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Changes in the Melting Characteristics of Bovine Tendon Collagen Induced by a Bacterial Collagenase
Author(s) -
BERNAL V.M.,
STANLEY D.W.
Publication year - 1986
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.1365-2621.1986.tb13944.x
Subject(s) - collagenase , differential scanning calorimetry , denaturation (fissile materials) , chemistry , tendon , collagen fibril , microbial collagenase , proteolysis , achilles tendon , fibril , biophysics , biochemistry , chromatography , anatomy , nuclear chemistry , enzyme , biology , physics , thermodynamics
Differential scanning calorimetry was used to study the changes produced by a commercial Clostridium histolyticum collagenase preparation on the melting behavior of bovine Achilles tendon collagen. The samples were heated at 5°C/min from 25 to 100°C. As a result of proteolysis, the collagenase‐treated samples were partially gelatinized at 25°C and, during the calorimetric experiments, exhibited significant decreases in their melting transition parameters when compared to intact collagen. The denaturation temperatures and enthalpies obtained were 61.6°C and 44.4 J/g sample for intact collagen and 43.6°C and 26.1 J/g sample for collagenase‐treated collagen. These differences may be accounted for by changes produced in the structural organization of the collagen fibrils by the collagenase treatment.