Effects of Fish Drying Methods on Functional, Antioxidant, and Antimicrobial Properties of African Catfish Protein Hydrolysates
DOI:
https://doi.org/10.24925/turjaf.v13i10.3070-3079.7904Keywords:
Hydrolysate, peptide, pepsin, African catfish, Hydrolysis degree, antioxidant, functional propertyAbstract
The study enzymatically hydrolyzed protein isolates from fresh and processed (freeze-dried and oven-dried) fillets of African catfish (ACF). The functional, antioxidant, and antimicrobial potentials of the ACF fillet protein hydrolysate (ACFPH) were investigated to expand the possibilities for their potential application in human health. ACF fillet was obtained and divided into three parts: the first part was freeze-dried, the second was oven-dried, and the last part was left fresh. Protein isolates were prepared from them and hydrolysed with pepsin. The degree of hydrolysis (DH) and peptide chain length (PCL) were calculated. The study analyzed the ACF fillet protein hydrolysates’ water and oil absorption capacity (functional properties). Antioxidant activity was estimated through ferric reducing power, metal chelating, and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging assays. The antimicrobial activity was tested using agar disc methods. The DH was time-dependent and indirectly proportional to PCL. Freeze-dried catfish fillet protein hydrolysate (FD-CFPH) was better hydrolyzed with 87 ± 3.54 % hydrolysis degree, and gave the least PCL value of 1.15. Fresh catfish fillet protein hydrolysate (FR-CFPH) was better water absorbent than FD-CFPH and oven-dried catfish fillet protein hydrolysate (OD-CFPH). FD-CFPH displayed the best oil absorption capacity (23.7 ± 1.75 mL/g). All antioxidant assays displayed concentration-dependent activity. FR-CFPH displayed the highest metal chelating activity and DPPH radical scavenging potential, while OD-CFPH showed the highest ferric reducing power. All the pepsin-produced ACFPH resulted in a high antifungal activity against Penicillium camemberti, but only FD-CFPH at the highest concentration was effective against Aspergillus flavus. For each examined bacterium, no discernible inhibitory zone was observed, suggesting that the hydrolysates were ineffective against the bacteria. The potential functional and antioxidant activities elicited by the ACFPH suggest that it could be employed to develop nutraceutical and therapeutic products for alleviating oxidative stress-related ailments.
References
Abd El-Rady, T. K., Tahoun, A. M., Abdin, M., & Amin, H. F. (2023). Effect of different hydrolysis methods on composition and functional properties of fish protein hydrolysate obtained from Bigeye tuna waste. International Journal of Food Science and Technology, 58(12), 6552–6562. https://doi.org/10.1111/ijfs.16769.
Adepoju, A. A., Isinkaye, O. D., Ofeniforo, B. E., Adeyiola, I. O., Agada, E. S. & Ayo-Dada, D. O. (2022). Comparative analysis of amino acid composition in the head, muscle, and tail of fresh African catfish (Clarias gariepinus). Journal of Agricultural Chemistry and Environment, 11, 231-239. https://doi.org/10.4236/jacen.2022.114016
Akbarian, M., Khani, A., Eghbalpour, S. & Uversky, V.N. (2022). Bioactive peptides: synthesis, sources, applications, and proposed mechanisms of action. International Journal of Molecular Sciences, 23, 1445-1475. https://doi.org/ 10.3390/ijms23031445.
Akinpelu, D. A., Aiyegoro, A. O. & Okoh, A. I. (2009). Studies on the biocidal and cell membrane disruption potentials of stem bark extracts of Afzelia africana (Smith). Biological Research, 42, 249-349. http://dx.doi.org/10.4067/S0716-97602009000300008
Alak, G., Atamanalp, M., Uçar, A., & Ozogul, F. (2025). Commercialization and pilot-scale production of fish protein hydrolysate: Challenges and recent developments. In Nirmal, N., Santivarangkna, C., Bekhit, A. E. D. A., & Barba, F. J. (Eds), Fish protein hydrolysates: from production to food and nutraceutical industry applications. (pp 315-341). Elsevier. https://doi.org/10.1016/B978-0-443-21654-1.00012-4
Aluko, R. E. (2015). Antihypertensive peptides from food proteins. Annual Review Food Science Technology, 6, 235–262. https://doi.org/10.1146/annurev-food-022814-015520.
