TY - JOUR
T1 - Angiotensin-converting enzyme inhibitory and antioxidant peptides from digestion of larvae and pupae of Asian weaver ant, Oecophylla smaragdina, Fabricius
AU - Pattarayingsakul, Werawich
AU - Nilavongse, Arjaree
AU - Reamtong, Onrapak
AU - Chittavanich, Pamorn
AU - Mungsantisuk, Idsada
AU - Mathong, Yuvadee
AU - Prasitwuttisak, Wipoo
AU - Panbangred, Watanalai
N1 - Funding Information:
This research was supported by a research grant from Mahidol University and the Development and Promotion of Science and Technology Talents Project (DPST). Mr Werawich Pattarayingsakul is also the recipient of a scholarship from the DPST. The authors are grateful to Dr James R Ketudat-Cairns for critical proofreading of the manuscript.
Publisher Copyright:
© 2016 Society of Chemical Industry
PY - 2017/8/15
Y1 - 2017/8/15
N2 - BACKGROUND: Mixed larvae and pupae of weaver ant (Oecophylla smaragdina) are widely used as an important food ingredient in regions of Thailand. They have high nutritional values and comprise 53% protein and 13% lipid. Peptides derived from food proteins have been shown to possess biological activities. RESULTS: Peptides derived from pepsin and trypsin digestion of these weaver ant larvae and pupae were purified based on angiotensin-converting enzyme (ACE) inhibitory and antioxidant activities, and their amino acid sequences were identified by liquid chromatography–tandem mass spectrometry (LC-MS/MS). In silico docking of peptides with ACE successfully predicted the inhibitory peptides as confirmed by their chemical synthesis. Two peptides with sequences of FFGT and LSRVP showed IC50 values for ACE inhibition of 19.5 ± 1.7 and 52.7 ± 4.0 µmol L−1, respectively. In addition, one potent antioxidant peptide with a sequence of CTKKHKPNC showed IC50 values of 48.2 ± 2.1 µmol L−1 for DPPH assay and 38.4 ± 0.2 µmol L−1 for ABTS assay, respectively. CONCLUSION: These results indicate that proteins from larvae and pupae of weaver ants are potential sources of peptides with anti-ACE and antioxidation bioactivities.
AB - BACKGROUND: Mixed larvae and pupae of weaver ant (Oecophylla smaragdina) are widely used as an important food ingredient in regions of Thailand. They have high nutritional values and comprise 53% protein and 13% lipid. Peptides derived from food proteins have been shown to possess biological activities. RESULTS: Peptides derived from pepsin and trypsin digestion of these weaver ant larvae and pupae were purified based on angiotensin-converting enzyme (ACE) inhibitory and antioxidant activities, and their amino acid sequences were identified by liquid chromatography–tandem mass spectrometry (LC-MS/MS). In silico docking of peptides with ACE successfully predicted the inhibitory peptides as confirmed by their chemical synthesis. Two peptides with sequences of FFGT and LSRVP showed IC50 values for ACE inhibition of 19.5 ± 1.7 and 52.7 ± 4.0 µmol L−1, respectively. In addition, one potent antioxidant peptide with a sequence of CTKKHKPNC showed IC50 values of 48.2 ± 2.1 µmol L−1 for DPPH assay and 38.4 ± 0.2 µmol L−1 for ABTS assay, respectively. CONCLUSION: These results indicate that proteins from larvae and pupae of weaver ants are potential sources of peptides with anti-ACE and antioxidation bioactivities.
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U2 - 10.1002/jsfa.8155
DO - 10.1002/jsfa.8155
M3 - Article
C2 - 27882566
AN - SCOPUS:85020455640
VL - 97
SP - 3133
EP - 3140
JO - Journal of the Science of Food and Agriculture
JF - Journal of the Science of Food and Agriculture
SN - 0022-5142
IS - 10
ER -