Minsk, Беларусь
Minsk, Беларусь
Minsk, Беларусь
Minsk, Беларусь
Minsk, Беларусь
Minsk, Беларусь
Stavropol, Россия
Stavropol, Россия
Chitosan reacts with amino acids and hydrolyzed whey proteins to produce biologically active complexes that can be used in functional foods. The research objective was to obtain chitosan biocomposites with peptides and amino acids with improved antioxidant and sensory properties. The research featured biocomposites of chitosan and succinylated chitosan with whey peptides and amino acids. The methods of pH metry and spectrophotometry were employed to study the interaction parameters between polysaccharides and peptides, while colorimetry and spectrophotometry served to describe the amino acids content. The antiradical effect was determined by the method of fluorescence recovery. Pure compounds and their complexes underwent a sensory evaluation for bitterness. Chitosan and succinylated chitosan formed complexes with whey peptides and such proteinogenic amino acids as arginine, valine, leucine, methionine, and tryptophan. The equimolar binding of tryptophan, leucine, and valine occurred in an aqueous chitosan solution (in terms of glucosamine). Methionine appeared to be the least effective in chitosan interaction, while arginine failed to complex both with chitosan and succinylated chitosan. Chitosan and succinylated chitosan biocomposites with peptides and leucine, methionine, and valine proved to be less bitter that the original substances. The samples with arginine maintained the same sensory properties. Chitosan complexes with tryptophan and peptides increased their antioxidant activity by 1.7 and 2.0 times, respectively, while their succinylated chitosan complexes demonstrated a 1.5 fold increase. Chitosan and succinylated chitosan biocomplexes with tryptophan and whey protein peptides had excellent antioxidant and sensory properties. However, chitosan proved more effective than succinylated chitosan, probably, because it was richer in protonated amino groups, which interacted with negatively charged amino acids groups.
Chitosan, succinylated chitosan, whey peptides, proteinogenic amino acids, chitosan biocomposites
1. Shivanna SK, Nataraj BH. Revisiting therapeutic and toxicological fingerprints of milk-derived bioactive peptides: An overview. Food Bioscience. 2020;38. https://doi.org/10.1016/j.fbio.2020.100771
2. Zhao C, Ashaolu TJ. Bioactivity and safety of whey peptides. LWT. 2020;134. https://doi.org/10.1016/j.lwt.2020.109935
3. Ye H, Tao X, Zhang W, Chen Y, Yu Q, Xie J. Food-derived bioactive peptides: production, biological activities, opportunities and challenges. Journal of Future Foods. 2022;2(4):294-306. https://doi.org/10.1016/j.jfutfo.2022.08.002
4. Nutten S, Schuh S, Dutter T, Heine RG, Kuslys M. Design, quality, safety and efficacy of extensively hydrolyzed formula for management of cow’s milk protein allergy: What are the challenges? Advances in Food and Nutrition Research. 2020;93:147-204. https://doi.org/10.1016/bs.afnr.2020.04.004
5. Liceaga AM, Hall F. Nutritional, functional and bioactive protein hydrolysates. In: Melton L, Shahidi F, Varelis P, editors. Encyclopedia of food chemistry. Reference work. Vol. 3. Elsevier; 2019. pp. 456-464. https://doi.org/10.1016/B978-0-08-100596-5.21776-9
6. Iwaniak A, Minkiewicz P, Darewicz M, Hrynkiewicz M. Food protein-originating peptides as tastants - Physiological, technological, sensory, and bioinformatic approaches. Food Research International. 2016;89:27-38. https://doi.org/10.1016/j.foodres.2016.08.010
7. Murray NM, Jacquie JC, O’Sullivan M, Hallihan A, Murphy E, Feeney EL, et al. Using rejection thresholds to determine acceptability of novel bioactive compounds added to milk-based beverages. Food Quality and Preference. 2019;73:276-283. https://doi.org/10.1016/j.foodqual.2018.10.014
