title: Iron (II)-chelating activity of buffalo αS-casein hydrolysed by corolase PP, alcalase and flavourzyme.
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.
authors.affiliation: Dairy Chemistry Division, National Dairy Research Institute, Karnal, Haryana India.
authors.forename: Arvind
authors.initials: A
authors.lastname: Jaiswal
authors.affiliation: Dairy Chemistry Division, National Dairy Research Institute, Karnal, Haryana India.
authors.forename: Rajesh
authors.initials: R
authors.lastname: Bajaj
authors.affiliation: Dairy Chemistry Division, National Dairy Research Institute, Karnal, Haryana India.
authors.forename: Bimlesh
authors.initials: B
authors.lastname: Mann
authors.affiliation: Dairy Chemistry Division, National Dairy Research Institute, Karnal, Haryana India.
authors.forename: Kiran
authors.initials: K
authors.lastname: Lata
keywords: Enzymatic hydrolysis; Ferrozine; Iron (II)-chelating; Ultrafiltration; αs-casein