Journals / Mediterranean Fisheries and Aquaculture Research / 2023 / Cilt: 6 Sayı: 1

Biochemical and Antimicrobial Properties of Alburnus tarichi Roe Protein Hydrolysate

Pages
26–36
Publication Date
2023-06-30
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

The results demonstrated the importance of amino acid composition in determin-ing the bioactive potential of the peptides.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:The protein hydrolysates with antioxidant and antimicrobial potential have become a theme of great interest for pharmaceutical, nutraceuticals, as well as food processing and preservation indus-tries.
📊
Key Findings & Data:On the other hand, chemical composition of fish protein hydrolysates is significant in nutri-tion perspective of human health.
💡
Conclusion & Impact:The results demonstrated the importance of amino acid composition in determin-ing the bioactive potential of the peptides.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Alburnus tarichi · Roe protein · Protein hydrolysate

Abstract

The protein hydrolysates with antioxidant and antimicrobial potential have become a theme of great interest for pharmaceutical, nutraceuticals, as well as food processing and preservation indus-tries. On the other hand, chemical composition of fish protein hydrolysates is significant in nutri-tion perspective of human health. Hence, in the present study proximate and amino acid composi-tions, antioxidant and antimicrobial activities of Alburnus tarichi roe protein hydrolysate was esti-mated. Protein, lipid, moisture, and ash content were found to be 87.24±0.1, 0.72±0.04, 8.79±0.3, and 7.01±0.09%, respectively. Glutamic acid, aspartic acid, lysine, leucine and alanine were found to be the most dominant amino acids, whereas, cysteine was found to be the lowest amino acid in roe protein hydrolysate. The IC50 value of roe protein hydrolysate for DPPH radical and hydroxyl-radical scavenging activities were 54.33 μg/mL and 77.02 μg/mL, respectively. The reducing power of A. tarichi roe protein hydrolysate was analyzed, the optical density values of roe protein hydroly-sate and gallic acid at 700 nm were 0.45±0.03 and 1.14±0.09, respectively. Roe protein hydrolysate had shown maximum zone of inhibition against Klebsiella pneumoniae (11.1±0.30 mm) followed by Salmonella enterica (10.7±0.46 mm), Proteus mirabilis (10.1±0.35 mm) and Candida albicans (8.7±0.34 mm). The results demonstrated the importance of amino acid composition in determin-ing the bioactive potential of the peptides. The results showed that roe protein hydrolysates of A. tarichi was proved to show good effect on antioxidant and antimicrobial activities and can be used a source for nutraceuticals and pharmaceuticals.

🔖

Cite This Article

BERKÖZ, M., YUNUSOĞLU, O., YILMAZ, F. Ö., HUNT, A. Ö., YALIN, S., TÜRKMEN, Ö. (2023). Biochemical and Antimicrobial Properties of Alburnus tarichi Roe Protein Hydrolysate. Mediterranean Fisheries and Aquaculture Research, Cilt: 6 Sayı: 1, 26–36. https://ajindex.com/articles/952681

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (10)

  1. Alboofetileh, M., Hamzeh, A., Abdollahi, M. (2021) Seaweed proteins as a source of bioactive peptides. Current Pharmaceutical Design 27: 1342–1352.
  2. Baker, D.H., Han, Y. (1994) Ideal amino acid profile for broiler chicks during three weeks post hatching. Poultry Science 73: 1441-1447.
  3. Bligh, E.G., Dyer, W.J. (1959) A rapid method of total lipid extraction and purification. Canadian Journal of Biochemistry and Physiology 37: 911-917.
  4. Borges, S., Odila, J., Voss, G., Martins, R., Rosa, A., Couto, J.A., Almeida, A., Pintado, M. (2023) Fish by-products: A source of enzymes to generate circular bioactive hydrolysates. Molecules (Basel) 28: 1155. Bueno-Solano, C., Lopez-Cervantes, J., Campas-Baypoli, O. N., Lauterio-Garcia, R., Adan-Bante, N.P., Sanchez-Machado, D.I. (2009) Chemical and biological characteristics of protein hydrolysates from fermented shrimp by-products Food Chemistry 112: 671-675.
  5. Chakniramol, S., Wierschem, A., Cho, M.G., Bashir, K.M.I. (2022) Physiological and clinical aspects of bioactive peptides from marine animals. Antioxidants (Basel) 11: 1021. Chalamaiah, M., Dinesh-Kumar, B., Hemalatha, R., Jyothirmayi, T. (2012) Fish protein hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: a review. Food Chemistry 135: 3020-3038.
  6. Choi, Y.J., Hur, S., Choi, B.D., Konno, K., Park, J.W. (2009) Enzymatic hydrolysis of recovered protein from frozen small croaker and functional properties of its hydrolysates. Journal of Food Science 74: 17-24.
  7. Dong, Y., Sheng, G., Fu, J., Wen, K. (2005) Chemical characterization and anti-anaemia activity of fish protein hydrolysate from Saurida elongate. Journal of the Science of Food and Agriculture 85: 2033-2039.
  8. Foh, M.B.K., Kamara, M.T., Amadou, I., Foh, B.M., Wenshui, X. (2011) Chemical and physiochemical properties of Tilapia (Oreochromis niloticus) fish protein hydrolysates and concentrate. International Journal of Biological Chemistry 5: 21-36.
  9. Folch, J., Lees, M., Sloane-Stanley, G.H. (1956) A simple method for the isolation and purification of total lipids from animal tissues. Journal of Biological Chemistry 226: 497-509.
  10. Ghassem, M., Fern, S.S., Said, M., Ali, Z.M., Ibrahim, S., Babji, A.S. (2014) Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates. Journal of Food Science and Technology 51: 467-475. González-Serrano, D.J., Hadidi, M., Varcheh, M., Jelyani, A.Z., Moreno, A., Lorenzo, J.M. (2022) Bioactive peptide