Aluko, R. E. (2021). Cardiovascular benefits of food protein-derived bioactive peptides. In Biologically Active Peptides (pp. 581-606). Academic Press. https://doi.org/10.1016/b978-0-12-821389-6.00009-1
Babu, D., Gurumurthy, P., Borra, S. K. & Cherian, K. M. (2013). Antioxidant and free radical scavenging activity of triphala determined by using different in vitro models. Journal of Medicinal Plants Research, 7(39), 2898-2905. https://doi.org/10.5897/JMPR2013.5124
Baraiya, R., Anandan, R., Elavarasan, K., Prakash, P., Rathod, S. K., Rajasree, S. R. & Renuka, V. (2024). Potential of fish bioactive peptides for the prevention of global pandemic non-communicable disease: production, purification, identification, and health benefits. Discover Food, 4(1), 34-54. https://doi.org/10.1007/s44187-024-00097-5.
Bashir, K. M. I., Chakniramol, S., Mansoor, S., Jahn, A., Cho, M.-G., & Choi, J.-S. (2024). Antioxidant Activity of Protein Hydrolysates from Redlip Mullet (Chelon haematocheilus) Muscle and Byproducts. Foods, 13(18), 3009. https://doi.org/10.3390/foods13183009
Canti, M., Sulistio, M.F., Wirawan, C.A., Prasetyanto, Y.E.A. & Lestari, D. (2023). A comparison of physicochemical, functional, and sensory properties of catfish protein isolate (Clarias gariepinus) produced using different defatting solvent. Food Research, 7(3), 1 – 11. https://doi.org/10.26656/fr.2017.7(3).860
Chalamaiah, M., Jyothirmayi, T., Diwan, P. V. & Dinesh Kumar, B. (2015). Antioxidant activity and functional properties of enzymatic protein hydrolysates from common carp (Cyprinus carpio) roe (egg). Journal of Food Science and Technology, 52, 5817-5825. https://doi.org/10.1007/s13197-015-1714-6
Chel-Guerrero, L., Cua-Aguayo, D., Betancur-Ancona, D., Chuc-Koyoc, A., Aranda-González, I. & Gallegos-Tintoré, S., (2020). Antioxidant and chelating activities from Lion fish (Pterois volitans L.) muscle protein hydrolysates produced by in vitro digestion using pepsin and pancreatin. Emirates Journal of Food and Agriculture, 32(1), 62-72. https://doi.org/10.9755/ejfa.2020.v32.i1.2060.
Dash, U. C., Bhol, N. K., Swain, S. K., Samal, R. R., Nayak, P. K., Raina, V., Panda, S. K., Kerry, R. G., Duttaroy, A. K. & Jena, A. B. (2025). Oxidative stress and inflammation in the pathogenesis of neurological disorders: Mechanisms and implications. Acta Pharmaceutica Sinica B, 15(1), 15-34. https://doi.org/10.1016/j.apsb.2024.10.004
Diniz, F. M. & Martin, A. M. (1997). Effects of the extent of enzymatic hydrolysis on functional properties of shark protein hydrolysate. LWT-food Science and Technology, 30(3), 266-272. https://doi.org/10.1006/fstl.1996.0184
Elavarasan, K. & Shamasundar, B. A. (2016). Effect of oven drying and freeze drying on the antioxidant and functional properties of protein hydrolysates derived from freshwater fish (Cirrhinus mrigala) using papain enzyme. Journal of Food Science and Technology, 53, 1303–1311. https://doi.org/10.1007/s13197-015-2084-9
Elavarasan, K., Shamasundar, B. A., Badii, F. & Howell, N. (2016). Angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven- and freeze-dried protein hydrolysate from freshwater fish (Cirrhinus mrigala). Food Chemistry, 206, 210-216. https://doi.org/10.1016/j.foodchem.2016.03.047
Elias, R. J., Kellerby, S. S. & Decker, E. A., (2008). Antioxidant activity of proteins and peptides. Critical Reviews in Food Science and Nutrition, 48(5), 430-441. https://doi.org/10.1080/10408390701425615
Foh, M. B. K., Amadou, I., Foh, B. M., Kamara, M. T., & Xia, W. (2010). Functionality and antioxidant properties of tilapia (Oreochromis niloticus) as influenced by the degree of hydrolysis. International Journal of Molecular Sciences, 11(4), 1851-1869. https://doi.org/10.3390/ijms11041851
Gaspar, A. L, & de Góes-Favoni, S. P. (2015). Action of microbial transglutaminase (MTGase) in the modification of food proteins: a review. Food Chemistry, 171, 315-22. https://doi.org/10.1016/j.foodchem.2014.09.019
Girgih, A. T., Udenigwe, C. C., Hasan, F. M., Gill, T. A. & Aluko, R. E. (2013). Antioxidant properties of Salmon (Salmo salar) protein hydrolysate and peptide fractions isolated by reverse-phase HPLC. Food Research International, 52(1), 315–322. https://doi.org/10.1016/j.foodres.2013.03.034
Guo, Y., Michael, N., Fonseca Madrigal, J., Sosa Aguirre, C. & Jauregi, P. (2019). Protein hydrolysate from Pterygoplichthys disjunctivus, armoured catfish, with high antioxidant activity. Molecules, 24(8), 1628. https://doi.org/10.3390/molecules24081628
Halim, N., Yusof, H. & Sarbon, N. (2016). Functional and bioactive properties of fish protein hydrolysates and peptides: a comprehensive review. Trends in Food Science & Technology, 51, 24–33. https://doi.org/10.1016/j.tifs.2016.02.007
Haryati, S., Budijanto, S. & Prangdimurti, E. (2021). Bioactive peptides from hydrolysates of Indonesian catfish protein isolate: characterization and properties of its antioxidant capacity. AACL Bioflux, 14(4), 1990-1999.
