Iron (II)-chelating activity of buffalo αS-casein hydrolysed by corolase PP, alcalase and flavourzyme.
J Food Sci Technol
; 52(6): 3911-8, 2015 Jun.
Article
en En
| MEDLINE
| ID: mdl-26028776
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 Fe(2+/)mg protein) was found after 8 h of hydrolysis for H2 (267.56 µM Fe(2+/)mg protein) and H3 group of hydrolysates (380.68 µM Fe(2+/)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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