypertensive Peptides from Marine Resources

14.1 Introduction

14.2 Antioxidative Peptides

14.3 Antihypertensive Peptides

14.4 Conclusion

References

Chapter 15: Potential Novel Therapeutics: Some Biological Aspects of Marine-derived Bioactive Peptides

15.1 Introduction

15.2 Marine-derived Proteins and Biopeptides with Antihypertensive Activity

15.3 Anticancer Effects of Marine-derived Bioactive Peptides

15.4 Antiviral Bioactivities of Marine-derived Bioactive Peptides

15.5 The Future of Marine Peptides as Therapeutics

References

Chapter 16: Hormone-like Peptides Obtained by Marine-protein Hydrolysis and Their Bioactivities

16.1 Introduction

16.2 Growth Hormone-Release Peptides

16.3 Opioid-Like Peptides

16.4 Immunomodulating Peptides

16.5 Glucose Uptake-Stimulating Peptides

16.6 Secretagogue and Calciotropic Activities

16.7 Limitations on the use of Hormone-like Peptides as Nutraceuticals

16.8 Further Development and Research Needs

References

Chapter 17: Antimicrobial Activities of Marine Protein and Peptides

17.1 Introduction

17.2 Preparation, Purification and Characterization

17.3 In Vitro Antimicrobial Studies

17.4 Antimicrobial Mechanisms

17.5 Applications and Prospects in Food Preservation

17.6 Conclusion

References

Chapter 18: Production and Antioxidant Properties of Marine-derived Bioactive Peptides

18.1 Introduction

18.2 Production of Antioxidant Peptides

18.3 Antioxidant Mechanism and Structure–activity Relationship

18.4 Industrial Applications and Perspectives

References

Chapter 19: Marine Peptides and Proteins with Cytotoxic and Antitumoral Properties

19.1 Introduction

19.2 Current Pipeline of Oncological Drugs Based on Natural Products

19.3 Current Pipeline of Marine Peptides with Antitumoral Activity

19.4 Major Biological Sources of Marine Cytotoxic Peptides and Proteins

19.5 Structural Motifs in Cytotoxic Peptides

19.6 Cytotoxic Acyclic Peptides

19.7 Cytotoxic Cyclic Peptides

19.8 Cytotoxic (Poly)Peptides Obtained by Enzymatic Hydrolysis of Seafood

19.9 Cytotoxic Polypeptides

19.10 Conclusion

19.11 Acknowledgments

References

Chapter 20: ACE-inhibitory Activities of Marine Proteins and Peptides

20.1 Introduction

20.2 Determination of ACE-inhibitory Peptide Activity

20.3 ACE-inhibitory Peptides from Marine Sources

20.4 Types of ACE-Inhibitor Peptide

20.5 Structure–Activity Relationships of ACE-Inhibitory Peptides

20.6 Conclusion

References

Chapter 21: Isolation and Biological Activities of Peptides from Marine Microalgae by Fermentation

21.1 Introduction

21.2 Utilization of Fermentation to Hydrolyze Protein

21.3 Microalgae As a Source of Protein

21.4 Metabolites of Proteolytic Hydrolysis by Fermentation

21.5 Hydrolyzed Microalgal Peptide Application

21.6 Conclusion

References

Chapter 22: Antioxidant Activities of Marine Peptides from Fish and Shrimp

22.1 Introduction

22.2 Production, Isolation, and Purification of Antioxidant Peptides

22.3 Methods Used to Measure Antioxidant Activity

22.4 Antioxidant Activity of Peptides

22.5 Antioxidant Mechanisms of Peptides

22.6 Applications and Prospects

References

Chapter 23: Fish-elastin Hydrolysate: Development and Impact on the Skin and Blood Vessels

23.1 Introduction

23.2 Starter Materials for Fish-elastin Hydrolysate

23.3 Preparation of Skipjack-elastin Hydrolysate

23.4 Impact of Ingestion of Skipjack-elastin Hydrolysate on Skin Conditions

23.5 Impact of Skipjack-elastin Hydrolysate on Blood Vessels

23.6 Safety of Skipjack-elastin Hydrolysate

23.7 Identification of Food-derived Elastin Peptide in Human Blood

23.8 Effect of Food-derived Elastin-peptide Pro-gly on Cells

23.9 Conclusion

References

Chapter 24: Free Radical-scavenging Activity of Marine Proteins and Peptides

24.1 Introduction

24.2 Formation of Free Radicals and Methods of Assaying Antioxidant Activity

24.3 Free Radical-scavenging Activity of Marine Proteins and Peptides

24.4 Conclusion

References

Chapter 25: Marine-derived Bioactive Peptides: Their Cardioprotective Activities and Potential Applications

