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Nutraceuticals Derived from Seed Storage Proteins Implications For Biocatalysis and Agricultural Biotechnology 17 (2019) 710–719 Contents lists available at ScienceDirect Biocatalysis and Agricultural Biotechnology journal homepage: www.elsevier.com/locate/bab Nutraceuticals derived from seed storage proteins: Implications for health wellness T Ashutosh Kumara, Dinesh K. Agarwala, Sunil Kumarb, Y. Mohan Reddyc, ∗ Anjani Devi Chintaguntad, K.V. Sarithac, Govind Pala, S.P. Jeevan Kumara, a ICAR- Indian Institute of Seed Science, Mau, U.P., 275103, India b ICAR- National Bureau of Agriculturally Important Microorganism, Mau, U.P., 275103, India c Department of Biotechnology, Sri Venkateswara University, Tirupati, A.P., 517502, India d Department of Biotechnology, Vignan`s Foundation for Science, Technology and Research, Vadlamudi, Guntur, A.P., 522213, India ARTICLE INFO ABSTRACT Keywords: Seed storage proteins are major source of proteins because of readily available bioactive peptides. These peptides Bioactive peptides are fragments of a protein, which showed positive implications on human wellness and gained wide importance Antimicrobial peptides owing to their health benefits such as antimicrobial, antiviral, antifungal, anti-tumor activities. In plants, the Angiotensin converting enzyme-II bioactive peptides are ubiquitous in distribution that act as a part of innate response upon elicitation. In ad- Anti-viral dition, these plant based bioactive peptides have structural similarity with the insect and animal sources. In most Anti-fungal of the cases, the bioactive peptides triggers their response by binding the target membrane that results into Anti-tumor activity permeabilization and rupture of the membrane. Delineating the potential of peptides having antiviral, anti- microbial and antiviral properties these can be used in the food and pharmaceutical industries. Further, these peptides can be used into the packaging material called active packaging that enhances the shelf life and quality of the food. In this review, seed storage proteins based bioactive peptides and their potent applications for health as well as food industry have been elucidated. 1. Introduction novel and cost effective drugs that alleviate the resistance tendency of micro-organisms. (Kumar et al., 2016). Moreover, these health benefits Seed, in the course of plant evolution, is a unique attribute in of seed storage proteins (SSP) can be explored in active packaging, gymnosperms and angiosperms responsible to endure during unfavor- where the peptides are incorporated into the polymer to increase the able conditions. Seed is a repository, which accumulates proteins, car- quality and shelf-life of a product (Chandusingh et al., 2017b). Hence, bohydrates and lipids to facilitate nutrition and protection to the de- in the paper, potential of bioactive peptides and their health benefits veloping embryo and other tissues. Among these primary metabolites, have been discussed with a focus on industrial applications that ulti- proteins are playing a vital role in maintaining the normal plant cell mately benefit the human wellness. metabolism. The proteins are classified mainly into two groups such as structural and biologically active proteins, whose functions are indis- 2. Seed storage proteins pensable in structural architecture of cell (cell wall) and protection of cellular machinery like enzyme inhibitors, enzymes, lectins etc Seed storage proteins (SSP) play a pivotal role in the human diet. It (Agarwal and Kumar et al., 2016). Recent studies emphatically ad- supplies the protein requirement to more than half of the global po- vocating the great advantages of bioactive peptides, whose physiolo- pulation, particularly for human and livestock (Chandusingh et al., gical functions have been manifested in the form of anti-viral and anti- 2017a). These proteins are abundant in nature and determines the tumor activities, immune-modulatory and reduces the cholesterol and quality of protein, as a result, these SSP's are widely preferred than the blood pressure (Kumar et al., 2017). Considering the physiological ac- animal based proteins (Kumar et al., 2016). For instance, essential tions of bioactive peptides and their potential for commercial viability, amino acids such as methionine and cysteine (sulphur containing amino particularly anti-microbial and anti-viral activities helps to develop a acids) are inadequately available in legumes; in contrary, cereals Abbreviations: Glucosaminoglycans, (GAG); Ribosome-inactivating proteins, (RIPs); Seed storage proteins, (SSP) ∗ Corresponding author. E-mail address: [email protected] (S.P.J. Kumar). https://doi.org/10.1016/j.bcab.2019.01.044 Received 11 October 2018; Received in revised form 16 January 2019; Accepted 17 January 2019 Available online 