Peptidome profiles and bioactivity elucidation of buffalo-milk dairy products after gastrointestinal digestion

Food Research International

Volumn 105, Issue , 2018, Pages 1003-1010

  Basilicata, Manuela Giovanna ^a   Pepe, Giacomo ^a,b   Sommella, Eduardo ^a   Ostacolo, Carmine ^c   Manfra, Michele ^d   Sosto, Gennaro ^e   Pagano, Giuseppe ^f   Novellino, Ettore ^c   Campiglia, Pietro ^a,g  

^a UNIVERSITY OF SALERNO   (Italy)

^b Pineta Grande Hospital   (Italy)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^d UNIVERSITY OF BASILICATA   (Italy)

^e Azienda Sanitaria Regionale del Molise   (Italy)

^f San Salvatore Dairy Factory   (Italy)

^g European Biomedical Research Institute Salerno   (Italy)

Author keywords

Bioaccessibility; Bioactive peptides; Buffalo milk dairy product; High resolution mass spectrometry; In vitro gastrointestinal digestion

Indexed keywords

BIOACTIVITY; DAIRY PRODUCTS; MASS SPECTROMETRY; PEPTIDES; PROTEINS;

BIOACCESSIBILITY; BIOACTIVE PEPTIDES; BUFFALO MILK; GASTROINTESTINAL DIGESTION; HIGH RESOLUTION MASS SPECTROMETRY;

DAIRIES;

CASEIN; PEPTIDE; WHEY PROTEIN;

ANIMAL; BUFFALO; CHEESE; CHEMISTRY; DIGESTION; ELECTROSPRAY MASS SPECTROMETRY; FOOD ANALYSIS; FOOD HANDLING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ICE CREAM; INTESTINAL SECRETIONS; MILK; NUTRITIONAL VALUE; PROCEDURES; PROTEIN DATABASE; PROTEOMICS; STOMACH JUICE; TANDEM MASS SPECTROMETRY;

ANIMALS; BUFFALOES; CASEINS; CHEESE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DATABASES, PROTEIN; DIGESTION; FOOD ANALYSIS; FOOD HANDLING; GASTRIC JUICE; ICE CREAM; INTESTINAL SECRETIONS; MILK; NUTRITIVE VALUE; PEPTIDES; PROTEOMICS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TANDEM MASS SPECTROMETRY; WHEY PROTEINS;

EID: 85038214274     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2017.12.038     Document Type: Article

References (40)

1. Abdel-Hamid, M., Otte, J., De Gobba, C., Osman, A., Hamad, E., Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins. International Dairy Journal 66 (2017), 91–98 (file:///C:/Users/Administrator/Downloads/1-s2.0-S0958694616303351-main%20(1).pdf).
2. Ahmad, S., Anjum, F.M., Huma, N., Sameen, A., Zahoor, T., Composition and physico-chemical characteristics of buffalo milk with particular emphasis on lipids, proteins, minerals, enzymes and vitamins. The Journal of Animal and Plant Sciences 23 (2013), 62–74 http://www.thejaps.org.pk/docs/Supplementary/vol-3-sup-1/14.pdf.
3. Anema, S.G., Li, Y., Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size. Journal of Dairy Research 70 (2003), 73–83 https://www.ncbi.nlm.nih.gov/pubmed/12617395.
4. Capriotti, A.L., Caruso, G., Cavaliere, C., Samperi, R., Ventura, S., Chiozzi, R.Z., Lagana, A., Identification of potential bioactive peptides generated by simulated gastrointestinal digestion of soybean seeds and soy milk proteins. Journal of Food Composition and Analysis 44 (2015), 205–213 http://www.sciencedirect.com/science/article/pii/S0889157515001738.
5. Capriotti, A.L., Cavaliere, C., Piovesana, S., Samperi, R., Laganà, A., Recent trends in the analysis of bioactive peptides in milk and dairy products. Analytical and Bioanalytical Chemistry 408 (2016), 2677–2685 https://www.ncbi.nlm.nih.gov/pubmed/26800979.
6. Coda, R., Rizzello, C.G., Pinto, D., Gobbetti, M., Selected lactic acid bacteria synthesize antioxidant peptides during sourdough fermentation of cereal flours. Applied and Environmental Microbiology 78 (2012), 1087–1096 http://aem.asm.org/content/78/4/1087.full.
7. Corredig, M., Douglas, D.G., Effect of temperature and pH on the interactions of whey proteins with casein micelles in skim milk. Food Research International 29 (1996), 49–55 http://www.sciencedirect.com/science/article/pii/0963996995000585.
8. Coste, M., Rochet, V., Léonil, J., Mollé, D., Bouhallab, S., Tomé, D., Identification of C-terminal peptides of bovine beta-casein that enhance proliferation of rat lymphocytes. Immunology Letters 33 (1992), 41–46 https://www.ncbi.nlm.nih.gov/pubmed/1427989.
9. D'Ambrosio, C., Arena, S., Salzano, A.M., Renzone, G., Ledda, L., Scaloni, A., A proteomic characterization of water buffalo milk fractions describing PTM of major species and identification of minor fractions involved in nutrient delivery and defense against pathogens. Proteomics 8 (2008), 3657–3666 https://www.ncbi.nlm.nih.gov/pubmed/18668696.
10. Donato, L., Guyomarc'h, F., Formation and properties of the whey protein/κ-casein complexes in heated skim milk. Dairy Science and Technology 89 (2009), 3–29 https://www.dairy-journal.org/articles/dst/abs/2009/01/dst0828/dst0828.html.
11. Fiat, A.M., Migliore-Samour, D., Jollès, P., Drouet, L., Bal dit Sollier, C., Caen, J., Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities. Journal of Dairy Science 76 (1993), 301–310 https://www.ncbi.nlm.nih.gov/pubmed/8436680.
12. Hayes, M., Stanton, C., Fitzgerald, G.F., Ross, R.P., Putting microbes to work: Dairy fermentation, cell factories and bioactive peptides. Part II: Bioactive peptide functions. Biotechnology Journal 2 (2007), 435–449 https://www.ncbi.nlm.nih.gov/pubmed/17407211.
13. Hemming, M.L., Selkoe, D.J., Farris, W., Effects of prolonged angiotensin-converting enzyme inhibitor treatment on amyloid beta-protein metabolism in mouse models of Alzheimer disease. Neurobiology of Disease 26 (2007), 273–281 https://www.ncbi.nlm.nih.gov/pubmed/17321748.
14. International Dairy Federation, The world dairy situation 2014. Bulletin no., 476/2014. 2014, International Dairy Federation (IDF), Brussels, Belgium http://www.idfa.org/docs/default-source/d-news/wds2014teaser.pdf?sfvrsn=2.
15. Jang, H.D., Swaisgood, H.E., Disulfide bond formation between thermally denatured β-lactoglobulin and κ-casein in casein micelles. Journal of Dairy Science 73 (1990), 900–904 http://www.sciencedirect.com/science/article/pii/S0022030290787462.
16. Jinsmaa, Y., Yoshikawa, M., Enzymatic release of neocasomorphin and beta-casomorphin from bovine beta-casein. Peptides 20 (1999), 957–962 https://www.ncbi.nlm.nih.gov/pubmed/10503774.
17. Juillerat-Jeanneret, L., Robert, M.C., Juillerat, M.A., Peptides from lactobacillus hydrolysates of bovine milk caseins inhibit prolyl-peptidases of human colon cells. Journal of Agricultural and Food Chemistry 59 (2011), 370–377 https://www.ncbi.nlm.nih.gov/pubmed/21126072.
18. Korhonen, H., Pihlanto-Leppäla, A., Rantamäki, P., Tupasela, T., Impact of processing on bioactive proteins and peptides. Trends in Food Science & Technology 9 (1998), 307–319 http://www.sciencedirect.com/science/article/pii/S0924224498000545.
19. Lacroix, I.M.E., Li-Chan, E.C.Y., Isolation and characterization of peptides with dipeptidyl peptidase-IV inhibitory activity from pepsin-treated bovine whey proteins. Peptides 54 (2014), 39–48 http://www.sciencedirect.com/science/article/pii/S0196978114000059.
20. Lim, G.E., Brubaker, P., Glucagon-like peptide 1 secretion by the L-cell. The view from within. Diabetes 55 (2006), S70–77 http://diabetes.diabetesjournals.org/content/55/Supplement_2/S70.
21. López, M.B., Jordán, M.J., Hellin, P., Castillo, M., Laencina, J., Kinetics of ĸ-casein hydrolysis by different rennet and coagulant enzymes in murciano-granadina goat milk. Milchwissenschaft 52 (1997), 370–372 http://www.manuelcastillo.es/pdfs-publications/Kinetics%20of%20k-casein%20hydrolisis%20by%20different%20rennet%20and%20coagulant%20enzymes%20in%20murciano-granadina%20gat%20milk.pdf.
22. López-Expósito, I., Minervini, F., Amigo, L., Recio, I., Identification of antibacterial peptides from bovine kappa-casein. Journal of Food Protection 69 (2006), 2992–2997 https://www.ncbi.nlm.nih.gov/pubmed/17186669.
23. Myöhänen, T.T., García-Horsman, J.A., Tenorio-Laranga, J., Männistö, P.T., Issues about the physiological functions of prolyl oligopeptidase based on its discordant spatial association with substrates and inconsistencies among mRNA, protein levels, and enzymatic activity. The Journal of Histochemistry and Cytochemistry 57 (2009), 831–848 https://www.ncbi.nlm.nih.gov/pubmed/19687473.
24. Pender, S.L.F., MacDonald, T.T., Matrix metalloproteinases and the gut-new roles for old enzymes. Current Opinion in Pharmacology 4 (2004), 546–550 https://www.ncbi.nlm.nih.gov/pubmed/15525541.
25. Pepe, G., Sommella, E., Ventre, G., Scala, M.C., Adesso, S., Ostacolo, C., Campiglia, P., Antioxidant peptides released from gastrointestinal digestion of “Stracchino” soft cheese: Characterization, in vitro intestinal protection and bioavailability. Journal of Functional Foods 26 (2016), 494–505 http://www.sciencedirect.com/science/article/pii/S175646461630233X.
26. Pierri, G., Kotoni, D., Simone, P., Villani, C., Pepe, G., Campiglia, P., Gasparrini, F., Analysis of bovine milk caseins on organic monolithic columns: An integrated capillary liquid chromatography–high resolution mass spectrometry approach for the study of time-dependent casein degradation. Journal of Chromatography A 1313 (2013), 259–269 https://www.ncbi.nlm.nih.gov/pubmed/24011725.
27. Pihlanto-Leppälä, A., Koskinen, P., Piilola, K., Tupasela, T., Korhonen, H., Angiotensin I-converting enzyme inhibitory properties of whey protein digests: Concentration and characterization of active peptides. Journal of Dairy Research 67 (2000), 53–64 https://www.ncbi.nlm.nih.gov/pubmed/10717843.
28. Piovesana, S., Capriotti, A.L., Cavaliere, C., La Barbera, G., Samperi, R., Zenezini Chiozzi, R., Laganà, A., Peptidome characterization and bioactivity analysis of donkey milk. Journal of Proteomics 119 (2015), 21–29 https://www.ncbi.nlm.nih.gov/pubmed/25668324.
