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Echave Álvarez, J. Seaweed Proteins and Derived Peptides. Encyclopedia. Available online: https://encyclopedia.pub/entry/20098 (accessed on 06 December 2025).
Echave Álvarez J. Seaweed Proteins and Derived Peptides. Encyclopedia. Available at: https://encyclopedia.pub/entry/20098. Accessed December 06, 2025.
Echave Álvarez, Javier. "Seaweed Proteins and Derived Peptides" Encyclopedia, https://encyclopedia.pub/entry/20098 (accessed December 06, 2025).
Echave Álvarez, J. (2022, March 02). Seaweed Proteins and Derived Peptides. In Encyclopedia. https://encyclopedia.pub/entry/20098
Echave Álvarez, Javier. "Seaweed Proteins and Derived Peptides." Encyclopedia. Web. 02 March, 2022.
Seaweed Proteins and Derived Peptides
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This entry is adapted from the peer-reviewed paper 10.3390/antiox11010176

Seaweeds are a typical food of East-Asian cuisine, to which are alleged several beneficial health effects have been attributed. Their availability and their nutritional and chemical composition have favored the increase in its consumption worldwide, as well as a focus of research due to their bioactive properties. In this regard, seaweed proteins are nutritionally valuable and comprise several specific enzymes, glycoproteins, cell wall-attached proteins, red algae phycobiliproteins, lectins, peptides, or mycosporine-like amino acids. 

seaweed protein peptides

1. Glycoproteins

These compounds are proteins covalently linked to various oligosaccharide chains (glycans). Two major types of sugar chains are found in GPs, those bounded by N-glycosyl linkages or by O-glycosyl linkages [1]. GPs are located on the cell wall, on the surface of the cell, or free after secretion, and their roles include intercellular interactions and recognition [2]. Proportions of proteins and sugars of GPs differ from different algae species. For example, Ulva sp. GPs-rich fractions showed a protein proportion up to 33.4% [3], while in Codium decorticatum, which has GPs of molecular weight (MW) around 48 kDa, the protein proportion reached 60% [4]. Regarding the composition of the prosthetic fraction, seaweed GPs seem to mainly contain mannose [2].

2. Lectins

Lectins are GPs that bind with high specificity to certain mono- or oligosaccharides. Seaweeds are good sources of novel lectins of low MW, especially red seaweeds [5]. The functions of lectins include gamete recognition and reproductive cell fusion, as well as defense against pathogens [5][6]. Lectins can be classified into four main groups: chitin-binding lectins, legume lectins, type-2 ribosome-inactivating proteins, and mannose-binding lectins [7]. In the case of seaweeds, the great majority of these proteins are mannose-binding, which are the major type of glycans found in them [2]. Likewise, relevant seaweed lectins are mannose-specific lectins, which show high binding affinity with these residues [8]. This property allows them to “agglutinate” particles containing these residues, as is the case of bacterial, viral, or eukaryote cell surface GPs [9]. One example is griffithsin, obtained from red Griffithsia sp. seaweeds, which has been described with diverse biological properties [10]. Due to these pharmacological properties, their characterization and isolation are a focus of research in medicine, molecular biology, or biochemistry. However, despite advances in the chemical characterization of seaweed lectins, additional information is still needed for a deeper understanding of their molecular structures, binding affinities, and possible biological functions for further applications [11].

3. Phycobiliproteins

PBPs are hydrosoluble chromophore proteins mainly present in cyanobacteria but also in red seaweeds. Their primary metabolic role is to act as light absorbents during photosynthesis [12]. PBPs include four classes of pigments: blue colored phycocyanin with absorption maxima (λmax) in the range between 610 and 620 nm, magenta-colored phycoerythrocyanin (λmax: 575 nm), bluish-green-colored allophycocyanin (λmax: 652 nm), and deep red- or pink-colored phycoerythrin (PE) with λmax between 540 and 570 nm [12]. The major PBP in red seaweeds is PE, of which phycoerythrobilin is its main prosthetic group (Figure 1) [13].
Antioxidants 11 00176 g001 550
Figure 1. Chemical structure of the chromophore group of R-phycoerythrin, some relevant mycosporine-like amino acids, and bioactive peptides isolated from seaweed protein hydrolysates. Peptide sequences and source are presented in Table 3.
PBPs are used as natural pigments in food, replacing synthetic dyes, or as fluorescent probes in research [14]. Despite this, they are being studied for the development of nutraceuticals due to their bioactivities such as anti-viral, anti-cancer, antioxidant, and anti-inflammatory [15]. For this reason, current research on these molecules lies in function and biosynthesis mechanisms, structure elucidations, and potential applications. Isolation of PBPs has been reported in many species, for instance, Neoporphyra haitanensis [14], Kappaphycus alvarezii [16], Centroceras clavulatum [12], or N. yezoensis [16].

