Peptidomics of Peptic Digest of Selected Potato Tuber Proteins: Post-Translational Modifications and Limited Cleavage Specificity

Journal of Agricultural and Food Chemistry

Volumn 64, Issue 11, 2016, Pages 2432-2437

  Rajendran, Subin R C K ^a   Mason, Beth ^b   Udenigwe, Chibuike C ^a  

^a DALHOUSIE UNIVERSITY   (Canada)

^b CAPE BRETON UNIVERSITY   (Canada)

Author keywords

bioactive peptides; bioinformatics; in silico; peptidomics; post translational modifications; potato proteins

Indexed keywords

BIOINFORMATICS; FORECASTING; HYDROLYSIS; POLYPEPTIDES;

BIOACTIVE PEPTIDES; BIOINFORMATICS TOOLS; IN-SILICO; PEPTIDOMICS; POST-TRANSLATIONAL MODIFICATIONS; POTATO PROTEIN ISOLATES; PROCESSING CONDITION; STRUCTURAL MODIFICATIONS;

PEPTIDES;

PEPSIN A; PEPTIDE; PLANT PROTEIN;

ANALYSIS; CHEMISTRY; DIETARY SUPPLEMENT; DIGESTION; FUNCTIONAL FOOD; METABOLISM; PLANT TUBER; POTATO; PROTEIN PROCESSING;

DIETARY SUPPLEMENTS; DIGESTION; FUNCTIONAL FOOD; PEPSIN A; PEPTIDES; PLANT PROTEINS; PLANT TUBERS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SOLANUM TUBEROSUM;

EID: 84961943250     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/acs.jafc.6b00418     Document Type: Article

References (29)

