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- W2474885144 abstract "Major protein feactions of peanut, namely, arachln, conarachin II and conarachin I. were Isolated, from defattedRour to homogeneity, and succinylated to 84, 83 and 85% levels, respectively. The protein fractions were also hydrolyzedWith alpha-chymotrypsin. Succinylated peanut proteins exhibited minimum solubility in the pH range 3.0 - 4.0, awayfrom the range for unmodified proteiml. Enzyme treatment improved the solubility, except in the pH range 2.0 - 3.0and above pH B.O. Succlnylation improved the water and fat absorption capacities of all the protein fractions. Theemulsifying capacity and activity of succtnylated peanut protein fractions were higher than the unmodified fractions.The emulsifying capadty of enzyme-hydrolyzed fractions increased by 30-50%. The emulsifying activity also Increased.after hydrolysis with alpha-chymotrypsin. Foam stabilities of succinylated peanut protein fractions were found to beimproved. except for conarachln II. After hydrolysis with alpha-chymotrypsin, the foam capacity and stability of peanutprotein fractions Improved In eve!)' instance, Maximum Improvement of functional properties occurred after chemicaland enzymatic modifications of arachin, the major fraction. Thus, either chemical or enzymatic modification improvesthe functional attributes of peanut protein fractions." @default.
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- W2474885144 date "1996-01-01" @default.
- W2474885144 modified "2023-09-26" @default.
- W2474885144 title "Alteration of functional properties of peanut (Arachis hypogaea L.) protein fractions by chemical and enzymatic modifications." @default.
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