Empirical and bioinformatic characterization of buffalo (Bubalus bubalis) colostrum whey peptides & their angiotensin I-converting enzyme inhibition

Food Chemistry

Volumn 228, Issue , 2017, Pages 582-594

  Ashok, N R ^a   Aparna, H S ^a  

^a UNIVERSITY OF MYSORE   (India)

Author keywords

Angiotensin I converting enzyme; Buffalo colostrum; Molecular docking; Nano LC MS MS; Whey peptides

Indexed keywords

ENZYME INHIBITION; ENZYMES; GENES; PEPTIDES;

ACE INHIBITORY PEPTIDES; ANGIOTENSIN I CONVERTING ENZYME INHIBITOR; ANGIOTENSIN I-CONVERTING ENZYME; BUFFALO COLOSTRUM; MOLECULAR DOCKING; MULTIFUNCTIONAL PROPERTIES; NANO-LC; THERAPEUTIC APPLICATION;

PROTEINS;

ACTIN RELATED PROTEIN 2-3 COMPLEX; ALPHA LACTALBUMIN; ANTIINFECTIVE AGENT; ANTIOXIDANT; BETA LACTOGLOBULIN; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; GELSOLIN; GLOBULAR PROTEIN; GLUTAMYL AMINOPEPTIDASE; GLYCOSYLPHOSPHATIDYLINOSITOL; IMMUNOGLOBULIN; IMMUNOMODULATING AGENT; LACTOFERRIN; LACTOPEROXIDASE; LACTOSE; LYSOZYME; MILK FAT; MILK PROTEIN; MYOSTATIN; OCTAPEPTIDE; OPIATE PEPTIDE; PANCREAS POLYPEPTIDE; PROTEOME; SECRETORY PROTEIN; SERUM ALBUMIN; SIGNAL PEPTIDE; SUCCINATE COENZYME A LIGASE; TRANSFERRIN; WHEY PROTEIN; PEPTIDE;

ANTIOXIDANT ACTIVITY; ARTICLE; CELLULAR DISTRIBUTION; CITRIC ACID CYCLE; COLOSTRUM; ENZYME INHIBITION; IN VITRO STUDY; LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY; MOLECULAR DOCKING; MOLECULAR WEIGHT; PEPTIDE SYNTHESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; TANDEM MASS SPECTROMETRY; ULTRAFILTRATION; WATER BUFFALO; ANIMAL; BUFFALO; CHEMISTRY; FEMALE; METABOLISM; PREGNANCY; PROCEDURES; WHEY;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; BUFFALOES; COLOSTRUM; FEMALE; MOLECULAR DOCKING SIMULATION; PEPTIDES; PEPTIDYL-DIPEPTIDASE A; PREGNANCY; WHEY;

EID: 85012993519     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.02.032     Document Type: Article

References (40)

