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Chemical Modification and Functional Properties of Acylated Beef Heart Myofibrillar Proteins
Author(s) -
EISELE T. A.,
BREKKE C. J.
Publication year - 1981
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1981.tb02999.x
Subject(s) - chemistry , succinic anhydride , acetic anhydride , solubility , myofibril , acylation , lysine , chemical modification , threonine , emulsion , succinylation , potassium , organic chemistry , serine , nuclear chemistry , biochemistry , amino acid , enzyme , catalysis
Beef heart myofibrils were acylated with 0.1, 0.3, 0.6, 0.8, 1.0, 1.5, 2.0, 3.0, and 5.0 mmoles anhydride/g protein, at pH 8.0–8.5 and 2–3°C, with acetic anhydride (AA), succinic anhydride (SA), cis,cis,cis,cis‐tetrahydrofuran‐2,3,4,5‐tetracarboxylic dianhydride (FA), and 1,2,4‐benzenetricarboxylic anhydride (BA). The anhydride reacted with e‐amino groups of lysine, sulfhydryl groups, and hydroxyl groups of tyrosine, serine, and threonine. Chemically modified beef heart myofibriliar proteins were superior to native heart myofibriliar proteins in solubility, emulsifying capacity, emulsion activity, and emulsion stability in a low salt solution of 0.1M NaCl, 0.05M potassium phosphate at pH 7.4 and 6.0. Protein modified with 0.5 mmole anhydride/g protein in 0.2M NaCl had a solubility greater than unmodified proteins in 0.6M NaCl at pH 7.4. Chemical modification also altered the pH‐solubility profile. The chemically modified beef heart myofibrillar proteins exhibited an emulsifying capacity at pH 6.0 and 7.4 that was greater than that of the native proteins at pH 7.4. The recommended extent of acylation for modifying beef heart myofibrils on a gram protein basis is 0.6 mmole AA, 1.5 moles SA, 0.6 mmole FA, and 0.6 mmole BA.