25.1 Introduction

25.2 Cardiovascular Diseases and Nutraceuticals

25.3 Sources of Marine Peptides

25.4 Development of Marine Bioactive Peptides

25.5 Oxidative Stress

25.6 Antihypertensive Activity

25.7 Anticoagulant Activity

25.8 Conclusion

References

Chapter 26: Biological Activities of Marine Bioactive Peptides

26.1 Introduction

26.2 Physiological Properties of Marine Bioactive Peptides

26.3 Conclusion

Acknowledgement

References

Chapter 27: Shark Fin Cartilage: Uses, Extraction and Composition Analysis

27.1 Introduction

27.2 History

27.3 Uses

27.4 Shark-fin Processing

27.5 Extraction of Elastoidin and Chondroitin Sulfate

27.6 Composition Analysis

References

Chapter 28: Marine Bioactive Peptide Sources: Critical Points and the Potential for New Therapeutics

28.1 Introduction

28.2 Marine Bioactive Peptide Sources

28.3 Critical Points and the Potential for New Therapeutics

28.4 Conclusion

References

Chapter 29: Applications of Marine-derived Peptides and Proteins in the Food Industry

29.1 Introduction

29.2 Marine-derived Proteins and Peptides Used in the Food Industry

29.3 Collagen and Gelatin

29.4 Extraction and Isolation of Marine-derived Proteins and Peptides

29.5 Food-related Applications of Marine-derived Proteins and Peptides

29.6 Conclusion

References

Chapter 30: Processing and Industrial Aspects of Fish-scale Collagen: A Biomaterials Perspective

30.1 Introduction

30.2 Structure and Composition of Collagen

30.3 Synthesis of Collagen

30.4 Type-i Collagen

30.5 Recombinant Collagen

30.6 Fish's Potential as an Alternative Source of Collagen

30.7 Emerging Applications of Type-I Collagen

30.8 Conclusion

Acknowledgement

References

Chapter 31: Properties, Biological Advantages and Industrial Significance of Marine Peptides

31.1 Introduction

31.2 Marine-peptide Properties

31.3 Industrial Development of Marine Bioactive Peptides

31.4 Biological Applications of Marine Peptides

31.5 Conclusion

References

Chapter 32: Muscle Proteins of Fish and Their Functions

32.1 Introduction

32.2 Fish Muscles

32.3 Myoglobin and Myofibrillar Proteins of Fish Muscle

32.4 Sarcoplasmic Protein

32.5 Antifreeze Proteins

References

Chapter 33: Marine-derived Collagen: Biological Activity and Application

33.1 Introduction

33.2 Sources of Marine Collagen

33.3 Applications of Marine Collagen

References

Chapter 34: Marine Antifreeze Proteins: Types, Functions and Applications

34.1 Introduction

34.2 Types of Marine AFP

34.3 Preparation of Fish AFPS

34.4 AFP Applications

34.5 Conclusion

References

Chapter 35: Antimicrobial Peptides in Marine Mollusks and their Potential Applications

35.1 Introduction

35.2 Characteristics of AMPS

35.3 Diversity Of Amps In Marine Mollusks

35.4 Applications of Mollusk-derived AMPS

References

Chapter 36: Protein Hydrolysates and Bioactive Peptides from Seafood and Crustacean Waste: Their Extraction, Bioactive Properties and Industrial Perspectives

36.1 Introduction

36.2 Overall Chemical Composition of Seafood and Crustaceans

36.3 Extraction of Protein Hydrolysates and Bioactive Peptides from Seafood and Crustacean Waste

36.4 Characterization of Fish-protein Hydrolysates and Bioactive Peptides

36.5 Functional and Bioactive Properties of Proteins and Peptides from Seafood and Crustacean Waste

36.6 Conclusion

References

Chapter 37: Production and Health Effects of Peptides from Fish Proteins

37.1 Introduction

37.2 Sources of Fish Peptides

37.3 Production of Fish Peptides

37.4 Health-promoting ability of fish peptides

37.5 Future Trends of Peptides from Fish Proteins

37.6 Conclusion

References

Index

This edition first published 2013 © 2013 by John Wiley & Sons, Ltd.

