IN SILICO ANALYSIS OF EDIBLE BIRD’S NEST PROTEINS AS POTENTIAL PRECURSORS FOR BIOACTIVE PEPTIDES
Keywords:ACE inhibitor, bioactve peptides, DPP-IV inhibitor, edible bird's nest, in silico
The present study aimed to perform an in silico evaluation of edible bird’s nest protein as potential precursors of bioactive peptides, as well as to determine whether such peptides can be released by selected proteolytic enzymes. Six edible bird’s nest (EBN) protein sequences from a previous study were chosen as potential precursors to produce bioactive peptides via in silico method using the BIOPEP database. AMCase protein sequences gave the highest number of bioactivities (16 to 18) and nucleobindin-2 protein gave the lowest number of bioactivities (9) among the other protein sequences. It was found that the most potential bioactive peptides from EBN proteins are angiotensin-converting enzyme (ACE) inhibitors and dipeptidyl peptidase-IV (DPPIV) inhibitors. Furthermore, in silico proteolysis using six selected enzymes was employed to release both dominant bioactivities in EBN proteins, which were ACE and DPP-IV inhibitors. This study shows that a combination of enzymes, chymotrypsin, and papain, produced the highest number of activities for both ACE and DPP-IV inhibitor peptides with the frequency of occurrence of bioactive peptides of 0.0968 and 0.1104, respectively. The toxic prediction tool, ToxinPred, found that all EBN peptides derived by in silico analysis were non-toxic. The current study proposed that EBN can serve as a potential source of bioactive peptides.
Agirbasli, Z. & Cavas, L. 2017. In silico evaluation of bioactive peptides from the green algae Caulerpa. Journal of Applied Phycology, 29(3): 1635-1646. DOI: https://doi.org/10.1007/s10811-016-1045-7
Aluko, R.E. 2017. Food protein-derived peptides: Production, isolation and purification. Proteins in Food Processing: Second Edition. 389-412. DOI: https://doi.org/10.1016/B978-0-08-100722-8.00016-4
Ambigaipalan, P., Al-Khalifa, A.S. & Shahidi, F. 2015. Antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using Alcalase, Flavourzyme and Thermolysin. Journal of Functional Foods, 18: 1125-1137. DOI: https://doi.org/10.1016/j.jff.2015.01.021
Amiza, M.A., Sai, J.Y. & Sarbon, N.M. 2014. Optimization of enzymatic hydrolysis conditions on angiotensin converting enzyme (ACE) inhibitory activity from edible bird’s nest. In: Proceedings of International Conference on Food Innovation 2014 (INNOVA2014). Penang. 27-28 August 2014.
BIOPEP. 2019. http://www.uwm.edu.pl/biochemia/index.php/pl/biopep/ (accessed 3.5.2019).
Bleakley, S., Hayes, M., O’ Shea, N., Gallagher, E. & Lafarga, T. 2017. Predicted release and analysis of novel ACE-I, renin, and DPP-IV inhibitory peptides from common oat (Avena sativa) protein hydrolysates using in silico analysis. Foods, 6(12): E108. DOI: https://doi.org/10.3390/foods6120108
Chen, H.M., Muramoto, K., Yamauchi, F., Fujimoto, K. & Nokihara, K. 1998. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. Journal of Agricultural and Food Chemistry, 46: 49-53. DOI: https://doi.org/10.1021/jf970649w
Cherkasov, A., Muratov, E.N., Fourches, D., Varnek, A., Baskin, I.I., Cronin, M., Dearden, J., Gramatica, P., Martin, Y.C., Todeschini, R., Consonni, V., Kuz’Min, V.E., Cramer, R., Benigni, R., Yang, C., Rathman, J., Terfloth, L., Gasteiger, J., Richard, A. & Tropsha, A. 2014. QSAR modeling: Where have you been? Where are you going to? Journal of Medicinal Chemistry, 57: 4977–5010. DOI: https://doi.org/10.1021/jm4004285
Fu, F., Young, J.F., Løkke, M.M., Lametsch, R., Aluko, R.E. & Therkildsen, M. 2016. Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions. Journal of Functional Foods, 24: 196-206. DOI: https://doi.org/10.1016/j.jff.2016.03.026
Gangopadhyay, N., Wynne, K., O’Connor, P., Gallagher, E., Brunton, N.P., Rai, D.K. & Hayes, M. 2016. In silico and in vitro analyses of the angiotensin-I converting enzyme inhibitory activity of hydrolysates generated from crude barley (Hordeum vulgare) protein concentrates. Food Chemistry, 203: 367-374. DOI: https://doi.org/10.1016/j.foodchem.2016.02.097
Garg, S., Apostolopoulos, V., Nurgali, K. & Mishra, V.K. 2018. Evaluation of in silico approach for prediction of presence of opioid peptides in wheat. Journal of Functional Foods, 41: 34-40. DOI: https://doi.org/10.1016/j.jff.2017.12.022
Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M.R., Appel, R.D. & Bairoch, A. 2005. Protein Identification and Analysis Tools on the ExPASy Server. (In) John M. Walker (Ed): The Proteomics Protocols Handbook, Humana Press. DOI: https://doi.org/10.1385/1-59259-890-0:571
Ghassem, M., Arihara, K., Mohammadi, S., Sani, N.A. & Babji, A.S. 2017. Identification of two novel antioxidant peptides from edible bird’s nest (Aerodramus fuciphagus) protein hydrolysates. Food Functions, 8(5): 2046-2052. DOI: https://doi.org/10.1039/C6FO01615D
Gupta, S., Kapoor, P., Chaudhary, K., Gautam, A., Kumar, R. & Raghava, G.P.S., 2013. In silico approach for predicting toxicity of peptides and proteins. PLoS One. 8. DOI: https://doi.org/10.1371/journal.pone.0073957
Hall, F., Johnson, P.E. & Liceaga, A., 2018. Effect of enzymatic hydrolysis on bioactive properties and allergenicity of cricket (Gryllodes sigillatus) protein. Food Chemistry. 262: 39-47. DOI: https://doi.org/10.1016/j.foodchem.2018.04.058
Hatanaka, T., Inoue, Y., Arima, J., Kumagai, Y., Usuki, H., Kawakami, K., Kimura, M., Mukaihara, T. 2012. Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran. Food Chemistry, 134(2): 797-802. DOI: https://doi.org/10.1016/j.foodchem.2012.02.183
Hildebrandt, M., Reutter, W., Arck, P., Rose, M. & Klapp, B.F. 2000. A guardian angel: the involvement of dipeptidyl peptidase IV in psychoneuroendocrine function, nutrition and immune defence. Clinical Science, 99: 93-104. DOI: https://doi.org/10.1042/cs0990093
Huang, S.L., Jao, C.L., Ho, K,P, Hsu, .K.C. 2012. Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates. Peptides, 35(1): 114-21. DOI: https://doi.org/10.1016/j.peptides.2012.03.006
International Diabetes Federation. 2017. IDF Diabetes Atlas (8th ed.), International Diabetes Federation, Brussels, Belgium.
Iwaniak, A., Dziuba, J. & Niklewicz, M., 2005. The BIOPEP database - a tool for the in silico method of classification of food proteins as the
source of peptides with antihypertensive activity. Acta Alimentaria, 34: 417-425.
Klompong, V., Benjakul, S., Kantachote, D. & Shahidi, F. 2007. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chemistry, 102: 1317-1327. DOI: https://doi.org/10.1016/j.foodchem.2006.07.016
Korhonen, H. & Pihlanto, A. 2006. Bioactive peptides: production and functionality. International Dairy Journal, 16: 945-960. DOI: https://doi.org/10.1016/j.idairyj.2005.10.012
Lacroix, I.M.E. & Li-chan, E.C.Y., 2012. Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase ( DPP )-IV inhibitors by an in silico approach. Journal of Functional Foods, 4: 403-422. DOI: https://doi.org/10.1016/j.jff.2012.01.008
Lafarga, T., Connor, P.O. & Hayes, M., 2014. Peptides Identification of novel dipeptidyl peptidaseIV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. Peptides, 59: 53-62. DOI: https://doi.org/10.1016/j.peptides.2014.07.005
Lee, S. & Hur, S. 2017. Antihypertensive peptides from animal products, marine organisms, and plants. Food Chemistry, 228: 506-517. DOI: https://doi.org/10.1016/j.foodchem.2017.02.039
