|
|
||||||||
University of Wisconsin,4 Madison 53706
Abstract
A summer sausage (fermented semi-dry variety) mix was prepared using a commercial formula, and myofibrillar and sarcoplasmic proteins were fractionated directly from it prior to any processing. The protein fractions were subjected to various combinations of acidity, salt and temperature. The sarcoplasmic proteins showed a 10% decrease in solubility during acidification alone, and an insolubilization of up to 60% when acidification was conducted in the presence of added NaCl. In contrast, the myofibrillar proteins decreased drastically in solubility at pH 5.7 to 40%, and then a further reduction occurred to 10% solubility at pH 4.4. Low salt concentrations (.33M) caused loss of solubility of myofibrillar proteins at a higher pH than if the protein were in .67 or 1.4M salt. Application of heat to low pH (4.8 to 5.3) solutions reduced the solubility of both protein fractions further than that caused by acidification without heat. The effects of pH were more reversible with the sarcoplasmic proteins than with the myofibrillar proteins.
1 Research supported by the College of Agricultural and Life Sciences, University of Wisconsin, Madison, and the Klement Sausage Co., Milwaukee, Wisconsin, Muscle Biology Laboratory Manuscript No. 62. Appreciation is expressed to R. Hapka and R. Tsai of the Product Control Laboratory, Klement Sausage Co. for their assistance and suggestions.
2 Present address: Klement Sausage Co., Milwaukee, Wisconsin.
4 Department of Meat and Animal Science.
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |