In Vitro Anti-Oxidation and Anti-Cholinesterase Activities of Tuna and Chicken Hydrolysates and their Maillard Reaction Products
DOI:
https://doi.org/10.31584/jhsmr.2023998Keywords:
bioactive peptides, Maillard reaction products, anti-oxidation, acetylcholinesterase inhibitorsAbstract
Objective: To evaluate the anti-oxidation and anticholinesterase activities and cell viability of chicken and tuna hydrolysates and their Maillard reaction products.
Material and Methods: Maillard reaction products (MRPs) derived from chicken or tuna hydrolysates were prepared by heating the hydrolysate with glucose at 84 °C for 90 minutes. Physical characteristics, ultraviolet (UV) absorbance, browning intensity, protein concentrations, molecular weight distribution, and amino acid profiles of the hydrolysates and MRPs were determined. The anti-oxidation properties of the hydrolysate and MRPs were evaluated by 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging assay. Anti-cholinesterase activities were evaluated using Ellman’s method. Cell viability of the samples was evaluated in RAW 264.7 cells.
Results: The MRPs presented as brown to dark brown liquids with Brix values ranging from 61.33 to 64.17 °Brix. The pH value ranged from 5.31 to 6.20. The UV absorbance at 294 nm and browning intensity at 420 nm of the MRPs were less than the absorbance of the corresponding hydrolysates. The protein concentrations were 41-44% (hydrolysates) and 18-20% (MRPs). The major constituents of the hydrolysates and MRPs were small molecules (MW<300 Da). The samples exhibited anti-oxidative activity (EC50 2.03 - 3.51 mg/mL) and anti-acetylcholinesterase activity (45-52% inhibition at 0.5 mg/mL). Both hydrolysates and MRPs showed no toxicity to RAW 264.7 cells at concentrations up to 1 mg/mL.
Conclusion: Chicken and tuna hydrolysates and their MRPs exhibited mild anti-oxidative and moderate acetylcholinesterase inhibitory activities.
References
Definition of Functional Food [homepage on the Internet] Texas: Functional Food Center, Inc.; 2023 [cited 2023 Apr 2]. Available from: https://www.functionalfoodscenter.net/
Thailand: food industry [homepage on the Internet] Bangkok: Thailand Board of Investment; 2023 [cited 2023 Apr 4]. Available from: https://www.boi.go.th/upload/content/Food%20industry_5aa7b40bd758b.pdf
Sarmadi BH, Ismail A. Antioxidative peptides from food proteins: a review. Peptides 2010; 31:1949-56.
Himaya SWA, Ngo DH, Ryu BM, Kim SK. An active peptide purified from gastrointestinal enzyme hydrolysate of Pacific cod skin gelatin attenuates angiotensin-1 converting enzyme (ACE) activity and cellular oxidative stress. Food Chem 2012;132:1872-82.
Betoret E, Betoret N, Vidal D, Fito P. Functional foods development: trends and technologies, Trends Food Sci Technol 2011;22:498–508.
Pihlanto-Leppälä A. Bioactive peptides derived from bovine whey proteins: opioid and ACE-inhibitory peptides. Trends Food Sci Tech 2001;11:347-56.
Ngo DH, Vo TS, Ngo DN, Wijesekara I, Kim SK. Biological activities and potential health benefits of bioactive peptides derived from marine organisms. Int J Biol Macromol 2012;51:378-83.
Li-Chan ECY. Bioactive peptides and protein hydrolysates: research trends and challenges for application as nutraceuticals and functional food ingredients. Curr Opin Food Sci 2015;1:28-37.
Fu Y, Zhang Y, Soladoye OP, Aluko RE. Maillard reaction products derived from food protein-derived peptides: insights into flavor and bioactivity. Crit Rev Food Sci Nutr 2020;60:3429-42.
Horvat S, Roscic M. Glycosylation of lysine-containing pentapeptides by glucuronic acid: New insights into the Maillard reaction. Carbohydr Res 2010;345:377-84.
Karnjanapratum S, O’Callaghan YC, Benjakul S, O’Brien NM. In vitro cellular bioactivities of Maillard reaction products from sugar-gelatin hydrolysate of unicorn leatherjacket skin system. J Funct Foods 2016;23:87-94.
Song R, Shi QQ, Yang PY, Wei RB. Identification of antibacterial peptides from Maillard reaction products of half-fin anchovy hydrolysates/glucose via LC-ESI-QTOF-MS analysis. J Funct Foods 2017;36:387–95.
