Contents

Cover

Title page

Copyright page

Preface

Chapter 1: Soy Protein: State-of-the-Art, New Challenges and Opportunities

1.1 Soy Protein: Introduction, Structure and Properties Relationship
1.2 Advances in Soy Protein-Based Nanocomposites
1.3 Applications of Soy Protein-Based Blends, Composites, and Nanocomposites
1.4 Biomedical Applications of Soy Protein
1.5 Electrospinning of Soy Protein Nanofibers: Synthesis and Applications
1.6 Soy Proteins as Potential Source of Active Peptides of Nutraceutical Significance
1.7 Soy Protein Isolate-Based Films
1.8 Use of Soy Protein-Based Carriers for Encapsulating Bioactive Ingredients
References

Chapter 2: Soy Protein: Introduction, Structure and Properties Relationship

2.1 Introduction
2.2 Structure of Soy Proteins
2.3 Source of Soy Proteins
2.4 Properties of Soy Proteins
2.5 Chemical Modification of Soy Proteins
2.6 Characterization of Soy Proteins
2.7 Conclusion
References

Chapter 3: Advances in Soy Protein-Based Nanocomposites

3.1 Introduction
3.2 Preparation Methods of Soy Protein Nanocomposites
3.3 Properties of Thermoplastic Soy Protein Nanocomposites
3.4 Protein-Based Nanocomposites
3.5 Conclusion
Acknowledgements
References

Chapter 4: Applications of Soy Protein-Based Blends, Composites, and Nanocomposites

4.1 Introduction
4.2 Applications of Soy Protein Particulars
4.3 Applications of Soy Protein-Based Blends
4.4 Applications of Soy Protein-Based Composites
4.5 Applications of Soy Protein-Based Nanocomposites
4.6 Conclusion
References

Chapter 5: Biomedical Applications of Soy Protein

5.1 Introduction
5.2 The Forms of SP
5.3 Wound-Dressing Materials
5.4 Potential Applications of SP in Regenerative Medicine and Tissue Engineering
5.5 Application of SP Product for Regeneration of Bone
5.6 Application of SP in Drug Delivery Systems
5.7 Conclusion
Acknowledgement
References

Chapter 6: Electrospinning of Soy Protein Nanofibers: Synthesis and Applications

6.1 Introduction
6.2 Properties of Soybean Proteins That Affect Electrospinning
6.3 Applications
6.4 Conclusion and Outlook
References

Chapter 7: Soy Proteins as Potential Source of Active Peptides of Nutraceutical Significance

7.1 Introduction
7.2 Soy Proteins as Source of Bioactive Peptides
7.3 Identification of Potential Bioactive Peptides from Soy Proteins
7.4 Production of Bioactive Peptides from Soy Proteins
7.5 Potential Applications of Bioactive Peptides from Soy Proteins
7.6 Conclusion
References

Chapter 8: Soy Protein Isolate-Based Films

8.1 Introduction
8.2 Soy Protein Film Preparation
8.3 Characterization of Soy Protein Films
8.4 Modifications
8.5 Applications
References

Chapter 9: Use of Soy Protein-Based Carriers for Encapsulating Bioactive Ingredients

9.1 Introduction
9.2 Encapsulation Methods
9.3 Soy Protein-Based Encapsulation Carriers
9.4 Conclusion
References

Index

End User License Agreement

List of Tables

Chapter 4

Table 4.1.: Applications of soy protein-based blends and composites in the biomedical field.
Table 4.2.: Production of packaging based on soy protein raw material.

Chapter 6

Table 6.1.: Summary of solvents and main conditions used in different soy protein electrospinning studies.

Chapter 7

Table 7.1.: Amino acid composition of soybean proteins*.
Table 7.2.: Identified bioactive peptides derived from soybean storage proteins through in silico hydrolysis with gastrointestinal enzymes and some commercial enzymes*,a,b.
Table 7.3.: Predicted bioactive peptides derived from soybean storage proteins through in silico hydrolysis with gastrointestinal enzymes and some commercial enzymes*,a,b.
Table 7.4.: Bioactive peptides derived from soybean proteins by different digestion procedures.

Chapter 8

Table 8.1.: Optimum extrusion conditions for protein/glycerol mixtures.
Table 8.2.: TS, strain at break (ε), E, and puncture tests of films at pH 2, 8, and 11 [78].
Table 8.3.: Structural parameters of native and heat-treated SPI derived from SAXS and DLS data.
Table 8.4.: Spacing values of zein-based materials tested by WAXS and SAXS [97].