Lin, K., Zhang, L-W., Han, X., Xin, L., Meng, Z-X., Gong, P-M. & Cheng, D-Y. 2018. Yak milk casein as potential precursor of angiotensin I-converting enzyme inhibitory peptides based on in silico proteolysis. Food Chemistry, 254: 340-347. DOI: https://doi.org/10.1016/j.foodchem.2018.02.051
Liu, M., Wang, Y., Liu, Y. & Ruan, R. 2016. Bioactive peptides derived from traditional Chinese medicine and traditional Chinese food : A review. Food Research International, 89(1): 63-73. DOI: https://doi.org/10.1016/j.foodres.2016.08.009
Liu, R., Cheng, J., & Wu, H. 2019. Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review. International Journal of Molecular Sciences, 20(3): 463. DOI: https://doi.org/10.3390/ijms20030463
Marciniak, A., Suwal, S., Naderi, N., Pouliot, Y., Doyen, A. 2018. Enhancing enzymatic hydrolysis of food proteins and production of bioactive peptides using high hydrostatic pressure technology. Trends in Food Science and Technolology, 80: 187-198. DOI: https://doi.org/10.1016/j.tifs.2018.08.013
Marcone. M.F. 2005. Characterization of the edible bird’s nest the “Caviar of the East”. Food Research International, 38(10): 1125-1134. DOI: https://doi.org/10.1016/j.foodres.2005.02.008
Minkiewicz, P., Dziuba, J., Iwaniak, A., Dziuba, M. & Darewicz, M. 2008. BIOPEP database and other programs for processing bioactive peptide sequences, Journal of AOAC International, 91(4): 965–980. DOI: https://doi.org/10.1093/jaoac/91.4.965
Nur ’Aliah, Ghassem, M., See S.F. & Salam Babji, A., 2016. Functional bioactive compounds from freshwater fish, edible birdnest, marine seaweed and phytochemical. American Journal of Food and Nutrition, 6: 33-38.
Quek, M.C., Chin, N.L., Yusof, Y.A., Law, C.L. & Tan, S.W. 2018. Characterization of edible bird’s nest of different production, species and geographical origins using nutritional composition, physicochemical properties and antioxidant activities. Food Research International, 109: 35–43. DOI: https://doi.org/10.1016/j.foodres.2018.03.078
Saengkrajang, W., Matan, N. & Matan, N. 2013. Nutritional composition of the farmed edible bird’s nest (Collocalia fuciphaga) in Thailand. Journal of Food Composition and Analysis, 31(1): 41-45. DOI: https://doi.org/10.1016/j.jfca.2013.05.001
Shahidi, F. & Zhong, Y. 2008. Bioactive Peptides. Journal of AOAC International, 91: 914-931. DOI: https://doi.org/10.1093/jaoac/91.4.914
Sila, A., Alvarez, O.M., Haddar, A., Frikha, F., Dhulster, P., Nedjar-Arroume, N. & Bougatef, A. 2016. Purification, identification and structural modelling of DPP-IV inhibiting peptides from barbel protein hydrolysate. Journal of Chromatography B, 1008: 260-269. DOI: https://doi.org/10.1016/j.jchromb.2015.11.054
Tu, M., Cheng, S., Lu, W. & Du, M. 2018. Advancement and prospects of bioinformatics analysis for studying bioactive peptides from food-derived protein: Sequence, structure, and functions. Trends in Analytical Chemistry, 105: 7–17. DOI: https://doi.org/10.1016/j.trac.2018.04.005
Udenigwe, C.C. & Fogliano, V. 2017. Food matrix interaction and bioavailability of bioactive peptides : Two faces of the same coin ? Journal of Functional Foods, 35: 9–12. DOI: https://doi.org/10.1016/j.jff.2017.05.029
Wong, Z.C.F., Chan, G.K.L., Wu, L., Lam, H.H.N., Yao, P., Dong, T.T.X. & Tsim, K.W.K. 2018. A comprehensive proteomics study on edible bird’s nest using new monoclonal antibody approach and application in quality control. Journal of Food Composition and Analysis, 31: 41–45. DOI: https://doi.org/10.1016/j.jfca.2017.12.014
Zheng, Z., Luo, J., Zuo, F., Zhang, Y., Ma, H. & Chen, S. 2016. Screening for potential novel probiotic Lactobacillus strains based on high dipeptidyl peptidase IV and α-glucosidase inhibitory activity. Journal of Functional Foods, 20: 486-495. DOI: https://doi.org/10.1016/j.jff.2015.11.030
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