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    Generation of Bioactive Hydrolysates and Peptides from Bovine Hemoglobin with In Vitro Renin, Angiotensin-I-Converting Enzyme and Dipeptidyl Peptidase-IV Inhibitory Activities

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    Author
    Lafarga, Tomas
    Rai, Dilip K.
    O'Connor, Paula M.
    Hayes, Maria
    Keyword
    Bioactive hydrolysates
    Functional food ingredients
    Bovine hemoglobin
    Bioactive peptides
    Date
    02/03/2016
    
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    URI
    http://hdl.handle.net/11019/1011
    Citation
    Lafarga, T., Rai, D. K., O'connor, P. and Hayes, M. (2016), Generation of Bioactive Hydrolysates and Peptides from Bovine Hemoglobin with In Vitro Renin, Angiotensin-I-Converting Enzyme and Dipeptidyl Peptidase-IV Inhibitory Activities. Journal of Food Biochemistry. doi: 10.1111/jfbc.12259
    Abstract
    Bovine hemoglobin was selected for use in the generation of bioactive hydrolysates with potential for use as functional food ingredients for prevention of disorders such as hypertension, obesity and diabetes. Bovine hemoglobin was isolated and hydrolyzed with papain, which was selected using in silico analysis. The generated hydrolysate was enriched by ultrafiltration and further purified by high performance liquid chromatography. A number of peptides were identified using de novo peptide sequencing and these peptides were chemically synthesized to confirm their bioactivity in vitro. Three multifunctional peptides with both, ACE-I and renin-inhibitory properties and one peptide with ACE-I-inhibiting properties were identified. These included the di-peptide HR with ACE-I and renin IC50 values of 0.19 and 7.09 mM, respectively. The generated papain hydrolysate of bovine hemoglobin not only inhibited the enzymes ACE-I and renin but also the enzyme DPP-IV, which has been linked to type-2 diabetes.
    Funder
    Teagasc Walsh Fellowship Programme; Department of Agriculture, Food and the Marine
    Grant Number
    11/F/043
    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.1111/jfbc.12259
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    Food Biosciences
    Food Biosciences
    Food Biosciences
    Food Biosciences

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