By-products of the whelk processing industry as valuable source of bioactive peptides
DOI:
https://doi.org/10.17501/26510251.2021.1103Keywords:
Shellfish, Bioactive peptides, Protein extraction, Protein hydrolysates, Waste management, Nutraceuticals, AntioxidantsAbstract
The fish and shellfish industry processes 851,984 tonnes of fish per year worldwide. However, only 43% of that is consumed, and valuable proteins that are going to waste. Protein hydrolysates are widely used in food technology for their nutritional and functional properties. The goal of this project is to extract protein from the shellfish processing industry by-products and create protein hydrolysates that have marketable value. The waste was divided into two types: raw waste (R) and cooked waste (C). The proteins were extracted using the pH shift method at acid (A), neutral (N) and basic (B) pH, they were then quantified using the Bradford assay, for which R had the highest protein yield. Proteins were also qualified using reverse phase high-performance liquid chromatography (RP-HPLC) that showed that R has more hydrophilic proteins while the C protein showed more peaks in the hydrophobic phase. The Fourier-transform infrared spectroscopy (FTIR) indicated the presence of glutamine, tyrosine and serine in the extracted proteins. Extracted proteins were then hydrolyzed using Alcalase and α-Chymotrypsin and the degree of hydrolysis measured with a 2,4,6-Trinitrobenzene Sulfonic Acid (TNBS) assay. It was possible to obtain higher degrees of hydrolysis (DH) of using Alcalase. The hydrolysates were tested for antioxidant activity using the DPPH (2,2-diphenyl-1-picryl-hydrazyl-hydrate) free radical antioxidant assay. Alcalase hydrolysates showed to have an IC50 for the DPPH assay of 33.79±2.96 µg/mL, 13.92±1.57 µg/mL and 36.09±3.04 µg/mL, and α-Chymotrypsin hydrolysates 43.24±2.11 µg/mL, 81.18±4.07 µg/mL and 56.02±2.29 µg/mL for A, N and B protein, respectively. The IC50 results obtained are significantly lower than the ones described in other studies using the same enzymes or other marine species. This can indicate that more heterogenous mixtures of by-product can originate extracted proteins that when hydrolyzed lead to higher radical scavenging activity.
Downloads
References
Barber, S. C., Mead, R. J., & Shaw, P. J. (2006). Oxidative stress in ALS: a mechanism of neurodegeneration and a therapeutic target. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1762(11-12), 1051-1067. Barth, A. (2007). Infrared spectroscopy of proteins. In Biochimica et Biophysica Acta - Bioenergetics (Vol. 1767, Issue 9, pp. 1073–1101). https://doi.org/10.1016/j.bbadis.2006.03.008
Bordbar, S., Ebrahimpour, A., Zarei, M., Abdul Hamid, A., & Saari, N. (2018). Alcalase-generated proteolysates of stone fish (Actinopyga lecanora) flesh as a new source of antioxidant peptides. International Journal of Food Properties (Vol 21, Issue 1, pp. 1541-1559). https://doi.org/10.1080/10942912.2018.1497060
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry, (Vol. 72; Issue 1-2, pp. 248-254). https://doi.org/10.1006/abio.1976.9999
Christen, Y. (2000). Oxidative stress and Alzheimer disease. The American Journal of Clinical Nutrition, (Vol 71, Issue 2, pp. 621S-629S). https://doi.org/10.1093/ajcn/71.2.621s
Corbett, C. M. (2010). The mystery of the whelk egg capsule protein: electrospinning, mechanical testing, and being outsmarted by an invertebrate (Doctoral dissertation, University of British Columbia). Retrieved from https://open.library.ubc.ca/collections/ubctheses/24/items/1.0071163
Ding, J. F., Li, Y. Y., Xu, J. J., Su, X. R., Gao, X., & Yue, F. P. (2011). Study on effect of jellyfish collagen hydrolysate on anti-fatigue and anti-oxidation. Food Hydrocolloids, (Vol 25, Issue 5, pp.1350–1353). https://doi.org/10.1016/j.foodhyd.2010.12.013
Dumandan, N. G., Angelica, M. R. N., Belina-Aldemita, M. D., & Torio, M. A. O. (2014). Extraction and characterization of bioactive peptides derived from the hydrolysates of total soluble proteins of pistachio nuts (Pistacia vera L.). Kimika, (Vol 25, Issue 1, pp. 1-10). https://doi.org/10.26534/kimika.v25i1.1-10
