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Nutritional Properties and Metabolic Studies of Acylated Beef Heart Myofibrillar Proteins
Author(s) -
EISELE T. A.,
BREKKE C. J.,
McCURDY S. M.
Publication year - 1982
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.1365-2621.1982.tb11023.x
Subject(s) - myofibril , casein , chemistry , biochemistry , hydrolysis , acetic anhydride , metabolism , hydrolyzed protein , food science , catalysis
Beef heart myofibrils were acylated with several concentrations of acetic (AA) and succinic (SA) anhydride, and digestibility and utilization of the myofibrillar proteins were determined. Results for in vitro hydrolysis of the untreated and acylated proteins varied, depending on the enzyme(s) used in the analysis. Rat protein efficiency ratios and net protein ratios for untreated (PER = 2.83, NPR = 116) and acetylked (PER = 2.55, NPR = 110) proteins were greater than for casein (PER = 2.50, NPR = 100), whereas values for succinylated proteins (PER = 2.36, NPR = 87) were less than for casein. Most of the radioactivity recovered after 24 hr from rats fed 14 C‐acylated myofibrillar proteins was in expired CO 2 ; 62.8% for 14 C‐acetylated and 45.8% for 14 C‐succinylated proteins. Rats acclimated to an acylated protein diet for 28 days showed improved metabolism of 14 C‐acetylated protein and decreased metabolism of 14 C‐succinylated proteins; 75.7% and 38.1% recovery as expired CO 2 , respectively.