Comparison of goat and sheep β-lactoglobulin to bovine β-lactoglobulin as potential source of dipeptidyl peptidase IV (DPP-4) inhibitors

International Dairy Journal

Volumn 24, Issue 2, 2012, Pages 97-101

  Tulipano, Giovanni ^a   Cocchi, Daniela ^a   Caroli, Anna Maria ^a  

^a UNIVERSITY OF BRESCIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY ASSAYS; AMINO ACID SEQUENCE; BIOACTIVE PEPTIDES; DIPEPTIDYL PEPTIDASE IV; IN-SILICO; IN-VITRO; IN-VITRO ANALYSIS; INHIBITORY ACTIVITY; INHIBITORY EFFECT; LACTOGLOBULIN; MOLECULAR DETERMINANTS; POTENTIAL SOURCES; WHEY PROTEINS;

AMINO ACIDS; PEPTIDES;

MAMMALS;

BOVINAE; CAPRA HIRCUS; MUS; OVIS ARIES;

EID: 84861898887     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2011.09.004     Document Type: Article

References (27)

1. Abubakar A., Saito T., Kitazawa H., Kawai Y., Itoh T. Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion. Journal of Dairy Science 1998, 81:3131-3138.
2. Akhavan T., Luhovyy B.L., Brown P.H., Cho C.E., Anderson G.H. Effect of premeal consumption of whey protein and its hydrolysate on food intake and postmeal glycemia and insulin responses in young adults. American Journal of Clinical Nutrition 2010, 91:966-975.
3. Caroli A.M., Chessa S., Erhardt G.J. Milk protein genetic variation in cattle: impact on animal breeding and human nutrition. Journal of Dairy Science 2009, 92:5335-5352.
4. Cerbulis J., Farrell H.M. Composition of milks of dairy cattle. I. Protein, lactose, and fat contents and distribution of protein fraction. Journal of Dairy Science 1975, 58:817-827.
5. Darmoul D., Voisin T., Couvineau A., Rouyer-Fessard C., Salomon R., Wang Y., et al. Regional expression of epithelial dipeptidyl peptidase IV in the human intestines. Biochemical and Biophysical Research Communications 1994, 203:1224-1229.
6. Drab S.R. Incretin-based therapy for type-2 diabetes mellitus: current status and future prospects. Pharmacotherapy 2010, 30:609-624.
7. Drucker D.J. Enhancing the action of incretin hormones: a new whey forward?. Endocrinology 2006, 147:3171-3172.
8. Drucker D.J. The biology of incretin hormones. Cell Metabolism 2006, 3:153-165.
9. Foltz M., Van der Pijl P.C., Duchateau G.S. Current in vitro testing of bioactive peptides is not valuable. Journal of Nutrition 2010, 140:117-118.
10. Frid A.H., Nilsson M., Holst J.J., Bjorck I.M. Effect of whey on blood glucose and insulin responses to composite breakfast and lunch meals in type 2 diabetic subjects. American Journal of Clinical Nutrition 2005, 82:69-75.
11. Ganai N.A., Bovenhuis H., van Arendonk J.A.M., Visker M.H.P.W. Novel polymorphisms in the bovine β-lactoglobulin gene and their effects on β-lactoglobulin protein concentration in milk. Animal Genetics 2008, 40:127-133.
12. s1-casein locus in cattle. Genetics Selection Evolution 1989, 21:547-554.
13. Gunnarsson P.T., Winzell M.S., Deacon C.F., Larsen M.O., Jelic K., Carr R.D., et al. Glucose-induced incretin hormone release and inactivation are differently modulated by oral fat and protein in mice. Endocrinology 2006, 147:3173-3180.
14. Hansen L., Deacon C.F., Orskov C., Holst J.J. Glucagone-like peptide-1-(7-36) amide is transformed to glucagon-like-peptide-1-(9-36) amide by dipeptidyl peptidase IV (DPPIV) in the capillaries supplying the L cells on the porcine intestine. Endocrinology 1999, 140:5356-5363.
15. Hernandez-Ledesma B., Recio I., Amigo L. Beta-lactoglobulin as a source of bioactive peptides. Amino Acids 2008, 35:257-265.
16. Holst J.J., Deacon C.F. Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes. Diabetes 1998, 47:1663-1670.
17. Lorenzini E.C., Chessa S., Chiatti F., Caroli A., Pagnacco G. Peptidi bioattivi di latte e derivati. Scienza e Tecnica Lattiero-Casearia 2007, 58:113-156.
18. Luhovyy B.L., Akhavan T., Anderson G.H. Whey proteins in the regulation of food intake and satiety. Journal of the American College of Nutrition 2007, 26:704S-712S.
19. Lum L.S., Dovč P., Medrano J.F. Polymorphisms of bovine β-lactoglobulin promoter and differences in the binding affinity of activator protein-2 transcription factor. Journal of Dairy Science 1997, 80:1389-1397.
20. Manders R.J., Koopman R., Sluijsmans W.E., van den Berg R., Verbeek K., Saris W.H., et al. Co-ingestion of a protein hydrolysate with or without additional leucine effectively reduces postprandial blood glucose excursions in type 2 diabetic men. Journal of Nutrition 2006, 136:1294-1299.
21. Meisel H. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 1997, 43:119-128.
22. Morifuji M., Koga J., Kawanaka K., Higuchi M. Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake rate in L6 myotubes and isolated skeletal muscles. Journal of Nutrition Science and Vitaminology 2009, 55:81-86.
23. Nilsson M., Holst J.J., Bjorck I.M. Metabolic effects of amino acid mixtures and whey protein in healthy subjects: studies using glucose equivalent drinks. American Journal of Clinical Nutrition 2007, 85:996-1004.
24. Nilsson M., Stenberg M., Frid A.H., Holst J.J., Bjorck I.M. Glycemia and insulinemia in healthy subjects after lactose-equivalent meals and other food proteins: the role of plasma amino acids and incretins. American Journal of Clinical Nutrition 2004, 80:1246-1253.
25. Petersen B.L., Ward L.S., Bastian E.D., Jenkins A.L., Campbell J., Vuksan V. A whey protein supplement decreases post-prandial glycemia. Nutrition Journal 2009, 8:47.
26. Sadat L., Cakir-Kiefer C., N'Negue M.-A., Gaillard J.-L., Girardet J.-M., Miclo L. Isolation and identification of antioxidative peptides from bovine α-lactalbumin. International Dairy Journal 2011, 21:214-221.
27. Tulipano G., Sibilia V., Caroli A.M., Cocchi D. Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors. Peptides 2011, 32:835-838.