|
|
||||||||
U. S. Department of Agriculture, Beltsville, Maryland 20705
Abstract
Bovine muscle glycogen isolated by cold-water extraction was hydrolyzed more slowly by phosphorylase and less completely by phosphorylase plus glucosidase than that isolated by KOH- or TCA-extraction. Although removal of much of the contaminating protein from cold-water-extracted glycogen moderately increased its enzymatic digestibility, the digestibility was still not as great as that for KOH- or TCA-extracted glycogen. Of the three glycogens tested, degree of branching was greatest for glycogen extracted by cold water. Although the evidence strongly suggests that bovine glycogen molecule extracted by cold water is the most complex and natural, a definitive conclusion must await further investigation.
1 Portions of this paper were presented at the American Society of Animal Science Annual Meeting, 1969 and 1970.
2 Market Quality Research Division, Agricultural Research Service.
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |