TY - JOUR
T1 - Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of camel milk protein hydrolysates generated with trypsin
AU - Nongonierma, Alice B.
AU - Paolella, Sara
AU - Mudgil, Priti
AU - Maqsood, Sajid
AU - FitzGerald, Richard J.
N1 - Funding Information:
The authors wish to thank the United Arab Emirates University for funding the project through University Program for Advanced Research (UPAR), funding code: 31F094. The work described herein was partly supported by Enterprise Ireland under Grant Number TC2013-0001 and the Science Foundation Ireland Research Infrastructure Fund.
Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2017/7/1
Y1 - 2017/7/1
N2 - Dipeptidyl 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.
AB - Dipeptidyl 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.
KW - Bioactive peptides
KW - Camel milk proteins
KW - Dipeptidyl peptidase IV inhibition
KW - In silico analysis
KW - Response surface methodology (RSM)
KW - Trypsin
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U2 - 10.1016/j.jff.2017.04.016
DO - 10.1016/j.jff.2017.04.016
M3 - Article
AN - SCOPUS:85018503944
SN - 1756-4646
VL - 34
SP - 49
EP - 58
JO - Journal of Functional Foods
JF - Journal of Functional Foods
ER -