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Library of Congress Cataloging-in-Publication Data

Kim, Se-Kwon, author.

Marine proteins and peptides : biological activities and applications / Se-Kwon Kim.

p. ; cm.

Includes bibliographical references and index.

Summary: ‘‘This book will provide cutting edge content on both the human health benefits of marine proteins and peptides, and their industrial applications’’ – Provided by publisher.

ISBN 978-1-118-37506-8 (cloth)

I. Title.

[DNLM: 1. Dietary Proteins– pharmacology. 2. Aquatic Organisms. 3. Drug Discovery. 4. Food Industry. 5. Peptide Hydrolases – pharmacology. 6. Seafood. QU 55.4]

615.1$′9–dc23

2012048619

A catalogue record for this book is available from the British Library.

Wiley also publishes its books in a variety of electronic formats. Some content that appears in print may not be available in electronic books.

Cover image: iStock © Olga Khoroshunova

Cover design by Meaden Creative

List of Contributors

N. AbdullahInstitute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, Malaysia

Mausumi AdhyaNSHM Faculty of Engineering and Technology, NSHM Knowledge Campus, Durgapur, West Bengal, India

Abdul Bakrudeen Ali AhmedInstitute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, Malaysia

Byul-Nim AhnDepartment of Chemistry, Pukyong National University, Nam-Gu, Busan, Republic of Korea

Dominic AgyeiBioengineering Laboratory, Department of Chemical Engineering, Monash University, Clayton, Victoria, Australia

Fernando AlbericioInstitute for Research in Biomedicine, Barcelona, Spain; CIBER-BBN, Networking Centre on Bioengineering, Biomaterials and Nanomedicine, Barcelona, Spain; University of Barcelona, Department of Organic Chemistry, Barcelona, Spain

Anil Kumar AnalFood Engineering and Bioprocess Technology, Asian Institute of Technology, Klongluang, Thailand

Loriano BallarinDepartment of Biology, University of Padova, Padova, Italy

Luísa BarreiraCentre of Marine Sciences, University of Algarve, Faro, Portugal

Irineu BatistaInstituto Nacional dos Recursos Biológicos, I.P./IPIMAR, Portugal

Matteo CammarataDepartment of Environmental Biology and Biodiversity, University of Palermo, Palermo, Italy

Bishnu Pada ChatterjeeDepartment of Natural Science, West Bengal University of Technology, Kolkata, India

Luísa CustódioCentre of Marine Sciences, University of Algarve, Faro, Portugal

Michael K. DanquahBioengineering Laboratory, Department of Chemical Engineering, Monash University, Clayton, Victoria, Australia

Pallab DattaBiomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India

Mahanama De ZoysaCollege of Veterinary Medicine, Chungnam National University, Yuseong-gu, Daejeon, Republic of Korea

Santanu DharaBiomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India

Shiyuan DongCollege of Food Science and Engineering, Ocean University of China, China

Karl-Erik EilertsenNorwegian College of Fishery Science, Faculty of Biosciences, Fisheries and Economics, University of Tromsø, Breivika, Norway

Edel O. ElvevollNorwegian College of Fishery Science, Faculty of Biosciences, Fisheries and Economics, University of Tromsø, Breivika, Norway

Richard J. FitzGeraldDepartment of Life Sciences, University of Limerick, Limerick, Ireland

Nicola FranchiDepartment of Biology, University of Padova, Padova, Italy

Yuki FujiiLaboratory of Glycobiology and Marine Biochemistry, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, Yokohama, Japan; Division of Functional Morphology, Department of Pharmacy, Faculty of Pharmaceutical Science, Nagasaki International University, Sasebo, Nagasaki, Japan

Hugo Sergio GarcíaUnidad de Investigación y Desarrollo en Alimentos, Instituto Tecnológico de Veracruz, Veracruz, Mexico

Venkateshwarlu GudipatiFishery Resources, Harvest and Post Harvest Management Division, Central Institute of Fisheries Education, Versova, Mumbai, India

Pádraigín A. HarnedyDepartment of Life Sciences, University of Limerick, Limerick, Ireland

Imtiaj HasanLaboratory of Glycobiology and Marine Biochemistry, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, Yokohama, Japan; Department of Biochemistry and Molecular Biology, Faculty of Science, Rajshahi University, Rajshahi, Bangladesh

