Nongonierma_et_al._JFF_2017.pdf (1.14 MB)
Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of camel milk protein hydrolysates generated with trypsin
journal contribution
posted on 2017-08-08, 11:28 authored by Alice B. Nongonierma, Sara Paolella, Priti Mudgil, Sajid Maqsood, Richard J. FitzgeraldDipeptidyl peptidase IV (DPP-IV) inhibitory peptides were identified in silico within camel milk proteins.
Camel milk was hydrolysed with trypsin using a design of experiments (DOE, temperature (40–60 C),
enzyme to substrate (E:S) ratio (0.50–2.00% (w/w)) and time (60–240 min)). Fifteen hydrolysates
(H1–H15) having DPP-IV half maximal inhibitory concentration (IC50) values between 0.52 ± 0.06 (H9)
and 1.26 ± 0.13 (H1) mg mL 1 were produced. Camel and bovine milk proteins hydrolysed at 40 C,
1.8% E:S and 218 min had DPP-IV IC50 values of 0.68 ± 0.08 and 0.85 ± 0.10 mg mL 1 (p < 0.05), respectively.
Potent and unique DPP-IV inhibitory peptides (Leu-Pro-Val-Pro-Gln and Trp-Lys) were identified
in camel milk protein hydrolysates, which were not present in bovine milk protein hydrolysates. The
DPP-IV inhibitory properties of camel milk peptides were reported for the first time in this study.
Camel milk is an interesting substrate to further investigate for its antidiabetic potential.
History
Publication
Journal of Functional Foods;34, pp. 49-58Publisher
ElsevierNote
peer-reviewedOther Funding information
United Arab Emirates University, SFI, EIRights
This is the author’s version of a work that was accepted for publication in Journal of Functional Foods. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Functional Foods, 2017, 34, pp. 49-58, http://dx.doi.org/10.1016/j.jff.2017.04.016Language
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