Chapter 9

Table 9.1.: Encapsulation with SPI-based wall material.

List of Illustrations

Chapter 3

Figure 3.1: Synthetic route for N-phthaloyl soy protein.
Figure 3.2: SEM images of the surfaces of SA-0 (a1, b1, and c1), SA-4 (a2, b2, and c2), SA-8 (a3, b3, and c3) and SA-20 (a4, b4, and c4) after seven-day exposure to three funguses at 37 °C. The number after SA means the content of AlCl₃. The character “a” in the labels means the plastic sheets were degraded by Chaetomium olivaceum, “b” means Trichoderma viride, and “c” means Aspergillus oryzae. The scale bar inside represents 30 μm.
Figure 3.3: Illustration of the cross-linking reactions for SPI/GPTMS/POSS (d) from SPI (c), GPTMS (b) and POSS (a).
Figure 3.4: Citric acid-modified starch nanoparticles (left) and unmodifiedstarch (right) (5%, w/v in water) after heating a 100 °C.
Figure 3.5: Reaction among SPI, MCNC, and EGDE (a) SPI, (b) EGDE, (c) MCNC, and (d) SPI-based films cross-linking networks.
Figure 3.6: Upper section SP-NFC composite aerogels of a few selected compositions: 100% NFC, 50:50 SP-NFC and 100% SP. Lower section tomography images of cubic sections of the respective aerogel.
Figure 3.7: TEM micrographs of soy protein/polystyrene nanoblends with (a) 5%, (b) 10%, (c) 20%, and (d) 50% styrene contents.
Figure 3.8: Reaction of arylated soy protein in water.
Figure 3.9: Photographs of the arylated soy protein films (a): left, middle, and right show SB, SB in water for 26 h, and SBWM just removed from water, respectively. SEM images of SB (b,c) and SBWM (d,e) films. Surface morphology (left) and cross-section (right).

Chapter 5

Figure 5.1: Structures of phytosterols found in SP.
Figure 5.2: Structures of selected carbohydrates found in SP.
Figure 5.3: Structures of main compounds in SP responsible for enhanced wound healing.
Figure 5.4: Different forms of wound dressings prepared from SP.
Figure 5.5: Different forms of SP-based drug delivery formulations.

Chapter 6

Figure 6.1: Electrospun soy protein/poly(ethylene oxide) from solutions with total polymer concentration of (a) 9 wt%, (b) 11 wt%, and (c) 13 wt%. The scale bar represents 10 μm. Figure reproduced from Cho et al. [18] with permission. Copyright © 2010 John Wiley & Sons, Inc.
Figure 6.2: FE-SEM images of soy protein/lignin with 10 wt% (based on dry fibers) of poly(ethylene oxide) as coadjutant polymer. Top row: glycinin (G)-lignin (L) fibers with different protein/lignin content (G1, G2, G3, G4). Bottom row: soy isolate (I)-lignin (L) fibers I2, I3, I4). Fiber diameter increase with lignin content (from left to right).The scale bar shown is 5 μm [21].Reprinted from Reactive and Functional Polymers, Vol. 85, Carlos Salas, Mariko Ago, Lucian A. Lucia, Orlando J. Rojas, Synthesis of soy protein-lignin nanofibers by solution electrospinning, Pages 221–227., Copyright © 2014 with permission from Elsevier.
Figure 6.3: Growing of human dermal fibroblasts after eight days of culture on electrospunscaffolds prepared form (a) 5% SPI, 0.05% PEO, (b) 8% SPI, 0.05% PEO (c) 40% zein, (d) gelatin, (e) poly(lactic-co-glycolic acid), PLGA, and (f) glass. (Nuclei, blue; F-actin cytoskeleton, red. Magnification: 200x). Figure reproduced from Lin et al. [10] with permission. Copyright © 2013 John Wiley & Sons, Inc. [10].
Figure 6.4: Micrograph of tissue from porcine model after 4 weeks injury, stained with Masson’s trichrome (MTS). (a) Healthy skin taken close to the untreated control. (b) Wound area of an untreated control. (c) Wound area of soy protein scaffold treated wound. Purple stained areas correspond to collagen [11]. Reprinted from Wound Medicine, Vol. 5, Yah-el Har-el, Jonathan A. Gerstenhaber, Ross Brodsky, Richard B. Huneke, Peter I. Lelkes. Electrospun soy protein scaffolds as wound dressings: Enhanced re-epithelialization in a porcine model of wound healing. Pages 9–15., Copyright © 2014 with permission from Elsevier.