Maria HayesFood BioSciences Department, Teagasc Food Research Centre, Ashtown, Dublin, Ireland

Chamila JayasingheDepartment of Food Science and Technology, Faculty of Livestock, Fisheries and Nutrition, Wayamba University of Sri Lanka, Makandura, Gonawilla, Sri Lanka

Barana C. JayawardanaDepartment of Animal Science, Faculty of Agriculture, University of Peradeniya, Peradeniya, Sri Lanka

Ida-Johanne JensenNorwegian College of Fishery Science, Faculty of Biosciences, Fisheries and Economics, University of Tromsø, Breivika, Norway

You-Jin JeonSchool of Marine Biomedical Sciences, Jeju National University, Jeju, Republic of Korea

Ramiro Baeza JiménezDepartamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica-CSIC, Madrid, Spain

Norihisa KaiNational Fisheries University, Yamaguchi, Japan

Robert A. KanalyLaboratory of Environmental Microbiology and Toxicology, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, Yokohama, Japan

Sung-Ho KangDivision of Polar Life Sciences, Korea Polar Research Institute and Department of Polar Sciences, University of Science and Technology, Incheon, Republic of Korea

Sarkar M. A. KawsarLaboratory of Glycobiology and Marine Biochemistry, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, Yokohama, Japan; Laboratory of Carbohydrate and Protein Chemistry, Department of Chemistry, Faculty of Science, University of Chittagong, Chittagong, Bangladesh

Hak Jun KimDivision of Polar Life Sciences, Korea Polar Research Institute and Department of Polar Sciences, University of Science and Technology, Incheon, Republic of Korea

Se-Kwon KimMarine Bioprocess Research Center, Pukyong National University, Busan, Republic of Korea; Department of Chemistry, Pukyoung National University, Nam-Gu, Busan, Republic of Korea

Suranga P. KodithuwakkuDepartment of Animal Science, Faculty of Agriculture, University of Peradeniya, Peradeniya, Sri Lanka

Yasuhiro KoideLaboratory of Glycobiology and Marine Biochemistry, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, Yokohama, Japan

Rune LarsenNorwegian College of Fishery Science, Faculty of Biosciences, Fisheries and Economics, University of Tromsø, Breivika, Norway

Jun Hyuck LeeDivision of Polar Life Sciences, Korea Polar Research Institute and Department of Polar Sciences, University of Science and Technology, Incheon, Republic of Korea

Sung Gu LeeDivision of Polar Life Sciences, Korea Polar Research Institute and Department of Polar Sciences, University of Science and Technology, Incheon, Republic of Korea

Zunying LiuCollege of Food Science and Engineering, Ocean University of China, China

Ruvini LiyanageInstitute of Fundamental Studies, Kandy, Sri Lanka

Hanne K. MæhreNorwegian College of Fishery Science, Faculty of Biosciences, Fisheries and Economics, University of Tromsø, Breivika, Norway

Buddika O. MalaweeraFaculty of Veterinary Medicine, Chungnam National University, Daejeon, Republic of Korea

Oscar Martínez-AlvarezInstitute of Food Science, Technology and Nutrition (ICTAN-CSIC), Madrid, Spain

Takeshi NagaiGraduate School of Agricultural Sciences, Yamagata University, Yamagata, Japan; The United Graduate School of Agricultural Sciences, Iwate University, Iwate, Japan; Graduate School, Prince of Songkla University, Songkhla, Thailand

Misako NakabaHayashikane Sangyo Co. Ltd., Yamaguchi, Japan

Dai-Hung NgoDepartment of Chemistry, Pukyong National University, Busan, Republic of Korea

Dai-Nghiep NgoDepartment of Biochemistry, Faculty of Biology, University of Science, VNU-HCM Ho Chi Minh City, Vietnam

Athapol NoomhormFood Engineering and Bioprocess Technology, Asian Institute of Technology, Klongluang, Thailand

A. NoorlidahInstitute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, Malaysia

Yukiko OgawaDivision of Microbiology, Department of Pharmacy, Faculty of Pharmaceutical Science, Nagasaki International University, Sasebo, Nagasaki, Japan

Yasuhiro OzekiLaboratory of Glycobiology and Marine Biochemistry, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, Yokohama, Japan

Pallabi PalBiomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India

R. PallelaDBT-ICGEB Center for Advanced Bioenergy Research, ICGEB, New Delhi, India

Ratih PangestutiMarine Bioprocess Research Center, Pukyong National University, Busan, Republic of Korea; Marine Biochemistry Laboratory, Department of Chemistry, Pukyong National University, Busan, Republic of Korea