8. Gonzalez Pereira A, Carpena M, García Oliveira P, Mejuto JC, Prieto MA, Simal Gandara J. Main applications of cyclodextrins in the food industry as the compounds of choice to form host-guest complexes. International Journal of Molecular Sciences. 2021;22(3). https://doi.org/10.3390/ijms22031339
9. Rudolph S, Riedel E, Henle T. Studies on the interaction of the aromatic amino acids tryptophan, tyrosine and phenylalanine as well as tryptophan-containing dipeptides with cyclodextrins. European Food Research and Technology. 2018;244(9):1511-1519. https://doi.org/10.1007/s00217-018-3065-9
10. Li J, Geng S, Liu B, Wang H, Liang G. Self-assembled mechanism of hydrophobic amino acids and β-cyclodextrin based on experimental and computational methods. Food Research International. 2018;112:136-142. https://doi.org/10.1016/j.foodres.2018.06.017
11. Halavach TM, Savchuk ES, Bobovich AS, Dudchik NV, Tsygankow VG, Tarun EI, et al. Antimutagenic and antibacterial activity of β-cyclodextrin clathrates with extensive hydrolysates of colostrum and whey. Biointerface Research in Applied Chemistry. 2021;11(2):8626-8638. https://doi.org/10.33263/BRIAC112.86268638
12. Halavach TM, Kurchenko VP, Tsygankow VG, Bondaruk AM, Tarun EI, Asafov VA. β-Cyclodextrin nanocomplexes with biologically active peptides from hydrolysed bovine whey and colostrum. Biointerface Research in Applied Chemistry. 2022;12(6):8502-8514. https://doi.org/10.33263/BRIAC126.85028514
13. Irastorza A, Zarandona I, Andonegi M, Guerrero P, de la Caba K. The versatility of collagen and chitosan: From food to biomedical applications. Food Hydrocolloids. 2021;116. https://doi.org/10.1016/j.foodhyd.2021.106633
14. Silva AO, Cunha RS, Hotza D, Francisco Machado RA. Chitosan as a matrix of nanocomposites: A review on nanostructures, processes, properties, and applications. Carbohydrate Polymers. 2021;272. https://doi.org/10.1016/j.carbpol.2021.118472
15. Ahmad SI, Ahmad R, Khan MS, Kant R, Shahid S, Gautam L, et al. Chitin and its derivatives: Structural properties and biomedical applications. International Journal of Biological Macromolecules. 2020;164:526-539. https://doi.org/10.1016/j.ijbiomac.2020.07.098
16. Wani TU, Pandith AH, Sheikh FA. Polyelectrolytic nature of chitosan: Influence on physicochemical properties and synthesis of nanoparticles. Journal of Drug Delivery Science and Technology. 2021;65. https://doi.org/10.1016/j.jddst.2021.102730
17. Benchamas G, Huang G, Huang S, Huang H. Preparation and biological activities of chitosan oligosaccharides. Trends in Food Science and Technology. 2021;107:38-44. https://doi.org/10.1016/j.tifs.2020.11.027
18. Lee JS, Nah H, Moon H-J, Lee SJ, Heo DN, Kwon IK. Controllable delivery system: A temperature and pH-responsive injectable hydrogel from succinylated chitosan. Applied Surface Science. 2020;528. https://doi.org/10.1016/j.apsusc.2020.146812
19. Deka BC, Bhattacharyya PK. DFT study on host-guest interaction in chitosan-amino acid complexes. Computational and Theoretical Chemistry. 2017;1110:40-49. https://doi.org/10.1016/j.comptc.2017.03.036
20. Medeiros Borsagli FGL, Carvalho IC, Mansur HS. Amino acid-grafted and N-acylated chitosan thiomers: Construction of 3D bio-scaffolds for potential cartilage repair applications. International Journal of Biological Macromolecules. 2018;114:270-282. https://doi.org/10.1016/j.ijbiomac.2018.03.133
21. Wang S, Shi L, Zhang S, Wang H, Cheng B, Zhuang X, et al. Proton-conducting amino acid-modified chitosan nanofibers for nanocomposite proton exchange membranes. European Polymer Journal. 2019;119:327-334. https://doi.org/10.1016/j.eurpolymj.2019.07.041
22. Rafiee F, Rezaie Karder F. Bio-crosslinking of chitosan with oxidized starch, its functionalization with amino acid and magnetization: As a green magnetic support for silver immobilization and its catalytic activity investigation. International Journal of Biological Macromolecules. 2020;146:1124-1132. https://doi.org/10.1016/j.ijbiomac.2019.09.238