Garcia-Garcia, G., Stone, J., & Rahimifard, S. (2019). Opportunities for waste valorisation in the food industry–A case study with four UK food manufacturers. Journal of Cleaner Production, (Vol 211, pp. 1339-1356). https://doi.org/10.1016/j.jclepro.2018.11.269
Harnedy, P. A., & FitzGerald, R. J. (2012). Bioactive peptides from marine processing waste and shellfish: A review. In Journal of Functional Foods (Vol. 4, Issue 1, pp. 6–24). https://doi.org/10.1016/j.jff.2011.09.001
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, (Vol 1, Issue 3, pp. 30-36). https://doi.org/10.12691/jfnr-1-3-3
Hoque, M. Z., Nurul Alam, M., & Nahid, K. A. (2018). Health consciousness and its effect on perceived knowledge, and belief in the purchase intent of liquid milk: Consumer insights from an emerging market. Foods, (Vol 7, Issue 9). https://doi.org/10.3390/foods7090150
Huang, G. R., Zhao, J., & Jiang, J. X. (2011). Effect of defatting and enzyme type on antioxidative activity of shrimp processing byproducts hydrolysate. Food Science and Biotechnology, (Vol 20, Issue 3, pp. 651-657). https://doi.org/10.1007/s10068-011-0092-8
Hynes, S., & Hennessy, T. (2012). Agriculture, fisheries and food in the Irish economy. The World Economy, (Vol 35, Issue 10, pp. 1340-1358). https://doi.org/10.1111/j.1467-9701.2012.01487.x
Kim, S. K., & Wijesekara, I. (2010). Development and biological activities of marine-derived bioactive peptides: A review. In Journal of Functional Foods (Vol. 2, Issue 1, pp. 1–9). https://doi.org/10.1016/j.jff.2010.01.003
Kim, S. M. (2011). Antioxidant and anticancer activities of enzymatic hydrolysates of solitary tunicate (Styela clava). Food Science and Biotechnology, (Vol 20, Issue 4, pp. 1075). https://doi.org/10.1007/s10068-011-0146-y
Kumar, A., & Venkatesu, P. (2012). Overview of the stability of α-chymotrypsin in different solvent media. Chemical Reviews, (Vol 112, Issue 7, pp. 4283-4307).
https://doi.org/10.1021/cr2003773
Mack, D., Huntington, T., Curr, C., & Joensen, J. (2004). Evaluation of fish waste management techniques. Report to the Scottish Environment Protection Agency. Poseidon Aquatic Resource Management Ltd, Lymington, Hampshire. Retrieved from: https://sedsh.gov.uk/Publications/2005/03/20717/52860
Murillo, W. (2017). Antioxidant potential use of bioactive peptides derived from mung bean hydrolysates (Vigna Radiata). African Journal of Food Science, (Vol 11, Issue 3, pp. 67-73). https://doi.org/10.5897/AJFS2016.1511
Neves, A. C., Harnedy, P. A., & FitzGerald, R. J. (2016). Angiotensin Converting Enzyme and Dipeptidyl Peptidase-IV Inhibitory, and Antioxidant Activities of a Blue Mussel (Mytilus edulis) Meat Protein Extract and Its Hydrolysates. Journal of Aquatic Food Product Technology, (Vol 25, Issue 8, pp.1221–1233). https://doi.org/10.1080/10498850.2015.1051259
Neves, A. C., Harnedy, P. A., O’Keeffe, M. B., Alashi, M. A., Aluko, R. E., & FitzGerald, R. J. (2017). Peptide identification in a salmon gelatin hydrolysate with antihypertensive, dipeptidyl peptidase IV inhibitory and antioxidant activities. Food Research International, (Vol 100, pp. 112–120). https://doi.org/10.1016/j.foodres.2017.06.065
Ngo, D. H., Qian, Z. J., Ryu, B., Park, J. W., & Kim, S. K. (2010). In vitro antioxidant activity of a peptide isolated from Nile tilapia (Oreochromis niloticus) scale gelatin in free radical-mediated oxidative systems. Journal of Functional Foods, (Vol 2, Isue 2, pp. 107-117). https://doi.org/10.1016/j.jff.2010.02.001
Nunomura, A., Castellani, R. J., Zhu, X., Moreira, P. I., Perry, G., & Smith, M. A. (2006). Involvement of oxidative stress in Alzheimer disease. Journal of neuropathology & experimental neurology, (Vol 65, Issue 7, pp. 631-641). 10.1097/01.jnen.0000228136.58062.bf
Ramakrishna, V., & Jailkhani, R. (2007). Evaluation of oxidative stress in Insulin Dependent Diabetes Mellitus (IDDM) patients. Diagnostic pathology, (Vol 2, Issue 1, pp. 1-6).
