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Iron (II)-chelating activity of buffalo αS-casein hydrolysed by corolase PP, alcalase and flavourzyme

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Abstract

Iron is a vital substance for human health which participates in many biochemical reactions. It also act as initiator for many harmful oxidative process. Buffalo αS-casein enriched fraction (80 %) was hydrolysed independently by corolase PP (H1), alcalase (H2), flavourzyme (H3) and sequentially by alcalase-flavourzyme (H4). After ultrafiltration (10 and 3 kDa) hydrolysates were analysed for their iron chelation activity using ferrozine. For H1 group of hydrolysates highest iron (II)-chelation activity (265.58 μM Fe2+/mg protein) was found after 8 h of hydrolysis for H2 (267.56 μM Fe2+/mg protein) and H3 group of hydrolysates (380.68 μM Fe2+/mg protein) after 6 h of hydrolysis. Sequential hydrolysis was not effective for iron (II)-chelation activity. 3 kDa fractions show higher iron (II)-chelation activity than 10 kDa fraction. Flavourzyme was more effective for generation of iron (II)-chelating peptides from buffalo αS-casein.

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Acknowledgments

We are thankful to our Director, Vice Chancellor of National Dairy Research Institute (Deemed University), Karnal, Haryana for providing facilities and encouragement. We also thank to Novozymes South Asia Pvt Ltd, Bangalore and AB enzymes for their gifted enzymes.

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Authors and Affiliations

  1. Dairy Chemistry Division, National Dairy Research Institute, Karnal, Haryana, India

    Arvind Jaiswal, Rajesh Bajaj, Bimlesh Mann & Kiran Lata

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  1. Arvind Jaiswal
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  4. Kiran Lata
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Correspondence to Arvind Jaiswal.

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Jaiswal, A., Bajaj, R., Mann, B. et al. Iron (II)-chelating activity of buffalo αS-casein hydrolysed by corolase PP, alcalase and flavourzyme. J Food Sci Technol 52, 3911–3918 (2015). https://doi.org/10.1007/s13197-014-1626-x

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  • DOI: https://doi.org/10.1007/s13197-014-1626-x

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