Novel Proteins for Food, Pharmaceuticals, and Agriculture

Sources, Applications, and Advances

Maria Hayes

• Publisher: Wiley-Blackwell
• Year: 2018
• Print ISBN:
  9781119385301
• Edition: 1
• eBook ISBN:
  9781119385325
• Topic: Biological Sciences
• Subtopic: Molecular Biology
• Index: Biological Sciences

A groundbreaking text that highlights the various sources, applications and advancements concerning proteins from novel and traditional sources

Novel Proteins for Food, Pharmaceuticals and Agriculture offers a guide to the various sources, applications, and advancements that exist and are currently being researched concerning proteins from novel and traditional sources. The contributors—noted experts in the field—discuss sustainable protein resources and include illustrative examples of bioactive compounds isolated from several resources that have or could obtain high market value in specific markets.

The text also explores a wide range of topics such as functional food formulations and pharmaceutical applications, and how they alter biological activity to provide therapeutic benefits, nutritional values and health protection. The authors also examine the techno-functional applications of proteins and looks at the screening process for identification of bioactive molecules derived from protein sources. In addition, the text provides insight into the market opportunities that exist for novel proteins such as insect, by-product derived, macroalgal and others. The authors also discuss the identification and commercialization of new proteins for various markets. This vital text:

• Puts the focus on the various sources, applications and advancements concerning proteins from novel and traditional sources
• Contains a discussion on how processing technologies currently applied to dairy could be applied to novel protein sources such as insect and macroalgal
• Reviews the sustainability of protein sources and restrictions that exist concerning development
• Offers ideas for creating an innovative and enterprising economy that is built on recent developments
• Details the potential to exploit key market opportunities in sports, infant and elderly nutrition and techno-functional protein applications

Written for industrial researchers as well as PhD and Post-doctoral researchers, and undergraduate students studying biochemistry, food engineering and biological sciences and those interested in market developments, Novel Proteins for Food, Pharmaceuticals and Agriculture offers an essential guide to the sources, applications and most recent developments of the proteins from both innovative and traditional sources.

1
Biological Roles and Production Technologies Associated with Bovine Glycomacropeptide

Shane Feeney^1,2 Lokesh Joshi² and Rita M. Hickey¹

¹Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland

²Advanced Glycoscience Research Cluster, National Centre for Biomedical Engineering Science, National University of Ireland Galway, Galway, Ireland

1.1 Introduction

Glycomacropeptide(GMP) is a casein‐derived whey peptide found in ‘sweet’ whey. The addition of chymosin to milk during cheese making enzymatically hydrolyses or cleaves the milk protein (kappa‐casein) into two peptides, an insoluble peptide (para‐kappa‐casein) and a soluble hydrophilic glycopeptide (GMP), as shown in Figure 1.1. The larger peptide, para‐kappa‐casein, contains the amino acid residues 1–105 and becomes coagulated and incorporated into the cheese curd. The smaller peptide, which contains the amino acid residues 106–169 (GMP), becomes soluble and is incorporated into the whey (Walstra et al. 2006). GMP is the third most abundant whey protein, after beta‐lactoglobulin and alpha‐lactalbumin, accounting for approximately 15–25% (1.2–1.5 g L⁻¹) of the total whey protein (Thomä‐Worringer et al. 2006). GMP is highly polar and has unique characteristics due to the absence of phenylalanine, tryptophan, tyrosine, histidine, arginine or cysteine residues (Neelima et al. 2013). The peptide is rich, however, in branched chain amino acids, such as isoleucine and valine (Marshall 2004; Krissansen 2007).

Figure 1.1 Bovine kappa‐casein structure which varies depending on its post‐translational modifications (phosphorylation and glycosylation). During cheese making, hydrolysis by chymosin releases the water‐soluble fragment para‐kappa‐casein and the hydrophilic glycomacropeptide.

At least 13 genetic variants of bovine kappa‐casein have been identified which have different post‐translational modifications (PTMs) and vary in their level of phosphorylation and glycosylation (Thomä‐Worringer et al. 2006). The average molecular weight for GMP is 7500 Da, whereas the highest recorded molecular weight is 9631 Da (Mollé and Léonil 2005). It has been suggested that the peptide has the ability to associate and dissociate under certain pH conditions, possibly explaining why molecular weights of between 14 and 30 kDa are observed via SDS‐PAGE (Galindo‐Amaya 2006; Farías et al. 2010).

Given the heterogeneity of GMP, there is no single isoelectric point (pI) assigned to GMP but the pI of the peptide portion is approximately 4, varying with PTM. Approximately 60% of GMP consists of O‐linked carbohydrate chains which are composed of mainly galactose (gal), N‐acetyl galactosamine (GalNAc) and N‐neuraminic acid (Neu5Ac) attached at threonine residues. Saito et al. (1991) determined via high‐performance liquid chromatography(HPLC) the distribution of monosaccharide, disaccharide, trisaccharide (straight and branched) and tetrasaccharide chains as 0.8%, 6.3%, 18.4%, 18.5% and 56.0%, respectively, while Mollé and Léonil (1995) identified five potential glycosylation sites using electrospray‐ionisation mass spectrometry(ESI–MS) (Saito et al. 1991; Molle and Leonil 1995). Glycosylation influences the physical properties of GMP such as solubility (Taylor and Woonton 2009) and its emulsifying and foaming properties (Kreuß and Kulozik 2009). Moreover, variations in glycosylation can occur over the course of lactation (Recio et al. 2009; Neelima et al. 2013). For instance, colostrum GMP has an elevated glycan content (Guerin et al. 1974). Only GalNAc, Gal and Neu5Ac have been identified in GMP glycans from mature milk, but glycans from colostrum samples in addition contain N‐acetylglucosamine (GlcNAc) and fucose (Fuc). Furthermore, a greater number of glycans and more complex structures have been identified in colostrum GMP (Fiat et al. 1988). A disialylated tetrasaccharide is the most abundant glycan present in mature GMP (Saito and Itoh 1992), and this high level of sialylation is vital for some of GMP’s biological activities, as will be discussed later. Commercially available forms of GMP contain approximately 8% sialic acid (Arla Food Ingredients and Agropur Ingredients).