https://doi.org/10.1186/1746-1596-2-22
Reeve, E., Albalat, A., Neil, D. M., & Smith, P. (2010). Utilization of shellfish processing waste as bait for whelk (Buccinum undatum) fishing. Retrieved from: http://eprints.gla.ac.uk/81404/
Sashidhar, R. B., Capoor, A. K., & Ramana, D. (1994). Quantitation of ϵ-amino group using amino acids as reference standards by trinitrobenzene sulfonic acid: A simple spectrophotometric method for the estimation of hapten to carrier protein ratio. Journal of immunological methods, (Vol 167, Issue 1-2, pp. 121-127). https://doi.org/10.1016/0022-1759(94)90081-7
Sbroggio, M. F., Montilha, M. S., Figueiredo, V. R. G. de, Georgetti, S. R., & Kurozawa, L. E. (2016). Influence of the degree of hydrolysis and type of enzyme on antioxidant activity of okara protein hydrolysates. Food Science and Technology, (Vol 36, Issue 2, pp. 375–381). http://dx.doi.org/10.1590/1678-457X.000216
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007). Free radicals and antioxidants in normal physiological functions and human disease. In International Journal of Biochemistry and Cell Biology (Vol. 39, Issue 1, pp. 44–84). https://doi.org/10.1016/j.biocel.2006.07.001
Vareltzis, P. K., & Undeland, I. (2012). Protein isolation from blue mussels (Mytilus edulis) using an acid and alkaline solubilisation technique-process characteristics and functionality of the isolates. Journal of the Science of Food and Agriculture, (Vol 92, Issue 15, pp. 3055–3064). https://doi.org/10.1002/jsfa.5723
Vertuani, S., Angusti, A., & Manfredini, S. (2004). The antioxidants and pro-antioxidants network: an overview. Current pharmaceutical design, (Vol 10, Issue 14, pp. 1677-1694). https://doi.org/10.2174/1381612043384655
Villa, A. L. V., Aragão, M. R. S., Dos Santos, E. P., Mazotto, A. M., Zingali, R. B., De Souza, E. P., & Vermelho, A. B. (2013). Feather keratin hydrolysates obtained from microbial keratinases: effect on hair fiber. Bmc Biotechnology, (Vol 13, Issue 1, pp. 1-11). https://doi.org/10.1186/1472-6750-13-15
Wan, M. Y., Dong, G., Yang, B. Q., & Feng, H. (2016). Identification and characterization of a novel antioxidant peptide from feather keratin hydrolysate. Biotechnology Letters, (Vol 38, Issue 4, pp. 643–649). https://doi.org/10.1007/s10529-015-2016-9
Wood-Kaczmar, A., Gandhi, S., & Wood, N. W. (2006). Understanding the molecular causes of Parkinson’s disease. In Trends in Molecular Medicine (Vol. 12, Issue 11, pp. 521–528). https://doi.org/10.1016/j.molmed.2006.09.007
Wruck, C. J., Fragoulis, A., Gurzynski, A., Brandenburg, L. O., Kan, Y. W., Chan, K., Hassenpflug, J., Freitag-Wolf, S., Varoga, D., Lippross, S., & Pufe, T. (2011). Role of oxidative stress in rheumatoid arthritis: Insights from the Nrf2-knockout mice. Annals of the Rheumatic Diseases, (Vol 70, Issue 5, pp. 844–850). https://doi.org/10.1136/ard.2010.132720
Downloads
Published
How to Cite
Issue
Section
License
This work is licensed under a Creative Commons Attribution 4.0 International License.