4. Mycosporine-Like Amino Acids

MAAs are small aminic secondary metabolites of MW below 400 Da (Figure 1) with strong absorption of ultraviolet (UV) radiation, typically between 320 and 360 nm. Thus, MAAs are useful molecules to protect cells from oxidative processes and solar UV-induced damage [17]. Up to now, more than 20 MAAs have been characterized in seaweeds and microalgae. From these, palaythine, asterina, shinorine, porphyra-334, mycosporine-glycine, usujirene, or palythene are most common in seaweeds [17]. They are naturally synthesized by various marine organisms, but seaweeds and microalgae are rich sources of them. However, they are much more abundant in red seaweeds, and only a small fraction of brown or green seaweeds presenting them [18]. For instance, porphyra-334 or shinorine are the most common in green or brown seaweeds such as Ulva intestinalis or Alaria esculenta, but red species like Pyropia columbina or C. crispus may additionally contain palythene much higher levels of mycosporine-glycine [18].

5. Protein-Derived Hydrolysates and Peptides

Peptides are protein fragments containing 2 to 40 AA in length generated from proteins by gastrointestinal digestion or from other hydrolyzation processes [19]. The importance of these molecules lies with the fact that some AA sequences, which are not active in SPs, show different biological properties after being released from the protein structure [20]. The development of algal peptides concentrates a blooming sector due to the diverse physiological activities of these molecules. Briefly, after the extraction and isolation of SPs, the main strategy to obtain BAPs from them involves their hydrolyzation (Figure 2). This may be performed by thermal, chemical, or enzymatic degradation, being the latter more extensively used since it allows more homogeneous and consistent patterns of hydrolyzation [21]. Thus, SP hydrolyzation using proteases can be used to maximize the yield of desired BAPs [21]. The process to describe the potential bioactive peptides requires testing different proteases in a single seaweed species [22][23][24], characterizing the BAP yield [25][26][27], optimizing the hydrolysis procedure [28], and exploring the effect of sequential hydrolysis using different proteases with defined conditions [29]. As hydrolyzation patterns and BAPs yielded are described, these approaches to define generated peptides allow covering a greater extent of potential bioactivities, as well as efficiency and effectiveness of extraction. Successful production of BPAs from hydrolyzed proteins of Porphyra spp, Palmaria palmata, Ulva spp, among others, have been reported [30][31][32].
Antioxidants 11 00176 g002 550
Figure 2. Schematic representation of seaweed protein hydrolysis into peptides. The hydrolyzation process usually involves the action of proteases and the adjustment of reaction parameters. Among the peptides produced by protein hydrolyzation, some display bioactive properties.