Chapter 7

Figure 7.1: Example of identification of bioactive peptides from glycinin G1 protein. Angiotensin I converting enzyme (ACE)-inhibitory peptides (ACEIPs; green), antioxidative peptides (AOPs; red), DPP-IV inhibitors (DPP-IVPs; blue), peptides that function as both ACEIP and AOP (pink), peptides that function as both ACEIPs and DPP-IVPs (purple) and peptides that function as both AOPs and DPP-IVPs (yellow). Different peptides having the same functionality in the adjacent rows are underlined.
Figure 7.2: Example of in silico hydrolysis with Asp-N in combination with GI enzymes (pepsin, trypsin, and chymotrypsin) and identification of bioactive peptides from glycinin G1 protein. Angiotensin I converting enzyme (ACE)-inhibitory peptides (ACEIPs; green), antioxidative peptides (AOPs; red), DPP-IV inhibitors (DPP-IVPs; blue), peptides that function as both ACEIPs and AOPs (pink), peptides that function as both ACEIPs and DPP-IVPs (purple) and peptides that function as both AOPs and DPP-IVPs (yellow). Predicted ACEIPs are in bold, predicted AOPs are italic and predicted DPP-IVPs are underlined. Peptide sequences in yellow are not assigned; separation from other adjacent peptide is by means of underlining.

Chapter 8

Scheme 8.1: Reaction of acetic and succinic anhydride with soy protein [32].
Figure 8.1: Structure of rutin and epicatechin (a) and TS and tensile elongation of SPI films with or without rutin and epicatechin (b) [8].
Figure 8.2: DMA of E’ (a) and loss modulus (b) on temperatures for SPI plastics. Note: BUT12, BUT13, GLY, PRO, and CON represent SPI plastics with 1,2-butanediol, 1,3-butanediol, glycerol, propylene glycol, and unplasticized SPI plastics, respectively [84].
Figure 8.3: TGA (a) and DTG (b) curves of SPI/PBAT blends in N₂ atmosphere [85].
Figure 8.4: DSC of SPI solutions (a) SPI films (b) at pH 2, 8, and 11 [31].
Figure 8.5: SEM images of cross-sections of the SPI-based films [10].
Figure 8.6: TEM images of SPI and modified SPI samples [41].
Figure 8.7: Surface morphology of SPI materials (a) unmodified (b) modified SPI films [89].
Figure 8.8: Surface dilatational modulus (E) as a function of surface pressure (π) for native and heat-treated SPI (SPI-90 and SPI-120) at the oil-water interface [91].
Figure 8.9: G′(a) and G″(b) curves of SPI and SPI-CNF to oscillatory shear frequency [92].
Figure 8.10: SAXS of SPI-based samples [91].
Figure 8.11: Proposed structure models of zein-oleic acid resin films, side view (a) and top view (b), aggregated longitudinally to form platelets [97].
Figure 8.12: Schematic diagram of possible interactions in cross-linked protein films (a) [119,120]; cross-linking reaction mechanisms of SPI and ESO (b) [10]; oxidized sucrose and soy protein (c) [121]; and Maillard reaction between amino acids and CMC (d) [122].
Figure 8.13: Scheme of LBL modification on mats [139].

Chapter 9

Figure 9.1: pH stability of free and encapsulated E. faecalis HZNU P2 in simulated gastric fluid (SGF) pH 2.5 and 2.0. (a) The stability of free and encapsulated E. faecalis HZNU P2 (SPI-alginate) in SGF pH 2.5. (b) The stability of free and encapsulated E. faecalis HZNU P2 (SPI-alginate) in SGF pH 2.0. (c) The stability of free and encapsulated E. faecalis HZNU P2 (soy milk-alginate) in SGF pH 2.5. (d) The stability of free and encapsulated E. faecalis HZNU P2 (soy milk-alginate) in SGF pH 2.0.
Figure 9.2: Release of encapsulated E. faecalis HZNU P2 in simulated intestine fluid (SIF). (a) SPI-Alginate microspheres. (b) Soy milk-Alginate microspheres.
Figure 9.3: Storage stability of free and encapsulated E. faecalis HZNU P2 at 4, 25 °C and 37 °C. (a) Storage stability of free and encapsulated E. faecalis HZNU P2 at 4 °C (SPI-alginate). (b) Storage stability of encapsulated E. faecalis HZNU P2 at 25 and 37 °C (SPI-alginate). (c) Storage stability of free and encapsulated E. faecalis HZNU P2 at 4 °C (soy milk-alginate). (d) Storage stability of free and encapsulated E. faecalis HZNU P2 at 4 °C (soy milk-alginate).