He, X., Cao, W., Zhao, Z. & Zhang, C. (2013). Analysis of protein composition and antioxidant activity of hydrolysates from Paphia undulate. Journal of Food and Nutrition Research, 1(3), 30-36.
Heffernan, S., Giblin, L. & O’Brien, N. (2021). Assessment of the biological activity of fish muscle protein hydrolysates using in vitro model systems. Food Chemistry, 359, 129852. https://doi.org/10.1016/j.foodchem.2021.129852
Igbinosa, O. O., Igbinosa, E. O., & Aiyegoro, O. A. (2009). Antimicrobial activity and phytochemical screening of stem bark extracts from Jatropha curcas (Linn). African Journal of Pharmacy and Pharmacology, 3 (2), 58-62. https://doi.org/10.5897/AJPP.9000049
Kusumaningtyas, E., Nurilmala, M. & Sibarani, D. (2019). Antioxidant and antifungal activities of collagen hydrolysates from the skin of milkfish (Chanos chanos) hydrolyzed using various Bacillus proteases. In IOP Conference Series: Earth and Environmental Science, 278(1), 012040. IOP Publishing. https://doi.org/10.1088/1755-1315/278/1/012040
Liu, L. L., Wang, H., Ren, G. Y., Duan, X., Li, D. & Yin, G. J. (2015). Effects of freeze-drying and spray drying processes on the functional properties of phosphorylation of egg white protein. International Journal of Agricultural and Biological Engineering, 8(4), 116－123. https://doi.org/10.3965/j.ijabe.20150804.1942
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193 (1), 265-275. https://doi.org/10.1016/S0021-9258(19)52451-6
Muangrod, P., Charoenchokpanich, W., Rungsardthong, V., Vatanyoopaisarn, S., Wonganu, B., Roytrakul, S. & Thumthanaruk, B. (2021). Effect of pepsin hydrolysis on antioxidant activity of jellyfish protein hydrolysate. In E3S Web of Conferences, 302, 02010). EDP Sciences. https://doi.org/10.1051/e3sconf/202130202010
Naqash, S. Y., & Nazeer, R. A. (2013). Antioxidant and functional properties of protein hydrolysates from pink perch (Nemipterus japonicus) muscle. Journal of Food Science and Technology, 50(5), 972-978. https://doi.org/10.1007/s13197-011-0416-y
Najafian, L. & Babji, A. S. (2012). A review of fish-derived antioxidant and antimicrobial peptides: their production, assessment, and applications. Peptides, 33, 178–185. https://doi.org/10.1016/j.peptides.2011.11.013
Nurhayati, T., & Nurjanah, C. H. S. (2014). Characterization of African catfish protein hydrolysate (Clarias gariepinus). Journal of Pengolah Hasil Perikan Indonesia, 16, 207-214
Odekanyin, O. O., Ayangbemi, A. O., & Jerome, A. J. (2019). Enzymatic production of Sarotherodon galilaeus muscle protein hydrolysates and assessment of its Alpha-amylase inhibitory and antioxidant potential. International Journal of Science, 8(11), 6-12. https://doi.org 10.18483/ijSci.2174
Ortizo, R. G. G., Sharma, V., Tsai, M. L., Wang, J. X., Sun, P. P., Nargotra, P., Kuo, C. H., Chen, C. W. & Dong, C. D., (2023). Extraction of novel bioactive peptides from fish protein hydrolysates by enzymatic reactions. Applied Sciences, 13(9), 5768. https://doi.org/10.3390/app13095768
Peñta‐Ramos, E. A., & Xiong, Y. L. (2002). Antioxidant activity of soy protein hydrolysates in a liposomal system. Journal of Food Science 67(8), 2952-2956. https://doi.org/10.1111/j.1365-2621.2002.tb08844.x
Prihanto, A. A., Nurdiani, R. & Sari, L. W. (2021). Production and characteristics of sailfin catfish (Pterygoplichthys pardalis) protein hydrolysate F1000Research, 10, 1089 https://doi.org/10.12688/f1000research.73335.1
Ramakrishnan, V. V., Hossain, A., Dave, D. & Shahidi, F. (2024). Salmon processing discards: a potential source of bioactive peptides – a review. Food Production, Processing and Nutrition, 6, 22-54. https://doi.org/10.1186/s43014-023-00197-2
Randriamahatody, Z., Randriamidosy, J. C., Mong, Y. J. M. & Razanamparany, J. L. (2022). Effects of two drying methods on the composition and functional properties of fish trimmings hydrolytic products. International Journal of Advanced Research and Innovative Ideas in Education, 8(6), 536-542.