29. Rival, S.G., Boeriu, C.G., Wichers, H.J., Caseins and caseinhydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition. Journal of Agricultural and Food Chemistry 49 (2001), 295–302 https://www.ncbi.nlm.nih.gov/pubmed/11170591.
30. Robert, M.C., Razaname, A., Mutter, M., Juillerat, M.A., Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by lactobacillus helveticus NCC 2765. Journal of Agricultural and Food Chemistry 52 (2004), 6923–6931 https://www.ncbi.nlm.nih.gov/pubmed/15537298.
31. Roeb, E., Dietrich, C.G., Winograd, R., Arndt, M., Breuer, B., Fass, J., Matern, S., Activity and cellular origin of gelatinases in patients with colon and rectal carcinoma. Differential activity of matrix metalloproteinase-9. Cancer 92 (2001), 2680–2691 https://www.ncbi.nlm.nih.gov/pubmed/11745204.
32. Rojas-Ronquillo, R., Cruz-Guerrero, A., Flores-Nájera, A., Rodríguez-Serrano, G., Gómez-Ruiz, L., Reyes-Grajeda, J.P., Jiménez-Guzmán, J., Antithrombotic and angiotensin-converting enzyme inhibitory properties of peptides released from bovine casein by Lactobacillus casei Shirota. International Dairy Journal 26 (2012), 147–154 http://www.sciencedirect.com/science/article/pii/S0958694612001161.
33. Silveira, S.T., Martínez-Maqueda, D., Recio, I., Hernández-Ledesma, B., Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin. Food Chemistry 141 (2013), 1072–1077 https://www.ncbi.nlm.nih.gov/pubmed/23790888.
34. Sommella, E., Pepe, G., Pagano, F., Ostacolo, C., Tenore, G.C., Russo, M.T., Campiglia, P., Detailed polyphenolic profiling of Annurca apple (M. pumila Miller cv Annurca) by a combination of RP-UHPLC and HILIC, both hyphenated to IT-TOF mass spectrometry. Food Research International 76 (2015), 466–477 https://www.ncbi.nlm.nih.gov/pubmed/28455027.
35. Sommella, E., Pepe, G., Ventre, G., Pagano, F., Conte, G.M., Ostacolo, C., Campiglia, P., Detailed peptide profiling of “Scotta”: From a dairy waste to a source of potential health-promoting compounds. Dairy Science & Technology 96 (2016), 763–771 https://link.springer.com/content/pdf/10.1007%2Fs13594-016-0297-y.pdf.
36. Tagliazucchi, D., Helal, A., Verzelloni, E., Conte, A., Bovine milk antioxidant properties: Effect of in vitro digestion and identification of antioxidant compounds. Dairy Science & Technology 96 (2016), 657–676 https://link.springer.com/content/pdf/10.1007%2Fs13594-016-0294-1.pdf.
37. Tenore, G.C., Ritieni, A., Campiglia, P., Stiuso, P., Di Maro, S., Sommella, E., Novellino, E., Antioxidant peptides from “mozzarella di Bufala Campana DOP” after simulated gastrointestinal digestion: In vitro intestinal protection, bioavailability, and anti-haemolytic capacity. Journal of Functional Foods 15 (2015), 365–375 http://www.sciencedirect.com/science/article/pii/S1756464615001656.
38. Yoshikawa, M., Tani, F., Chiba, H., Structure-activity relationship of opioid antagonist peptides derived from milk proteins. Shiba, T., (eds.) Peptide chemistry, 1988, Protein Research Foundation, Osaka, 473–476.
39. Zenezini Chiozzi, R., Capriotti, A.L., Cavaliere, C., La Barbera, G., Piovesana, S., Samperi, R., Laganà, A., Purification and identification of endogenous antioxidant and ACE-inhibitory peptides from donkey milk by multidimensional liquid chromatography and nanoHPLC-high resolution mass spectrometry. Analytical and Bioanalytical Chemistry 408 (2016), 5657–5666 https://www.ncbi.nlm.nih.gov/pubmed/27325462.
40. Zhang, Y., Chen, R., Zuo, F., Ma, H., Zhang, Y., Chen, S., Comparison of dipeptidyl peptidase IV-inhibitory activity of peptides from bovine and caprine milk casein by in silico and in vitro analyses. International Dairy Journal 53 (2016), 37–44 http://www.sciencedirect.com/science/article/pii/S0958694615001879.