The aim of this chapter is to provide an overview of the state of the art in research regarding the functional role of GMP in maintaining and improving human health which is summarised in Table 1.1and providing better knowledge on the isolation and detection of GMP as an ingredient in functional or medical foods.

Table 1.1 Biofunctional roles of GMP in improving human health.

Bioactivity	Reference
Management of PKU	Etzel (2004); Ney et al. (2008); Ney et al. ()2016
Ability to bind cholera toxin and E. colienterotoxins	Kawasaki et al. (1992) – cholera toxin Isoda et al. (1999) – E. coliheat labile enterotoxins
Inhibition of bacterial and viral adhesion	Neeser et al. (1988) – cariogenic bacteria Neeser et al. (1994) – cariogenic bacteria Neeser et al. (1995) – cariogenic bacteria Schüpbach et al. (1996) – cariogenic bacteria Bruck et al. (2006a) – E. coli, Salmonella typhimurium, Shigella flexneri Nakajima et al. (2005) – E. coli Rhoades et al. (2005) – E. coli Feeney et al. (2017) – E. coli Kawasaki et al. (1993a) – human influenza virus Dosako et al. (1992) – Epstein–Barr virus
Suppression of gastric secretions	Beucher et al. (1994) – gastric secretions Yvon et al. (1994) – gastric secretions Stan EYa et al. (1983) – gastric secretions
Promotion of bifidobacterial growth	Brody (2000) – review has several examples Thomä‐Worringer et al. (2006) – review has several examples Recio et al. (2009) – review has several examples O’Riordan et al. (2014) – review has several examples
Reduction in intestinal epithelial cell barrier dysfunction	Rong et al. (2015) – barrier function Feeney et al. (2017) – barrier function
Modulation of immune system responses	Brody (2000) – review has several examples Daddaoua et al. (2005) – anti‐inflammatory activity Requena et al. (2008) – anti‐inflammatory activity Requena et al. (2010) – anti‐inflammatory activity Lopez‐Posadas et al. (2010) – anti‐inflammatory activity Cui et al. (2017) – ulcerative colitis Jimenez et al. (2012) – control of allergic diseases

1.2 Biological Properties Associated with Glycomacropeptide

1.2.1 Management of Phenylketonuria

Phenylketonuria (PKU) (OMIM 261600) is an autosomal recessive disorder caused by mutations in the phenylalanine hydroxylase(PAH) gene that encodes the enzyme which catalyses the conversion of phenylalanine (Phe) to tyrosine (Tyr) in a reaction dependent on the essential PAH co‐factor tetrahydrobiopterin (Blau et al. 2010). Tyr is an essential amino acid in PKU. Normal intake of dietary protein in untreated PKU causes Phe to accumulate in blood, leading to toxic concentrations of Phe in the brain and intellectual disability (Vockley et al. 2014). The main therapy for PKU is long‐term adherence to a low‐Phe diet that limits Phe intake from natural foods that contain protein, and supplements with special medical formulas t...

Table of contents

• Cover
• Table of Contents
• List of Contributors
• About the Editor
• Preface
• Chapter 1: Biological Roles and Production Technologies Associated with Bovine Glycomacropeptide
• Chapter 2: Meat Proteins as a Potential Source of Bioactive Ingredients for Food and Pharmaceutical Use
• Chapter 3: Human Gastrointestinal Endogenous Proteins: A Recently Discovered Source of Gut Modulatory Peptides
• Chapter 4: Cereal Proteins: Potential Health Applications and Allergenicities
• Chapter 5: Meat By‐Products: New Insights into Potential Technical and Health Applications
• Chapter 6: Potential Applications of Plant‐Derived Proteins in the Food Industry
• Chapter 7: Seaweed Proteins and Applications in Animal Feed
• Chapter 8: Marine By‐Products as a Source of Proteins for Potential Food, Pharma, and Agricultural Feed Use
• Chapter 9: Bioavailability, Bioaccessibility, and Nutritional Measurement of Proteins
• Chapter 10: Protein from Vegetable Sources: A Focus on Pea Protein
• Chapter 11: Seaweeds as a Source of Proteins for Use in Pharmaceuticals and High‐Value Applications
• Chapter 12: Microalgal Bioactive Compounds Including Protein, Peptides, and Pigments: Applications, Opportunities, and Challenges During Biorefinery Processes
• Chapter 13: Current and Future Trends in Protein Use and Consumption
• Chapter 14: Allergenicity of Food Proteins
• Chapter 15: Industrial Processing of Proteins
• Chapter 16: The Role of Immunoglobulins from Bovine Colostrum and Milk in Human Health Promotion
• Index
• End User License Agreement