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 3kDa) hydrolysates were analysed for their iron chelation activity using ferrozine. For H1 group of hydrolysates highest iron (II)-chelation activity (265.58μM Fe(2+/)mg protein) was found after 8h of hydrolysis for H2 (267.56μM Fe(2+/)mg protein) and H3 group of hydrolysates (380.68μM Fe(2+/)mg protein) after 6h of hydrolysis. Sequential hydrolysis was not effective for iron (II)-chelation activity. 3kDa fractions show higher iron (II)-chelation activity than 10kDa fraction. Flavourzyme was more effective for generation of iron (II)-chelating peptides from buffalo αS-casein.
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