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PARAMETERS OF TEXTURE CHANGE IN PROCESSED FISH: CROSS‐LINKAGE OF PROTEINS

PARAMETERS OF TEXTURE CHANGE IN PROCESSED FISH: CROSS‐LINKAGE OF PROTEINS Soluble myosin and insoluble protein (i. e., soluble only in 5 % sodium dodecyl sulfate) were obtained from fresh and processed Sacramento blackfish and analyzed for the existence of possible cross‐links. Free sulfhydryl groups decreased somewhat in freezing and more in frozen storage. None were present after dehydration or cooking nor in any insoluble fractions, so that presumably these were oxidized in the formation of cross‐links. Ester bonds were much more numerous in insoluble protein than in soluble myosin, but their relative content was not clearly related to processing. Aldehyde groups decreased in myosin after cooking and dehydration, and were absent from insoluble protein. The presumptive Schiff base content was somewhat greater in soluble protein than in myosin and appeared to increase upon freezing and dehydration. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Texture Studies Wiley

PARAMETERS OF TEXTURE CHANGE IN PROCESSED FISH: CROSS‐LINKAGE OF PROTEINS

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References (22)

Publisher
Wiley
Copyright
Copyright © 1970 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-4901
eISSN
1745-4603
DOI
10.1111/j.1745-4603.1970.tb00746.x
Publisher site
See Article on Publisher Site

Abstract

Soluble myosin and insoluble protein (i. e., soluble only in 5 % sodium dodecyl sulfate) were obtained from fresh and processed Sacramento blackfish and analyzed for the existence of possible cross‐links. Free sulfhydryl groups decreased somewhat in freezing and more in frozen storage. None were present after dehydration or cooking nor in any insoluble fractions, so that presumably these were oxidized in the formation of cross‐links. Ester bonds were much more numerous in insoluble protein than in soluble myosin, but their relative content was not clearly related to processing. Aldehyde groups decreased in myosin after cooking and dehydration, and were absent from insoluble protein. The presumptive Schiff base content was somewhat greater in soluble protein than in myosin and appeared to increase upon freezing and dehydration.

Journal

Journal of Texture StudiesWiley

Published: Nov 1, 1970

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