23. Taketa TB, Mahl CRA, Calais GB, Beppu MM. Amino acid-functionalized chitosan beads for in vitro copper ions uptake in the presence of histidine. International Journal of Biological Macromolecules. 2021;188:421-431. https://doi.org/10.1016/j.ijbiomac.2021.08.017
24. Fernandes J, Ghate MV, Basu Mallik S, Lewis SA. Amino acid conjugated chitosan nanoparticles for the brain targeting of a model dipeptidyl peptidase-4 inhibitor. International Journal of Pharmaceutics. 2018;547(1-2):563-571. https://doi.org/10.1016/j.ijpharm.2018.06.031
25. Hefni HHH, Nagy M, Azab MM, Hussein MHM. O-Acylation of chitosan by L-arginine to remove the heavy metals and total organic carbon (TOC) from. Egyptian Journal of Petroleum. 2020;29(1):31-38. https://doi.org/10.1016/j.ejpe.2019.10.001
26. Wang Y, Han Q, Wang Y, Qin D, Luo Q, Zhang H. Self-assembly, rheological properties and antioxidant activities of chitosan grafted with tryptophan and phenylalanine. Colloids and Surfaces A: Physicochemical and Engineering Aspects. 2020;597. https://doi.org/10.1016/j.colsurfa.2020.124763
27. Pereira MBB, França DB, Araújo RC, Silva-Filho EC, Rigaud B, Fonseca MG, et al. Amino hydroxyapatite/chitosan hybrids reticulated with glutaraldehyde at different pH values and their use for diclofenac removal. Carbohydrate Polymers. 2020;236. https://doi.org/10.1016/j.carbpol.2020.116036
28. Torkaman S, Rahmani H, Ashori A, Najafi SHM. Modification of chitosan using amino acids for wound healing purposes: A review. Carbohydrate Polymers. 2021;258. https://doi.org/10.1016/j.carbpol.2021.117675
29. Zhong Y, Shahidi F. Methods for the assessment of antioxidant activity in foods. In: Shahidi F, editor. Handbook of antioxidants for food preservation. A volume in Woodhead Publishing Series in Food Science, Technology and Nutrition. Woodhead Publishing; 2015. pp. 287-333. https://doi.org/10.1016/b978-1-78242-089-7.00012-9
30. Tarun EI, Zaitseva MV, Kravtsova OI, Kurchenko VP, Golovach TN. Effect of whey protein peptides on recovery of fluorescence level in system with activated form of oxygen. Proceedings of the Belarusian State University. Series of Physiological, Biochemical and Molecular Biology Sciences. 2016;11(1):231-236. (In Russ.). https://www.elibrary.ru/ymgpfb
31. Hu Z, Qin YQ, Guang J, Cai Y. Preparation and characterization of chitosan amino acid salts. IOP Conference Series: Materials Science and Engineering. 2019;504. https://doi.org/10.1088/1757-899X/504/1/012023
32. Daroit DJ, Brandelli A. In vivo bioactivities of food protein-derived peptides - a current review. Current Opinion in Food Science. 2021;39:120-129. https://doi.org/10.1016/j.cofs.2021.01.002
33. Bielecka M, Cichosz G, Czeczot H. Antioxidant, antimicrobial and anticarcinogenic activities of bovine milk proteins and their hydrolysates - A review. International Dairy Journal. 2022;127. https://doi.org/10.1016/j.idairyj.2021.105208
34. Galland F, de Espindola JS, Lopes DS, Taccola MF, Pacheco MTB. Food-derived bioactive peptides: Mechanisms of action underlying inflammation and oxidative stress in the central nervous system. Food Chemistry Advances. 2022;1. https://doi.org/10.1016/j.focha.2022.100087
35. Anraku M, Gebicki JM, Iohara D, Tomida H, Uekama K, Maruyama T, et al. Antioxidant activities of chitosans and its derivatives in in vitro and in vivo studies. Carbohydrate Polymers. 2018;199:141-149. https://doi.org/10.1016/j.carbpol.2018.07.016
36. Abd El-Hack ME, El-Saadony MT, Shafi ME, Zabermawi NM, Arif M, Batiha GE, et al. Antimicrobial and antioxidant properties of chitosan and its derivatives and their applications: A review. International Journal of Biological Macromolecules. 2020;164:2726-2744. https://doi.org/10.1016/j.ijbiomac.2020.08.153
