Preparation and characterization of iron-chelating peptides from whey protein: An alternative approach for chemical iron fortification

• Published in: Food research international 2021-03, Vol.141, p.110133-110133, Article 110133
• Main Authors: Athira, S., Mann, Bimlesh, Sharma, Rajan, Pothuraju, Ramesh, Bajaj, Rajesh Kumar
• Format: Article
• Language: English
• Subjects: Antioxidant property; Dietary iron supplement; Enzymolysis; Iron-chelating peptides; Whey proteins
• ISSN: 0963-9969; 1873-7145
• DOI: 10.1016/j.foodres.2021.110133

[Display omitted] •Whey protein derived peptides exhibited iron chelating ability.•Structural transformation observed in FTIR spectra of peptide-iron complex.•Chelation reduced the zeta potential and antioxidant property of peptides.•Size of chelated peptide sequence ranged from 275 to 1916 Da.•81% of identified peptide sequences contain glutamic and aspartic acid. Iron fortification of staple food is a strategy utilized worldwide to address the concern of dietary iron deficiency. However, traditional salt-based fortification methods have limitations with gastrointestinal stability and bioavailability. Iron chelating peptides from easily available and scalable proteins such as whey protein have been proposed as promising candidates to circumvent the above mentioned limitations by enhancing iron absorption and bioavailability. In this study, we report methods to produce whey protein derived iron-chelating peptides and describe their physicochemical characteristics. Peptides derived from whey proteins prepared by ultrafiltration of whey followed by hydrolysation were iron chelated to produce peptide-iron complexes. These complexes had a size of 422.9 ± 3.41 nm, chelated iron content of 36.42 µg/ mg protein, and a low zeta potential (−10.80 mV) compared to whey peptides. Spectra analysis using ultraviolet–visible absorption and Fourier transform infrared spectroscopy showed structural transformation indicating iron chelation. Mass spectrometric analysis using LC-MS/MS confirmed the presence of both hydrophilic and hydrophobic peptides in the complexes with sizes ranging from 275 Da to 1916 Da. Furthermore, reduction in the antioxidant property of peptides following iron complexing indicates iron chelation. Our results suggest that whey protein derived peptide-iron complexes can be used as a potential alternative for chemical iron fortificants for food products and also as iron supplements.