Nicolò ParrinelloDepartment of Environmental Biology and Biodiversity, University of Palermo, Palermo, Italy

Ravichandra PotumarthiBioengineering Laboratory, Department of Chemical Engineering, Monash University, Clayton, Victoria, Australia

K. PriyaPSG College of Arts and Science, Coimbatore, Tamilnadu, India

C. Senaka RanadheeraDepartment of Agricultural Systems, Faculty of Agriculture, Rajarata University of Sri Lanka, Anuradhapura, Sri Lanka

D. M. Dilan RasikaDepartment of Animal Science, Faculty of Agriculture, University of Peradeniya, Peradeniya, Sri Lanka

Juan Antonio Noriega RodríguezDepartamento de Ingeniería Química y Metalurgia, Universidad de Sonora, Sonora, Mexico

M. T. RosnaInstitute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, Malaysia

BoMi RyuMarine Bioprocess Research Center, Pukyong National University, Busan, South Korea

Kalpa SamarakoonSchool of Marine Biomedical Sciences, Jeju National University, Jeju, Republic of Korea

Soumi Dey SarkarBiomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India

Kenji SatoDivision of Applied Life Sciences, Graduate School of Life and Environment Sciences, Kyoto Prefectural University, Kyoto, Japan

Mahinda SenevirathneDepartment of Food Science and Technology, Faculty of Applied Sciences, Sabaragamuwa University of Sri Lanka, Sri Lanka

Yasutaka ShigemuraDepartment of Nutrition, Faculty of Domestic Science, Tokyo Kasei University, Tokyo, Japan

Eri ShiratsuchiHayashikane Sangyo Co. Ltd., Yamaguchi, Japan

Shigeki SugawaraDivision of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan

Nobutaka SuzukiNagoya Research Institute, Aichi, Japan

R. M. TahaInstitute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, Malaysia

Yasuhiro TanoueNational Fisheries University, Yamaguchi, Japan

João VarelaCentre of Marine Sciences, University of Algarve, Faro, Portugal

Janak K. VidanarachchiDepartment of Animal Science, Faculty of Agriculture, University of Peradeniya, Peradeniya, Sri Lanka

M. VijayakumarInstitute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, Malaysia

Catarina Vizetto-DuarteCentre of Marine Sciences, University of Algarve, Faro, Portugal

Thanh-Sang VoDepartment of Chemistry, Pukyong National University, Busan, Republic of Korea

Punchira VongsawasdiDepartment of Microbiology, King Mongkut's University of Technology, Thonburi, Thailand

Qiukuan WangCollege of Food Science and Engineering, Dalian Ocean University, Dalian, China

Tao WangCollege of Food Science and Engineering, Dalian Ocean University, Dalian, China; Center for Excellence in Post-Harvest Technologies, North Carolina A&T State University, Kannapolis, NC, USA

Isuru WijesekaraMarine Bioprocess Research Center, Department of Chemistry, Pukyong National University, Busan, Republic of Korea

W. M. Niluni Methsala WijesundaraFaculty of Animal Science and Export Agriculture, Uva Wellassa University of Sri Lanka, Badulla, Sri Lanka

Michio YamadaHayashikane Sangyo Co. Ltd., Yamaguchi, Japan

Hidetaro YasumitsuExpert Laboratory for Life Environments, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, Yokohama, Japan

Mingyong ZengCollege of Food Science and Engineering, Ocean University of China, China

Qiancheng ZhaoCollege of Food Science and Engineering, Dalian Ocean University, Dalian, China

Yuanhui ZhaoCollege of Food Science and Engineering, Ocean University of China, China

Chapter 1

Marine-derived Peptides: Development and Health Prospects

Se-Kwon Kim1,2 and Isuru Wijesekara2

1Marine Bioprocess Research Center, Department of Chemistry, Pukyong National University, Busan, Republic of Korea

2Department of Chemistry, Pukyoung National University, Nam-Gu, Busan, Republic of Korea

