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Preparation of succinylated yeast protein: Composition and solubility
Author(s) -
Vananuvat P.,
Kinsella John E.
Publication year - 1978
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260200903
Subject(s) - succinylation , isoelectric point , solubility , succinic anhydride , yeast , chemistry , chromatography , biochemistry , amino acid , organic chemistry , lysine , enzyme
Abstract A method for the succinylation of yeast Proteins during their isolation is described. Some factor affecting the extent of succinylation are described, e.g., heating of protein (80°C for 5 min) prior to dervatization reduced maximum succinylation of available ε‐amino groups from 88 to 54%. Succinylation of amino groups progressively increased as the concentration of succinic anhydride was increased and there was a concomitant decrease in nucleic acid content of the precipitated protein concentrate from 12.5 to 5.3 for 0 and 88% succinylation, respectively, succinylation enhanced the solubility of the protein concentrates particularly below pH 7 and it decreased the isoelectric point pH. 4.5 to 4.0.