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LOW‐TEMPERATURE, LONG‐TIME HEATING OF BOVINE MUSCLE 3. Collagenolytic Activity
Author(s) -
LAAKKONEN E.,
SHERBON J. W.,
WELLINGTON G. H.
Publication year - 1970
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.1365-2621.1970.tb12133.x
Subject(s) - collagenase , chemistry , polyacrylamide gel electrophoresis , enzyme , electrophoresis , biochemistry , fraction (chemistry) , chromatography , food science
SUMMARY: Naturally occurring collagenolytic activity was found in the water‐soluble fraction of bovine muscle. General proteolytic activity determined with Azocoll indicated that this total activity was much greater than the collagenase activity specifically determined according to the method of Wünsch and Heidrich. The collagenase fraction was concentrated by polyacrylamide gel electrophoresis and the activity of the enzyme was studied under various pH and temperature conditions. This collagenase could remain active in the meat at cooking temperatures experienced in long‐time, low‐temperature cooking, < 60°C. With faster heating and higher internal temperatures, > 70‐80°C, the collagenase observed in this study is inactivated.

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