28 January 2019 1878-8181/ © 2019 Published by Elsevier Ltd. A. Kumar et al. Biocatalysis and Agricultural Biotechnology 17 (2019) 710–719 contain tryptophan, lysine and threonine that are significantly low. 3. Albumin (1.6-2S) Hence, to supplement the adequate nutritious food, SSP having en- riched essential amino acids can be nourished (Vinutha et al., 2014a). Albumins derived from plant proteins have similar characteristics as Seed storage proteins are synthesized either in endosperm or cotyledon an egg albumin, which is able to coagulate. Later, these proteins were and stores the protein moiety in the form of protein storage vacuoles classified based on solubility in water and coagulable with heat. (PSV) also known as protein bodies. At physiological conditions, these However, during extraction from tissues, salt availability at low con- protein bodies are densely available in mature seeds, where the psv is centrations in the tissues should be removed using dialysis techniques, embedded with the protein deposits (Singh et al., 2015). otherwise obtaining true fraction of albumin is difficult. Albumins are Bioactive peptides are specific moieties of protein that influence the generally found at lower concentration in seeds and the best char- physiological functions and ultimately lead to health wellness acterized types are leucosin (wheat, barley), phaselin, legumelin and (Chandusingh et al., 2017b). Bioactive peptides when released in the ricin from kidney bean, legumes and castor bean, respectively. Youle gastrointestinal (GI) region, play different functions such as anti-viral, and Huang (1981) have extracted the seed storage proteins using su- anti-microbial, anti-tumor, anti-thrombic, anti-hypertensive, anti-oxi- crose gradient ultracentrifugation to compare salt soluble protein dant and immunomodulatory that ultimately improves the health fraction from 12 different species covering legumes and grass (Cizeau et al., 2000; Kumar et al., 2017). Assimilation of bioactive (monocot). Ultracentrifugation separation showed three peaks such as peptides in the GI region depends on the size, length and hydro- 2S, II S and 7S, among which the 2S (cysteine) fraction is comparatively phobicity of the peptide. For instance, mono and di peptides are ac- higher than the other fractions. tively transported via intestinal epithelium with the help of H+ gra- dient, whereas, oligopeptides would transport through intestinal 3.1. Structure of albumin epithelium either by para cellular channels or pinocytosis based on hydrophobicity and size of the peptide (Sinha et al., 2016). However, Seed storage albumins are abundantly available proteins that are after absorption, the peptides might be degraded by the action of serum soluble in water and are easily broken-down during seed germination to protease released from the intestine. Hence, peptidase degradation re- supplement nutrients such as sulphur and nitrogen for the seedling sistant mechanism would be inevitable to exert the physiological role of development. However, in seed maturation phase these proteins un- SSP on the body, when administered through intra-venous or oral dergo post-translational modifications and trafficking before deposition mode. with great stability and quantity in protein storage vacuoles. Ericson fi Seed storage proteins are classi ed into four types by Osborne and et al. (1986) has deciphered the primary structure of a processed and Campbell (1898), considering the criteria of solubility and ex- mature napin (an albumin). In this study, napin-type albumin precursor tractability (Fig. 1). They are: from rapeseed has been cloned, isolated and purified the matured napin. Structural studies on napin revealed that it is a heterodimeric 2S – • Albumins [(1.6S 2S) (water soluble)] albumin protein, comprised of two subunits of 30–40 and 60–90 amino – • Globulins [(7S 13S) (soluble in dilute salt solutions)] acid residues, respectively. 2S albumin synthesized as a precursor • Glutelins (soluble in dilute acid or alkali) protein has been transported co-translationally into the endoplasmic • Prolamins (soluble in water/alcohol mixtures) reticulum lumen. In the post translational modifications, the protein undergoes conformational changes into a folded form by introduction Globulins and prolamins remain as oligomers and small aggregates, of four intra-chain disulphide bonds with eight conserved cysteine re- whereas, the glutelins form large disulphide bonded aggregates, whose sidues, which further transported into the cell vacuole (O'Kane at al., solubility is poor in water (Singh et al., 2017). In dicots (eg. legumes), 2004a). Moreover, in the vacuole, partial folded protein undergoes albumins and globulins occupies a major proportion; but in monocots proteolytic processing that result into two subunits,
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