References

  1. Charoensiddhi, S.; Conlon, M.A.; Franco, C.M.M.; Zhang, W. The development of seaweed-derived bioactive compounds for use as prebiotics and nutraceuticals using enzyme technologies. Trends Food Sci. Technol. 2017, 70, 20–33.
  2. Yoshiie, T.; Maeda, M.; Kimura, M.; Hama, Y.; Uchida, M.; Kimura, Y. Structural features of N-glycans of seaweed glycoproteins: Predominant occurrence of high-mannose type N-glycans in marine plants. Biosci. Biotechnol. Biochem. 2012, 76, 1996–1998.
  3. Wijesekara, I.; Lang, M.; Marty, C.; Gemin, M.-P.; Boulho, R.; Douzenel, P.; Wickramasinghe, I.; Bedoux, G.; Bourgougnon, N. Different extraction procedures and analysis of protein from Ulva sp. in Brittany, France. J. Appl. Phycol. 2017, 29, 2503–2511.
  4. Thangam, R.; Senthilkumar, D.; Suresh, V.; Sathuvan, M.; Sivasubramanian, S.; Pazhanichamy, K.; Gorlagunta, P.K.; Kannan, S.; Gunasekaran, P.; Rengasamy, R.; et al. Induction of ROS-Dependent Mitochondria-Mediated Intrinsic Apoptosis in MDA-MB-231 Cells by Glycoprotein from Codium decorticatum. J. Agric. Food Chem. 2014, 62, 3410–3421.
  5. Barre, A.; Simplicien, M.; Benoist, H.; Van Damme, E.J.M.; Rougé, P. Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties. Mar. Drugs 2019, 17, 440.
  6. Frenkel, J.; Vyverman, W.; Pohnert, G. Pheromone signaling during sexual reproduction in algae. Plant J. 2014, 79, 632–644.
  7. Damme, E.J.M.; Van Peumans, W.J.; Barre, A.; Rougé, P. Plant Lectins: A Composite of Several Distinct Families of Structurally and Evolutionary Related Proteins with Diverse Biological Roles. CRC Crit. Rev. Plant Sci. 1998, 17, 575–692.
  8. Ambrosio, A.L.; Sanz, L.; Sánchez, E.I.; Wolfenstein-Todel, C.; Calvete, J.J. Isolation of two novel mannan- and L-fucose-binding lectins from the green alga Enteromorpha prolifera: Biochemical characterization of EPL-2. Arch. Biochem. Biophys. 2003, 415, 245–250.
  9. Wu, M.; Tong, C.; Wu, Y.; Liu, S.; Li, W. A novel thyroglobulin-binding lectin from the brown alga Hizikia fusiformis and its antioxidant activities. Food Chem. 2016, 201, 7–13.
  10. Günaydın, G.; Edfeldt, G.; Garber, D.A.; Asghar, M.; Noȅl-Romas, L.; Burgener, A.; Wählby, C.; Wang, L.; Rohan, L.C.; Guenthner, P.; et al. Impact of Q-Griffithsin anti-HIV microbicide gel in non-human primates: In situ analyses of epithelial and immune cell markers in rectal mucosa. Sci. Rep. 2019, 9, 18120.
  11. Fontenelle, T.P.C.; Lima, G.C.; Mesquita, J.X.; Lopes, J.L.; de Brito, T.V.; Vieira-Júnior, F.C.; Sales, A.B.; Aragão, K.S.; de Souza, M.H.L.P.; Barbosa, A.L.R.; et al. Lectin obtained from the red seaweed Bryothamnion triquetrum: Secondary structure and anti-inflammatory activity in mice. Int. J. Biol. Macromol. 2018, 112, 1122–1130.
  12. Nair, D.; Krishna, J.G.; Panikkar, M.V.N.; Nair, B.G.; Pai, J.G.; Nair, S.S. Identification, purification, biochemical and mass spectrometric characterization of novel phycobiliproteins from a marine red alga, Centroceras clavulatum. Int. J. Biol. Macromol. 2018, 114, 679–691.
  13. Yabuta, Y.; Fujimura, H.; Kwak, C.S.; Enomoto, T.; Watanabe, F. Antioxidant activity of the phycoerythrobilin compound formed from a dried Korean purple laver (Porphyra sp.) during in vitro digestion. Food Sci. Technol. Res. 2010, 16, 347–351.
  14. Chen, X.; Wu, M.; Yang, Q.; Wang, S. Preparation, characterization of food grade phycobiliproteins from Porphyra haitanensis and the application in liposome-meat system. LWT Food Sci. Technol. 2017, 77, 468–474.
  15. Li, W.; Su, H.; Pu, Y.; Chen, J.; Liu, L.; Liu, Q.; Qin, S. Phycobiliproteins: Molecular structure, production, applications, and prospects. Biotechnol. Adv. 2019, 37, 340–353.
