TY - JOUR
T1 - Fractionation and identification of antioxidant peptides from an enzymatically hydrolysed Palmaria palmata protein isolate
AU - Harnedy, Pádraigín A.
AU - O'Keeffe, Martina B.
AU - FitzGerald, Richard J.
N1 - Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2017/10
Y1 - 2017/10
N2 - Proteins derived from the macroalgal species Palmaria palmata have emerged as potential substrates for the generation of bioactive peptides. The aim of this study was to fractionate, identify and characterize antioxidant peptides from a P. palmata protein hydrolysate. The P. palmata protein hydrolysate generated with the food-grade proteolytic enzyme Corolase PP was sequentially fractionated using solid phase extraction and semi-preparative (SP) RP-HPLC. The most active SP-RP-HPLC peptide fraction (SP-RP-HPLC-30-F26) was analysed by ESI-MS/MS. Seventeen novel peptide sequences were identified in this fraction. Of the peptides selected for synthesis, Ser-Asp-Ile-Thr-Arg-Pro-Gly-Gly-Asn-Met, showed the highest oxygen radical absorbance capacity (ORAC) and ferric reducing antioxidant power (FRAP) activity with values of 152.43 ± 2.73 and 21.23 ± 0.90 nmol TE/μmol peptide, respectively. The results presented herein indicate that P. palmata derived peptides may have potential applications as health enhancing ingredients and as food preservatives due to their antioxidant activity.
AB - Proteins derived from the macroalgal species Palmaria palmata have emerged as potential substrates for the generation of bioactive peptides. The aim of this study was to fractionate, identify and characterize antioxidant peptides from a P. palmata protein hydrolysate. The P. palmata protein hydrolysate generated with the food-grade proteolytic enzyme Corolase PP was sequentially fractionated using solid phase extraction and semi-preparative (SP) RP-HPLC. The most active SP-RP-HPLC peptide fraction (SP-RP-HPLC-30-F26) was analysed by ESI-MS/MS. Seventeen novel peptide sequences were identified in this fraction. Of the peptides selected for synthesis, Ser-Asp-Ile-Thr-Arg-Pro-Gly-Gly-Asn-Met, showed the highest oxygen radical absorbance capacity (ORAC) and ferric reducing antioxidant power (FRAP) activity with values of 152.43 ± 2.73 and 21.23 ± 0.90 nmol TE/μmol peptide, respectively. The results presented herein indicate that P. palmata derived peptides may have potential applications as health enhancing ingredients and as food preservatives due to their antioxidant activity.
KW - Antioxidant
KW - Antioxidant peptide
KW - Bioactive peptide
KW - Food protein hydrolysates
KW - Palmaria palmata
KW - Peptide identification
KW - Simulated gastrointestinal digestion
UR - http://www.scopus.com/inward/record.url?scp=85025163723&partnerID=8YFLogxK
U2 - 10.1016/j.foodres.2017.07.037
DO - 10.1016/j.foodres.2017.07.037
M3 - Article
C2 - 28873704
AN - SCOPUS:85025163723
SN - 0963-9969
VL - 100
SP - 416
EP - 422
JO - Food Research International
JF - Food Research International
ER -