1.1 Introduction

The role of protein in the human diet has been acknowledged recently worldwide. Dietary proteins have become a source of physiologically active components, which have a positive impact on the body's function after gastrointestinal digestion. Bioactive peptides may be produced by one of three methods: solvent extraction, enzymatic hydrolysis and microbial fermentation of food proteins. Marine-derived bioactive food proteins and biopeptides are often effective in promoting health and lead to a reduction in the risk of disease. Recently, much attention has been paid by consumers to natural bioactive compounds as functional ingredients. Hence, it can be suggested that marine-derived bioactive food proteins and biopeptides are alternative sources for synthetic ingredients that can contribute to consumers' well-being, as a part of functional foods, pharmaceuticals and/or cosmetics. Furthermore, they can be utilized in other industries such as medicine, animal feed, printing, textile and so on. This chapter presents an overview of the development, health effects, industrial perspectives and commercial trends of marine-derived bioactive food proteins and biopeptides used in the food, pharmaceutical and cosmetic industries.

1.2 Development of Marine Peptides

Enzymatic hydrolysis of marine-derived proteins allows preparation of bioactive peptides, which can be obtained by in vitro hydrolysis of protein substrates using appropriate proteolytic enzymes. The physicochemical conditions of the reaction media, such as the temperature and pH of the protein solution, must then be adjusted in order to optimize the activity of the enzyme used. Proteolytic enzymes from microbes, plants and animals can be used for the hydrolysis process of marine proteins in order to develop bioactive peptides. Enzymatic hydrolysis is carried out under optimal conditions to obtain a maximum yield of peptides. For example, α-chymotrypsin, papain, Neutrase and trypsin have been applied to the hydrolysis of tuna dark muscle under optimal pH and temperature conditions for each by Qian et al. (2007).

One of the most important factors in producing bioactive peptides with desired functional properties for use as functional materials is their molecular weight (Deeslie & Cheryan, 1981). Therefore, for efficient recovery and in order to obtain bioactive peptides with a desired molecular size and functional property, an ultrafiltration membrane system can be used. This system's main advantage is that the molecular-weight distribution of the desired peptide can be controlled by adoption of an appropriate ultrafiltration membrane (Cheryan & Mehaia, 1990). In order to obtain functionally active peptides, it is normal to use three enzymes in order to allow sequential enzymatic digestion. Moreover, it is possible to obtain serial enzymatic digestions in a system using a multistep recycling membrane reactor combined with an ultrafiltration membrane system to separate marine-derived bioactive peptides (Jeon et al., 1999). This membrane bioreactor technology has recently emerged for the development of bioactive compounds and has potential for the utilization of marine proteins as value-added neutraceuticals with beneficial health effects.

1.3 Health Benefits of Marine Peptides

Marine-derived antihypertensive peptides have shown potent antihypertensive effect with angiotensin-I-converting enzyme (ACE)-inhibition activity. The potency of these marine-derived peptides has been expressed as an IC50 value, which is the the ACE-inhibitor concentration that inhibits 50% of ACE activity. The inhibition modes of ACE-catalyzed hydrolysis of these antihypertensive peptides have been determined by Lineweaver–Burk plots. Competitive ACE-inhibitory peptides have been reported most frequently (Lee et al., 2010; Zhao et al., 2009). These inhibitors can bind to the active site in order to block it or to the inhibitor-binding site remote from the active site in order to alter the enzyme conformation such that the substrate no longer binds to the active site. In addition, a noncompetitive mechanism has been observed in some peptides (Qian et al., 2007; Suetsuna & Nakano, 2000). Numerous in vivo studies of marine-derived antihypertensive peptides in spontaneously hypertensive rats have shown potent ACE-inhibition activity (Fahmi et al., 2004; Zhao et al., 2009).

Recently, a number of studies have observed that peptides derived from different marine-protein hydrolysates act as potential antioxidants; these have been isolated from marine organisms such as jumbo squid, oyster, blue mussel, hoki, tuna, cod, Pacific hake, capelin, scad, mackerel, Alaska pollock, conger eel, yellow fin sole, yellow stripe trevally and microalgae (Kim & Wijesekara, 2010). The beneficial effects of antioxidant marine bioactive peptides in scavenging free radicals and reactive oxygen species (ROS) and in preventing oxidative damage by interrupting the radical chain reaction of lipid peroxidation are well known. The inhibition of lipid peroxidation by marine bioactive peptide, isolated from jumbo squid, has been determined by a linoleic acid model system; its activity was much higher than α-tocopherol and was close to the highly active synthetic antioxidant BHT (Mendis et al., 2005b).