1. Anup, C.P., Melvin, P., Shilpa, N., Gandhi, M.N., Jadhav, M., Ali, H., Kini, K.R., Proteomic analysis of elicitation of downy mildew disease resistance in pearl millet by seed priming with β-aminobutyric acid and Pseudomonas fluorescens. Journal of Proteomics 120 (2015), 58–74.
2. Aparna, H.S., Salimath, P.V., Isolation and characterization of a sialo-glycopeptide from buffalo colostrum. Glycoconjugate Journal 13 (1996), 63–67.
3. Aparna, H.S., Salimath, P.V., Acidic glycoproteins of buffalo colostrum and their influence on the growth of Bifidobacterium bifidus. Nutrition Research 19 (1999), 295–303.
4. Benjamini, Y., Hochberg, Y., Controlling the false discovery rate: a practical and powerful approach to multiple testing. Journal of the Royal Statistical Society: Series B (Methodological), 1995, 289–300.
5. Briesemeister, S., Rahnenführer, J., Kohlbacher, O., YLoc—An interpretable web server for predicting subcellular localization. Nucleic Acids Research 38:Suppl. 2 (2010), W497–W502.
6. Carbonaro, M., Nardini, M., Maselli, P., Nucara, A., Chemico-physical and nutritional properties of traditional legumes (lentil, Lens culinaris L., and grass pea, Lathyrus sativus L.) from organic agriculture: an explorative study. Organic Agriculture 5 (2015), 179–187.
7. Chougule, R.A., Aparna, H.S., Characterization of β-lactoglobulin from buffalo (Bubalus bubalis) colostrum and its possible interaction with erythrocyte lipocalin-interacting membrane receptor. Journal of Biochemistry 150 (2011), 279–288.
8. Chougule, R.A., Shilpa, P., Salimath, B.P., Sosalegowda, A.H., Buffalo colostrum β-lactoglobulin inhibits VEGF-induced angiogenesis by interacting with G protein-coupled receptor kinase. Applied Biochemistry and Biotechnology 171 (2013), 366–381.
9. Church, F.C., Swaisgood, H.E., Porter, D.H., Catignani, G.L., Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science 66 (1983), 1219–1227.
10. Coroian, A., Erler, S., Matea, C.T., Mireșan, V., Răducu, C., Bele, C., Coroian, C.O., Seasonal changes of buffalo colostrum: physicochemical parameters, fatty acids and cholesterol variation. Chemistry Central Journal, 7, 2013, 1.
11. Fuglsang, A., Rattray, F.P., Nilsson, D., Nyborg, N.C., Lactic acid bacteria: inhibition of angiotensin converting enzyme in vitro and in vivo. Antonie van Leeuwenhoek 83 (2003), 27–34.
12. Gao, X., McMahon, R.J., Woo, J.G., Davidson, B.S., Morrow, A.L., Zhang, Q., Temporal changes in milk proteomes reveal developing milk functions. Journal of Proteome Research 11 (2012), 3897–3907.
13. Golinelli, L.P., Del Aguila, E.M., Paschoalin, V.M.F., Silva, J.T., Conte-Junior, C.A., Functional aspect of colostrum and whey proteins in human milk. Journal of Human Nutrition & Food Science, 2, 2014, 1035.
14. Issaq, H.J., Chan, K.C., Blonder, J., Ye, X., Veenstra, T.D., Separation, detection and quantitation of peptides by liquid chromatography and capillary electrochromatography. Journal of Chromatography A 1216 (2009), 1825–1837.
15. Jiang, J., Chen, S., Ren, F., Luo, Z., Zeng, S.S., Yak milk casein as a functional ingredient: preparation and identification of angiotensin-I-converting enzyme inhibitory peptides. Journal of Dairy Research 74 (2007), 18–25.
16. Jimsheena, V.K., Gowda, L.R., Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: Structure–activity relationship. Peptides 31 (2010), 1165–1176.
17. Korhonen, H., Pihlanto, A., Bioactive peptides: production and functionality. International Dairy Journal 16 (2006), 945–960.
18. Langer, P., Differences in the composition of colostrum and milk in eutherians reflect differences in immunoglobulin transfer. Journal of Mammalogy 90 (2009), 332–339.
19. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193 (1951), 265–275.
20. Manninen, A.H., Protein hydrolysates in sports nutrition. Nutrition & Metabolism, 6, 2009, 1.
21. Marambe, H.K., Shand, P.J., Wanasundara, J.P., Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion. Journal of Agricultural and Food Chemistry 59 (2011), 9596–9604.
22. Miguel, M., Recio, I., Gómez-Ruiz, J.A., Ramos, M., Lopez-Fandino, R., Angiotensin I–converting enzyme inhibitory activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection 67 (2004), 1914–1920.
23. Ngoh, Y.Y., Gan, C.Y., Enzyme-assisted extraction and identification of antioxidative and α-amylase inhibitory peptides from Pinto beans (Phaseolus vulgaris cv. Pinto). Food Chemistry 190 (2016), 331–337.
24. Ortiz-Chao, P., Gómez-Ruiz, J.A., Rastall, R.A., Mills, D., Cramer, R., Pihlanto Ellipsis, A., Jauregi, P., Production of novel ACE inhibitory peptides from β-lactoglobulin using Protease N Amano. International Dairy Journal 19 (2009), 69–76.
25. Pellegrini, A., Dettling, C., Thomas, U., Hunziker, P., Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochimica et Biophysica Acta (BBA)-General Subjects 1526 (2001), 131–140.
26. Picariello, G., Mamone, G., Addeo, F., Ferranti, P., Novel mass spectrometry-based applications of the ‘omic’ sciences in food technology and biotechnology. Food Technology and Biotechnology 50 (2012), 286–305.
27. Pihlanto-Leppälä, A., Bioactive peptides derived from bovine whey proteins: Opioid and ace-inhibitory peptides. Trends in Food Science & Technology 11 (2000), 347–356.
28. 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.
29. Pihlanto-Leppälä, A., Rokka, T., Korhonen, H., Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins. International Dairy Journal 8 (1998), 325–331.
30. Plaisancié, P., Claustre, J., Estienne, M., Henry, G., Boutrou, R., Paquet, A., Léonil, J., A novel bioactive peptide from yoghurts modulates expression of the gel-forming MUC2 mucin as well as population of goblet cells and Paneth cells along the small intestine. The Journal of Nutritional Biochemistry 24 (2013), 213–221.
31. Quirós, A., Ramos, M., Muguerza, B., Delgado, M.A., Miguel, M., Aleixandre, A., Recio, I., Identification of novel antihypertensive peptides in milk fermented with Enterococcus faecalis. International Dairy Journal 17 (2007), 33–41.
32. Re, R., Pellegrini, N., Proteggente, A., Pannala, A., Yang, M., Rice-Evans, C., Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radical Biology and Medicine 26 (1999), 1231–1237.
33. Rohit, A.C., Sathisha, K., Aparna, H.S., A variant peptide of buffalo colostrum β-lactoglobulin inhibits angiotensin I-converting enzyme activity. European Journal of Medicinal Chemistry 53 (2012), 211–219.
34. Saavedra, L., Hebert, E.M., Minahk, C., Ferranti, P., An overview of “omic” analytical methods applied in bioactive peptide studies. Food Research International 54 (2013), 925–934.
35. Saidi, S., Deratani, A., Belleville, M.P., Amar, R.B., Antioxidant properties of peptide fractions from tuna dark muscle protein by-product hydrolysate produced by membrane fractionation process. Food Research International 65 (2014), 329–336.
36. Sánchez-Rivera, L., Martínez-Maqueda, D., Cruz-Huerta, E., Miralles, B., Recio, I., Peptidomics for discovery, bioavailability and monitoring of dairy bioactive peptides. Food Research International 63 (2014), 170–181.
37. Scammell, A.W., Production and uses of colostrum. Australian Journal of Dairy Technology, 56, 2001, 74.
38. Sharma, S., SIngh, R., Rana, S., Bioactive peptides: A review. Int J Bioautomation 15 (2011), 223–250.
39. Tsai, J.S., Chen, T.J., Pan, B.S., Gong, S.D., Chung, M.Y., Antihypertensive effect of bioactive peptides produced by protease-facilitated lactic acid fermentation of milk. Food Chemistry 106 (2008), 552–558.
40. Weber, K., Pringle, J.R., Osborn, M., Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods in Enzymology 26 (1972), 3–27.