1. Korhonen, H.; Pihlanto, A. Bioactive peptides: Production and functionality Int. Dairy J. 2006, 16, 945-960 10.1016/j.idairyj.2005.10.012
2. Udenigwe, C. C.; Aluko, R. E. Food protein-derived bioactive peptides: Production, processing, and potential health benefits J. Food Sci. 2012, 77, R11-R24 10.1111/j.1750-3841.2011.02455.x
3. Nagpal, R.; Behare, P.; Rana, R.; Kumar, A.; Kumar, M.; Arora, S.; Morotta, F.; Jain, S.; Yadav, H. Bioactive peptides derived from milk proteins and their health beneficial potentials: an update Food Funct. 2011, 2, 18-27 10.1039/C0FO00016G
4. Hubbell, J. Bioactive biomaterials Curr. Opin. Biotechnol. 1999, 10, 123-129 10.1016/S0958-1669(99)80021-4
5. Das, A. K.; Collins, R.; Ulijn, R. V. Exploiting enzymatic (reversed) hydrolysis in directed self-assembly of peptide nanostructures Small 2008, 4, 279-287 10.1002/smll.200700889
6. Yoshikawa, M. Bioactive peptides derived from natural proteins with respect to diversity of their receptors and physiological effects Peptides 2015, 72, 208-225 10.1016/j.peptides.2015.07.013
7. Guang, C.; Phillips, R. D. Plant food-derived angiotensin I converting enzyme inhibitory peptides J. Agric. Food Chem. 2009, 57, 5113-5120 10.1021/jf900494d
8. Sharma, J.; Yadav, D.; Paliwal, S. Discovery of novel DPP IV inhibitors: application of pharmacophore-based virtual screening Med. Chem. Res. 2013, 22, 558-572 10.1007/s00044-012-0044-8
9. Minkiewicz, P.; Dziuba, J.; Iwaniak, A.; Dziuba, M.; Darewicz, M. BIOPEP database and other programs for processing bioactive peptide sequences J. AOAC Int. 2008, 91, 965-980
10. Nongonierma, A. B.; FitzGerald, R. J. An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides Food Chem. 2014, 165, 489-498 10.1016/j.foodchem.2014.05.090
11. Udenigwe, C. C. Towards rice bran protein utilization: In silico insight on the role of oryzacystatins in biologically-active peptide production Food Chem. 2016, 191, 135-138 10.1016/j.foodchem.2015.01.043
12. Gasteiger, E.; Hoogland, C.; Gattiker, A.; Duvaud, S.; Wilkins, M. R.; Appel, R. D.; Bairoch, A. Protein identification and analysis tools on the ExPASy server. In The Proteomics Protocols Handbook; Walker, J. M., Ed.; Humana Press: Totowa, NJ, 2005; pp 571-607.
13. Mooney, C.; Haslam, N. J.; Pollastri, G.; Shields, D. C. Towards the improved discovery and design of functional peptides: common features of diverse classes permit generalized prediction of bioactivity PLoS One 2012, 7, e45012 10.1371/journal.pone.0045012
14. Mohan, A.; Udechukwu, M. C.; Rajendran, S. R. C. K.; Udenigwe, C. C. Modification of peptide functionality during enzymatic hydrolysis of whey proteins RSC Adv. 2015, 5, 97400-97407 10.1039/C5RA15140F
15. Udenigwe, C. C.; Udechukwu, M. C.; Yiridoe, C.; Gibson, A.; Gong, M. Antioxidant mechanism of potato protein hydrolysates against in vitro oxidation of reduced glutathione J. Funct. Foods 2016, 20, 195-203 10.1016/j.jff.2015.11.004
16. Han, X.; He, L.; Xin, L.; Shan, B.; Ma, B. PeaksPTM: Mass spectrometry-based identification of peptides with unspecified modifications J. Proteome Res. 2011, 10, 2930-2936 10.1021/pr200153k
17. Broeckx, V.; Boonen, K.; Pringels, L.; Sagaert, X.; Prenen, H.; Landuyt, B.; Schoofs, L.; Maes, E. Comparison of multiple protein extraction buffers for GeLC-MS/MS proteomic analysis of liver and colon formalin-fixed, paraffin-embedded tissues Mol. BioSyst. 2016, 12, 553-565 10.1039/C5MB00670H
18. Beausoleil, S. A.; Villén, J.; Gerber, S. A.; Rush, J.; Gygi, S. P. A probability-based approach for high-throughput protein phosphorylation analysis and site localization Nat. Biotechnol. 2006, 24, 1285-1292 10.1038/nbt1240
19. Biasini, M.; Bienert, S.; Waterhouse, A.; Arnold, K.; Studer, G.; Schmidt, T.; Kiefer, F.; Cassarino, T. G.; Bertoni, M.; Bordoli, L. et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information Nucleic Acids Res. 2014, 42, W252-W258 10.1093/nar/gku340
20. Stupar, R. M.; Beaubien, K. A.; Jin, W.; Song, J.; Lee, M.-K.; Wu, C.; Zhang, H.-B.; Han, B.; Jiang, J. Structural diversity and differential transcription of the patatin multicopy gene family during potato tuber development Genetics 2006, 172, 1263-1275 10.1534/genetics.105.051219
21. Stadtman, E. R.; Moskovitz, J.; Levine, R. L. Oxidation of methionine residues of proteins: biological consequences Antioxid. Redox Signaling 2003, 5, 577-582 10.1089/152308603770310239
22. Schöneich, C. Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease Biochim. Biophys. Acta, Proteins Proteomics 2005, 1703, 111-119 10.1016/j.bbapap.2004.09.009
23. Hamada, J. S.; Swanson, B. Deamidation of food proteins to improve functionality Crit. Rev. Food Sci. Nutr. 1994, 34, 283-292 10.1080/10408399409527664
24. Cuq, J. L.; Provansal, M.; Guilleux, F.; Cheftel, C. Oxidation of methionine residues of casein by hydrogen peroxide. Effects on in vitro digestibility J. Food Sci. 1973, 38, 11-13 10.1111/j.1365-2621.1973.tb02763.x
25. Jacques, S.; Ghesquière, B.; De Bock, P.-J.; Demol, H.; Wahni, K.; Willems, P.; Messens, J.; Van Breusegem, F.; Gevaert, K. Protein methionine sulfoxide dynamics in Arabidopsis thaliana under oxidative stress Mol. Cell. Proteomics 2015, 14, 1217-1229 10.1074/mcp.M114.043729
26. Walsh, G.; Jefferis, R. Post-translational modifications in the context of therapeutic proteins Nat. Biotechnol. 2006, 24, 1241-1252 10.1038/nbt1252
27. Udenigwe, C. C. Bioinformatics approaches, prospects and challenges of food bioactive peptide research Trends Food Sci. Technol. 2014, 36, 137-143 10.1016/j.tifs.2014.02.004
28. Udenigwe, C. C.; Gong, M.; Wu, S. In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides Process Biochem. 2013, 48, 1794-1799 10.1016/j.procbio.2013.08.013
29. Fu, Y.; Wu, W.; Zhu, M.; Xiao, Z. In silico assessment of the potential of patatin as a precursor of bioactive peptides J. Food Biochem. 2015, 10.1111/jfbc.12213