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Library of Congress Cataloging-in-Publication Data
ISBN 978-1-119-41830-6

Preface

Many of the recent research accomplishments in the area of soy-based blends, composites and bionanocomposites are presented in this book. In addition to introducing soy protein and its structure and relationship properties, an attempt has been made to cover many other relevant topics such as the state-of-the-art, new challenges, advances and opportunities in the field; biomedical applications of soy protein; electrospinning of soy protein nanofibers, their synthesis and applications; soy proteins as a potential source of active peptides of nutraceutical significance; soy protein isolate-based films; and use of soy protein-based carriers for encapsulating bioactive ingredients.

This book is intended to serve as a one-stop reference resource for important research accomplishments in the area of soy protein-based biocomposites and bionanocomposites. It will be a very valuable reference source for university and college faculties, professionals, post-doctoral research fellows, senior graduate students, and researchers from R&D laboratories working in the area of soy protein and its biocomposites and bionanocomposites. Since the various chapters in this book have been contributed by prominent researchers from industry, academia and government/private research laboratories across the globe, it is an up-to-date record of the major findings and observations in the field. The first chapter acts as an introduction to soy protein-based blends, composites and nanocomposites, including their scope, state of the art, preparation methods, environmental concerns regarding nanoparticles and related challenges and opportunities.

Included in the second chapter introducing general aspects of soy proteins, is a discussion of their source, structure and relationship properties. Chemical modification and characterization of soy proteins are also included in this chapter along with a description of the applications of soy protein-based nanocomposites and blends. Advances in soy protein-based nanocomposites are addressed in the third chapter, in which the authors discuss how the incorporation of nanoparticles proves to be an effective way to improve physical properties, especially the mechanical properties and water resistance which limit their extensive use. The properties of the resulting nanocomposites are highly dependent on the processing methods, nature of nanofillers, as well as the dispersion effect of the filler in the matrix. Therefore, the fabrication methods, property-structure relationship, and application of soy protein nanocomposites are also reviewed in this chapter.

The following chapter on applications of soy protein-based blends, composites and nanocomposites discusses many topics, including the particulars of soy protein applications, soy protein-based blends, and those of soy protein-based nanocomposites. The fifth chapter based on biomedical applications of soy protein summarizes many of the recent accomplishments in the area of biomedical research. In this chapter, the authors discuss various topics such as forms and properties of soy proteins, application of plant protein in biomedical applications, application of soy proteins in wound dressings, and the potential use of soy proteins in products and applications in regenerative medicine, tissue engineering, and drug delivery systems.

The following chapter is a good structural basis for the understanding of electrospinning of soy protein nanofibers. Discussed in the chapter are the production of nanofibers from different synthetic and natural polymers, the physical properties of soy proteins that affect their electrospinning, followed by a summary of relevant work that has been done in the area. The chapter closes with a discussion on possible applications of electrospun nanofibers from soy proteins. The use of soy proteins as a potential source of active peptides of nutraceutical significance is the subject of the seventh chapter, which introduces the main concepts along with examples to help readers understand them. This chapter is devoted to reviewing the literature to identify and describe the available methodologies for the identification and production of bioactive peptides from soybean proteins. In addition, potential applications of these peptides as functional foods and therapeutic agents are also highlighted.

The authors of the eighth chapter present a brief account of the topic of soy protein isolate-based films, including soy protein film preparation, characterization of soy protein films, modifications and applications. The last chapter of the book reviews recent progress in the preparation of soy protein-based carriers for bioactive ingredients encapsulation.

In conclusion, the editors would like to express their sincere gratitude to all of the contributors to this book for their excellent support in the successful completion of this venture. We are grateful to them for the commitment and sincerity they have shown towards their contributions. Without their enthusiasm and support, this book would not have been possible. We would also like to thank all the reviewers who have taken their valuable time to make critical comments on each chapter. We also thank the publisher John Wiley and Sons Ltd. and Scrivener Publishing for recognizing the demand for such a book, realizing the increasing importance of the area of soy protein-based blends, composites and nanocomposites, and for starting such a new project, which not many other publishers have handled.

Visakh. P. M
Olga Nazarenko
Tomsk, Russia
June 2017