Zhao T, Zhang Q, Wang S, Qiu C, Liu Y, Su G, et al. Effects of Maillard reaction on bioactivities promotion of anchovy protein hydrolysate: The key role of MRPs and newly formed peptides with basic and aromatic amino acids. LWT 2018;97:245-253.
Nie XH, Zhao LM, Regenstein JM, Xu D, Meng XH. Antioxidant capacity of Maillard reaction products’ fractions with different molecular weight distribution from chicken bone hydrolysate-galactose system. Int J Food Sci Technol 2017; 52:1632-38.
Oh JG, Chun SH, Kim DH et al. Anti-inflammatory effect of sugar-amino acid Maillard reaction products on intestinal inflammation model in vitro and in vivo. Carbohydr Res 2017;449:47-58.
Holzgrabe U, Kapková P, Alptüzün V, Scheiber J, Kugelmann E. Targeting acetylcholinesterase to treat neurodegeneration. Expert Opin Ther Targets 2007;11: 161-79.
Pizzino G, Irrera N, Cucinotta M, Pallio G, Mannino F, Arcoraci V, et al. Oxidative stress: harms and benefits for human health. Oxid Med Cell Longev 2017;2017:8416763.
Furman D, Campisi J, Verdin E, Carrera-Bastos P, Targ S, Franceschi C, et al. Chronic inflammation in the etiology of disease across the life span. Nat Med 2019;25:1822–32.
Chen K, Yang Q, Hong H, Feng L, Liu J, Luo Y. Physicochemical and functional properties of Maillard reaction products derived from cod (Gadus morhua L.) skin collagen peptides and xylose. Food Chem 2020;333:127489.
Baliyan S, Mukherjee R, Priyadarshini A, Vibhuti A, Gupta A, Pandey RP, Chang CM. Determination of antioxidants by DPPH radical scavenging activity and quantitative phytochemical Analysis of Ficus religiosa. Molecules 2022;27:1326.
Ellman GL, Courtney KE, Andres V, Featherstone RM. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharm 1961;7:88-95.
Suwanhom P, Nualnoi T, Khongkow P, Lee VS, Lomlim L. Synthesis and evaluation of chromone-2-carboxamidoalkylamines as potent acetylcholinesterase inhibitors. Med Chem Res 2020;29:564-74.
Joo T, Sowndhararajan K, Hong S, Lee J, Park SY, Kim S, Jhoo JW. Inhibition of nitric oxide production in LPS-stimulated RAW 264.7 cells by stem bark of Ulmus pumila L. Saudi J Biol Sci 2014;21:427-35.
Ameruoso A, Palomba R, Palange AL, Cervadoro A, Lee A, Di Mascolo D, Decuzzi P. Ameliorating amyloid-β fibrils triggered inflammation via curcumin-loaded polymeric nanoconstructs. Front Immunol 2017;8:1411.
Temussi PA. The good taste of peptides. J Pept Sci 2012;18:73-82.
Zhang Y, Dorjpalam B, Ho CT. Contribution of peptides to volatile formation in the Maillard reaction of casein hydrolysate with glucose. J Agric Food Chem 1992;40:2467-71.
Van Lancker F, Adams A, De Kimpe N. Chemical modifications of peptides and their impact on food properties. Chem Rev 2011;111:7876-903.
Fu Y, Zhang Y, Soladoye OP, Aluko RE. Maillard reaction products derived from food protein-derived peptides: insights into flavor and bioactivity. Crit Rev Food Sci Nutr 2020;60:3429-42.
Zhu D, Damodaran S, Lucey JA. Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates produced in aqueous solution. J Agric Food Chem 2010;58:2988-94.
Nooshkam M, Varidi M, Bashash M. The Maillard reaction products as food-born antioxidant and anti-browning agents in model and real food systems. Food Chem 2019;275:644-60.
Chen K, Zhao J, Shi X, Abdul Q, Jiang Z. Characterization and antioxidant activity of products derived from xylose-bovine casein hydrolysate Maillard reaction: Impact of reaction time. Foods 2019;8:242.
Hampel H, Hardy J, Blennow K, Chen C, Perry G, Kim SH et al. The Amyloid-β pathway in Alzheimer’s disease. Mol Psychiatry 2021;26:5481–503.
Downloads
Published
How to Cite
Issue
Section
License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
