Omics-prediction of bioactive peptides from the edible cyanobacterium Arthrospira platensis proteome

Journal of the Science of Food and Agriculture

Volumn 98, Issue 3, 2018, Pages 984-990

  Ji, Chaofan ^a   Han, Jing ^a   Zhang, Jingbo ^a   Hu, Jing ^a   Fu, Yinghuan ^a   Qi, Hang ^a   Sun, Yue ^a   Yu, Chenxu ^a,b  

^a DALIAN POLYTECHNIC UNIVERSITY   (China)

^b Iowa State University   (United States)

Author keywords

Arthrospira platensis; edible cyanobacterium; in silico; peptides; proteome

Indexed keywords

BACTERIAL PROTEIN; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; DIPEPTIDYL PEPTIDASE IV INHIBITOR; PEPTIDE; PROTEOME;

AMINO ACID SEQUENCE; BIOLOGY; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; SPIRULINA;

AMINO ACID SEQUENCE; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; BACTERIAL PROTEINS; COMPUTATIONAL BIOLOGY; DIPEPTIDYL-PEPTIDASE IV INHIBITORS; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEOME; SPIRULINA;

EID: 85040258569     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.8546     Document Type: Article

References (27)

1. Li-Chan EC, Bioactive peptides and protein hydrolysates: research trends and challenges for application as nutraceuticals and functional food ingredients. Curr Opin Food Sci 1:28–37 (2015).
2. Ibañez E and Cifuentes A, Benefits of using algae as natural sources of functional ingredients. J Sci Food Agric 93:703–709 (2013).
3. Shahidi F and Ambigaipalan P, Novel functional food ingredients from marine sources. Curr Opin Food Sci 2:123–129 (2015).
4. Sheih IC, Fang TJ, Wu TK and Lin PH, Anticancer and antioxidant activities of the peptide fraction from algae protein waste. J Agric Food Chem 58:1202–1207 (2010).
5. Vo TS, Ryu B and Kim SK, Purification of novel anti-inflammatory peptides from enzymatic hydrolysate of the edible microalgal Spirulina maxima. J Funct Foods 5:1336–1346 (2013).
6. Samarakoon KW, O-Nam K, Ko JY, Lee JH, Kang MC, Kim D et al., Purification and identification of novel angiotensin-I converting enzyme (ACE) inhibitory peptides from cultured marine microalgae (Nannochloropsis oculata) protein hydrolysate. J Appl Phycol 25:1595–1606 (2013).
7. Udenigwe CC, Bioinformatics approaches, prospects and challenges of food bioactive peptide research. Trends Food Sci Technol 36:137–143 (2014).
8. Saavedra L, Hebert EM, Minahk C and Ferranti P, An overview of ‘omic’ analytical methods applied in bioactive peptide studies. Food Res Int 54:925–934 (2013).
9. Minkiewicz P, Dziuba J, Iwaniak A, Dziuba M and Darewicz M, BIOPEP database and other programs for processing bioactive peptide sequences. J AOAC Int 91:965–980 (2008).
10. Je JY, Cho YS, Gong M and Udenigwe CC, Dipeptide Phe-Cys derived from in silico thermolysin-hydrolysed RuBisCO large subunit suppresses oxidative stress in cultured human hepatocytes. Food Chem 171:287–291 (2015).
11. Lafarga T, O'Connor P and Hayes M, In silico methods to identify meat-derived prolyl endopeptidase inhibitors. Food Chem 175:337–343 (2015).
12. Chang YW and Alli I, In silico assessment: suggested homology of chickpea (Cicer arietinum L.) legumin and prediction of ACE-inhibitory peptides from chickpea proteins using BLAST and BIOPEP analyses. Food Res Int 49:477–486 (2012).
13. Udenigwe CC and Howard A, Meat proteome as source of functional biopeptides. Food Res Int 54:1021–1032 (2013).
14. Jamers A, Blust R and Coen DW, Omics in algae: paving the way for a systems biological understanding of algal stress phenomena? Aquat Toxicol 92:114–121 (2009).
15. Plaza M, Herrero M, Cifuentes A and Ibáñez E, Innovative natural functional ingredients from microalgae. J Agric Food Chem 57:7159–7170 (2009).
16. Ejike CECC, Collins SA, Balasuriya N, Swanson AK, Mason B and Udenigwe CC, Prospects of microalgae proteins in producing peptide-based functional foods for promoting cardiovascular health. Trends Food Sci Technol 59:30–36 (2017).
17. Cheevadhanarak S, Paithoonrangsarid K, Prommeenate P, Kaewngam W, Musigkain A, Tragoonrung S et al., Draft genome sequence of Arthrospira platensis C1 (PCC9438). Stand Genomic Sci 6:43–53 (2012).
18. Nahnsen S, Bielow C, Reinert K and Kohlbacher O, Tools for label-free peptide quantification. Mol Cell Proteomics 12:549–556 (2013).
19. Ji C, Cao X, Liu H, Qu J, Yao C, Zou H et al., Investigating cellular responses during photohydrogen production by the marine microalga Tetraselmis subcordiformis by quantitative proteome analysis. Appl Biochem Biotechnol 177:649–661 (2015).
20. Zybailov BL, Florens L and Washburn MP, Quantitative shotgun proteomics using a protease with broad specificity and normalized spectral abundance factors. Mol BioSyst 3:354–360 (2007).
21. Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD and Bairoch A, ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31:3784–3788 (2003).
22. Lefort F, Calmin G, Crovadore J, Falquet J, Hurni J-P, Osteras M et al., Whole-genome shotgun sequence of Arthrospira platensis strain Paraca, a cultivated and edible Cyanobacterium. Genome Announc 2: e00751-14 (2014).
23. Raven JA, Rubisco: still the most abundant protein of Earth? New Phytol 198:1–3 (2013).
24. Panchaud A, Affolter M and Kussmann M, Mass spectrometry for nutritional peptidomics: how to analyze food bioactives and their health effects. J Proteomics 75:3546–3559 (2012).
25. Minkiewicz P, Dziuba J and Michalska J, Bovine meat proteins as potential precursors of biologically active peptides: a computational study based on the BIOPEP database. Food Sci Technol Int 17:39–45 (2011).
26. Carrasco-Castilla J, Hernández-Álvarez AJ, Jiménez-Martínez C, Jacinto-Hernández C, Alaiz M, Girón-Calle J, Vioque J et al., Antioxidant and metal chelating activities of Phaseolus vulgaris L. var. Jamapa protein isolates, phaseolin and lectin hydrolysates. Food Chem 131:1157–1164 (2012).
27. Lacroix IM and Li-Chan EC, Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. J Funct Foods 4:403–422 (2012).