  16. Guan, X.; Wang, J.; Zhu, J.; Yao, C.; Liu, J.; Qin, S.; Jiang, P. Photosystem II Photochemistry and Phycobiliprotein of the Red Algae Kappaphycus alvarezii and Their Implications for Light Adaptation. BioMed Res. Int. 2013, 2013, 256549.
  17. Gacesa, R.; Lawrence, K.P.; Georgakopoulos, N.D.; Yabe, K.; Dunlap, W.C.; Barlow, D.J.; Wells, G.; Young, A.R.; Long, P.F. The mycosporine-like amino acids porphyra-334 and shinorine are antioxidants and direct antagonists of Keap1-Nrf2 binding. Biochimie 2018, 154, 35–44.
  18. Sun, Y.; Zhang, N.; Zhou, J.; Dong, S.; Zhang, X.; Guo, L.; Guo, G. Distribution, Contents, and Types of Mycosporine-Like Amino Acids (MAAs) in Marine Macroalgae and a Database for MAAs Based on These Characteristics. Mar. Drugs 2020, 18, 43.
  19. Cian, R.E.; Martínez-Augustin, O.; Drago, S.R. Bioactive properties of peptides obtained by enzymatic hydrolysis from protein byproducts of Porphyra columbina. Food Res. Int. 2012, 49, 364–372.
  20. Lorenzo, J.M.; Munekata, P.E.S.; Gómez, B.; Barba, F.J.; Mora, L.; Pérez-Santaescolástica, C.; Toldrá, F. Bioactive peptides as natural antioxidants in food products—A review. Trends Food Sci. Technol. 2018, 79, 136–147.
  21. Echave, J.; Fraga-Corral, M.; Garcia-Perez, P.; Popović-Djordjević, J.; Avdović, E.H.; Radulović, M.; Xiao, J.; Prieto, M.A.; Simal-Gandara, J. Seaweed Protein Hydrolysates and Bioactive Peptides: Extraction, Purification and Applications. Mar. Drugs 2021, 19, 500.
  22. Cao, D.; Lv, X.; Xu, X.; Yu, H.; Sun, X.; Xu, N. Purification and identification of a novel ACE inhibitory peptide from marine alga Gracilariopsis lemaneiformis protein hydrolysate. Eur. Food Res. Technol. 2017, 243, 1829–1837.
  23. Sun, S.; Xu, X.; Sun, X.; Zhang, X.; Chen, X.; Xu, N. Preparation and identification of ACE inhibitory peptides from the marine macroalga Ulva intestinalis. Mar. Drugs 2019, 17, 179.
  24. Admassu, H.; Gasmalla, M.A.A.; Yang, R.; Zhao, W. Identification of Bioactive Peptides with α-Amylase Inhibitory Potential from Enzymatic Protein Hydrolysates of Red Seaweed (Porphyra spp). J. Agric. Food Chem. 2018, 66, 4872–4882.
  25. Beaulieu, L.; Sirois, M.; Tamigneaux, É. Evaluation of the in vitro biological activity of protein hydrolysates of the edible red alga, Palmaria palmata (dulse) harvested from the Gaspe coast and cultivated in tanks. J. Appl. Phycol. 2016, 28, 3101–3115.
  26. Indumathi, P.; Mehta, A. A novel anticoagulant peptide from the Nori hydrolysate. J. Funct. Foods 2016, 20, 606–617.
  27. Paiva, L.; Lima, E.; Neto, A.I.I.; Baptista, J. Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate. J. Funct. Foods 2016, 26, 65–76.
  28. Zhang, X.; Cao, D.; Sun, X.; Sun, S.; Xu, N. Preparation and identification of antioxidant peptides from protein hydrolysate of marine alga Gracilariopsis lemaneiformis. J. Appl. Phycol. 2019, 31, 2585–2596.
  29. Furuta, T.; Miyabe, Y.; Yasui, H.; Kinoshita, Y.; Kishimura, H. Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Phycobiliproteins of Dulse Palmaria palmata. Mar. Drugs 2016, 14, 32.
  30. Cermeño, M.; Stack, J.; Tobin, P.R.; O’Keeffe, M.B.; Harnedy, P.A.; Stengel, D.B.; FitzGerald, R.J. Peptide identification from a Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities. Food Funct. 2019, 10, 3421–3429.
  31. Harnedy, P.A.; O’Keeffe, M.B.; FitzGerald, R.J. Purification and identification of dipeptidyl peptidase (DPP) IV inhibitory peptides from the macroalga Palmaria palmata. Food Chem. 2015, 172, 400–406.
  32. Cian, R.E.; Hernández-Chirlaque, C.; Gámez-Belmonte, R.; Drago, S.R.; Sánchez de Medina, F.; Martínez-Augustin, O. Green alga Ulva spp. hydrolysates and their peptide fractions regulate cytokine production in splenic macrophages and lymphocytes involving the TLR4-NFκB/MAPK pathways. Mar. Drugs 2018, 16, 235.
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