Salami, S. A., Osukoya, O. A., Adewale, O. B., Odekanyin, O., Obafemi, T. O. & Kuku, A. (2023). Bioactivities of Garcinia kola enzymatic hydrolysates at different enzyme-substrate ratios. AMB Express, 13, 78 – 89. https://doi.org/10.1186/s13568-023-01583-2
Seniman, M. S., Yusop, S. M. & Babji, A. S. (2014). Production of enzymatic protein hydrolysates from freshwater catfish (Clarias batrachus). The 2014 UKM FST Postgraduate Colloquium. AIP Conference Proceedings, 1614, 323-328. https://doi.org/doi:10.10631/1.4895216.
Shahidi, F., Xiao-Quing, H. & Synowiecki, J. (1995). Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chemistry, 53, 285-293. https://doi.org/10.1016/0308-8146(95)93934-J
Srikanya, A., Dhanapal, K., Sravani, K., Madhavi, K., Yeshdas, B. & Kumar, P.G. (2018). Antioxidant and antimicrobial activity of protein hydrolysate prepared from tilapia fish waste by enzymatic treatment. International Journal of Current Microbiology and Applied Sciences, 7(10), 2891-2899. https://doi.org/10.20546/ijcmas.2018.710.336
Sukkhown, P., Jangchud, K., Lorjaroenphon, Y. & Pirak, T. (2018). Flavored-functional protein hydrolysates from enzymatic hydrolysis of dried squid by-products: Effect of drying method. Food Hydrocolloids, 76, 103-112. https://doi.org/10.1016/j.foodhyd.2017.01.026
Taheri, A., Anvar, S. A. A., Ahari, H. & Fogliano, V. (2013). Comparison the functional properties of protein Hydrolysates from poultry by-products and rainbow trout. Iranian Journal of Fisheries Sciences, 12(1), 154-169.
Tejpal, C. S., Vijayagopal, P., Elavarasan, K., Linga Prabu, D., Lekshmi, R. G. K., Asha, K. K., Anandan, R., Chatterjee, N. S. & Mathew, S. (2017). Antioxidant, functional properties, and amino acid composition of pepsin-derived protein hydrolysates from whole tilapia waste as influenced by pre-processing ice storage. Journal of Food Science and Technology, 54, 4257-4267. https://doi.org/10.1007/s13197-017-2897-9
Torres-Fuentes, C., Alaiz, M., & Vioque, J. (2012). Affinity purification and characterization of chelating peptides from chickpea protein hydrolysates. Food Chemistry. 129, 485–490. https://doi.org/10.1016/j.foodchem.2011.04.103
Viji, P., Phannendra, T. S., Jesmi, D., Madhusudana Rao, B., Dhiju Das, P. H., & George, N. (2019). Functional and Antioxidant Properties of Gelatin Hydrolysates Prepared from Skin and Scale of Sole Fish. Journal of Aquatic Food Product Technology, 28(10), 976–986. https://doi.org/10.1080/10498850.2019.1672845
Wang, L., Sun, J., Ding, S. & Qi, B. (2018). Isolation and identification of novel antioxidant and antimicrobial oligopeptides from enzymatically hydrolyzed anchovy fish meal. Process Biochemistry, 74, 148–55. https://doi.org/10.1016/j.procbio.2018.08.021
Zaky, A. A., Simal-Gandara, J., Eun, J. B., Shim, J. H. & Abd El-Aty, A. M. (2021). Bioactivities, Applications, Safety, and Health Benefits of Bioactive Peptides from Food and By-Products: A Review. Frontiers in Nutrition, 8, 815640. https://doi.org/10.3389/fnut.2021.815640.
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