Marine-derived antimicrobial peptides have described in the hemolymph of many marine invertebrates (Tincu & Taylor, 2004), including the spider crab (Stensvag et al., 2008), oyster (Liu et al., 2008), American lobster (Battison et al., 2008), shrimp (Bartlett et al., 2002) and green sea urchin (Li et al., 2008). Antibacterial activity has been reported in the hemolymph of the blue crab, Callinectus sapidus; it was highly inhibitory to Gram-negative bacteria (Edward et al., 1996). Although there are several reports of antibacterial activity in seminal plasma, few antibacterial peptides have been reported in the mud crab, Scylla serrata (Jayasankar & Subramonium, 1999).

The anticoagulant marine bioactive peptides have rarely been reported, but have been isolated from marine organisms such as marine echiuroid worm, starfish and blue mussel. Moreover, marine anticoagulant proteins have been purified from blood ark shell and yellow fin sole. The anticoagulant activity of these peptides has been determined by prolongation of activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TP) assays and compared with heparin, the commercial anticoagulant.

Biologically active marine peptides are food-derived peptides that exert a physiological, hormone-like effect beyond their nutritional value, and have a possible role in reducing the risk of cardiovascular diseases by lowering plasma cholesterol level and show anticancer activity through a reduction in cell proliferation on human breast-cancer cell lines. Moreover, calcium-binding bioactive peptides derived from pepsin hydrolysates of the marine fish species Alaska pollock (Theragra chalcogramma) and hoki frame (Johnius belengerii) can be introduced to Asians with lactose indigestion and intolerance as an alternative to dairy products (Kim & Wijesekara, 2010).

1.4 Conclusion

Marine-derived proteins and bioactive peptides have potential for use as functional ingredients in neutraceuticals and pharmaceuticals due to their effectiveness in both prevention and treatment of diseases. Moreover, cost-effective and safe drugs can be produced from marine bioactive proteins and peptides. Further studies and clinical trials are needed for these bioactive proteins and peptides.

References

Cheryan, M., Mehaia, M. A. (1990). Membrane bioreactors: enzyme process. In: Schwartzberg, H., Rao, M. A. eds. Biotechnology and Food Process Engineering. Marcel Dekker: New York.

Deeslie, W. D., Cheryan, M. (1981). Continuous enzymatic modification of proteins in an ultrafiltration reactor. Journal of Food Science, 46, 1035–1042.

Jeon, Y. J., Byun, H. G., Kim, S. K. (1999). Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochemistry, 35, 471–478.

Lee, S. H., Qian, Z. J., Kim, S. K. (2010). A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. Food Chemistry, 118, 96–102.

Qian, Z. J., Je, J. Y., Kim, S. K. (2007). Antihypertensive effect of angiotensin I converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle, Thunnus obesus. Journal of Agricultural and Food Chemistry, 55, 8398–8403.

Chapter 2

Bioactive Proteins and Peptides from Macroalgae, Fish, Shellfish and Marine Processing Waste

Pádraigín A. Harnedy and Richard J. FitzGerald

Department of Life Sciences, University of Limerick, Limerick, Ireland

2.1 Introduction

The marine environment, which makes up more than 70% of the earth's surface, represents a vast, relatively untapped resource for biofunctional compound mining. To date, numerous nitrogenous components (protein, peptides and amino acids) with diverse biological activities have been identified in macroalgae, fish and shellfish. Furthermore, macroalgae, fish, shellfish and marine processing waste contain significant quantities of high-quality protein (10–47% (w/w)), which represents a good candidate raw material for further biofunctional peptide mining.

Significant quantities of waste are generated annually from onshore processing of fish and shellfish and during the processing of aquacultured fish and shellfish. For example, in Norway 800 000 metric tonnes of byproducts were generated by fish processing industries in 2009 (Rustad et al., 2011). It has been estimated that up to 25% of fish and shellfish can end up as waste. In general, this waste material consists of trimmings, viscera, fins, bones, head, skin, undersized fish and shellfish, damaged shellfish and shells. These waste components contain significant levels of protein with potential biofunctional and technofunctional properties. The mining and subsequent exploitation of marine byproducts/waste streams for components with bioactive properties represents a specific strategy for added-value generation. Furthermore, it provides a solution to the legal restrictions, high costs and environmental problems associated with disposal of such waste material. However, regulations concerning the treatment, storage and transport of fish and shellfish byproducts must be carefully adhered to if these raw materials are to be used as sources of functional food ingredients.