title: Generation, Fractionation, and Characterization of Iron-Chelating Protein Hydrolysate from Palm Kernel Cake Proteins.
abstract: Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtilisin, flavourzyme, trypsin, chymotrypsin, and pepsin to generate different protein hydrolysates. Peptide content and iron-chelating activity of each hydrolysate were evaluated using O-phthaldialdehyde-based spectrophotometric method and ferrozine-based colorimetric assay, respectively. The results revealed a positive correlation between peptide contents and iron-chelating activities of the protein hydrolysates. Protein hydrolysate generated by papain exhibited the highest peptide content of 10.5 mM and highest iron-chelating activity of 64.8% compared with the other hydrolysates. Profiling of the papain-generated hydrolysate by reverse phase high performance liquid chromatography fractionation indicated a direct association between peptide content and iron-chelating activity in most of the fractions. Further fractionation using isoelectric focusing also revealed that protein hydrolysate with basic and neutral isoelectric point (pI) had the highest iron-chelating activity, although a few fractions in the acidic range also exhibited good metal chelating potential. After identification and synthesis of papain-generated peptides, GGIF and YLLLK showed among the highest iron-chelating activities of 56% and 53%, whereas their IC50 were 1.4 and 0.2 μM, respectively.
authors.affiliation: Dept. of Food Science, Faculty of Food Science and Technology, Univ. Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia.|Dept. of Food Science and Technology, College of Agriculture and Natural Resources, Islamic Azad Univ, Sanandaj Branch, Sanandaj, Iran.
authors.forename: Mohammad
authors.initials: M
authors.lastname: Zarei
authors.affiliation: Dept. of Food Science, Faculty of Food Science and Technology, Univ. Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia.
authors.forename: Rahele
authors.initials: R
authors.lastname: Ghanbari
authors.affiliation: Dept. of Food Science, Faculty of Food Science and Technology, Univ. Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia.
authors.forename: Naser
authors.initials: N
authors.lastname: Tajabadi
authors.affiliation: Dept. of Food Science, Faculty of Food Science and Technology, Univ. Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia.
authors.forename: Azizah
authors.initials: A
authors.lastname: Abdul-Hamid
authors.affiliation: Dept. of Food Science, Faculty of Food Science and Technology, Univ. Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia.
authors.forename: Fatimah Abu
authors.initials: FA
authors.lastname: Bakar
authors.affiliation: Dept. of Food Science, Faculty of Food Science and Technology, Univ. Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia.
authors.forename: Nazamid
authors.initials: N
authors.lastname: Saari
mesh_terms: D028023:Arecaceae / Q000737:chemistry*; D005591:Chemical Fractionation; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D007501:Iron / Q000378:metabolism*; D007502:Iron Chelating Agents / Q000737:chemistry / Q000494:pharmacology*; D007526:Isoelectric Point; D010206:Papain / Q000378:metabolism*; D010434:Pepsin A / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000032:analysis / Q000494:pharmacology*; D010940:Plant Proteins / Q000737:chemistry*; D011492:Protein Hydrolysates / Q000737:chemistry / Q000494:pharmacology*; D013053:Spectrophotometry; D013381:Subtilisins / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism; D009764:o-Phthalaldehyde
chemical_list: D007502:Iron Chelating Agents; D010455:Peptides; D010940:Plant Proteins; D011492:Protein Hydrolysates; D009764:o-Phthalaldehyde; D007501:Iron; D010450:Endopeptidases; D010447:Peptide Hydrolases; C412470:flavourzyme; D013381:Subtilisins; D014357:Trypsin; D010206:Papain; D010434:Pepsin A
keywords: chelating activity; palm kernel cake; peptide; protein hydrolysate