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Effect of heat treatment on the enzymatic stability of grass carp skin collagen and its ability to form fibrils in vitro
Author(s) -
Yang Huan,
Wang Haibo,
Zhao Yan,
Wang Haiyin,
Zhang Hanjun
Publication year - 2014
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.6724
Subject(s) - endothermic process , denaturation (fissile materials) , differential scanning calorimetry , chemistry , fibril , enzymatic hydrolysis , enthalpy , circular dichroism , thermal stability , size exclusion chromatography , enzyme , biophysics , chromatography , crystallography , biochemistry , nuclear chemistry , organic chemistry , thermodynamics , biology , physics , adsorption
BACKGROUND The molecular configuration, molecular weight distribution and thermal transition enthalpy (Δ H ) of grass carp skin ( GCS ) collagens after heat treatment under different conditions were measured using circular dichroism, gel filtration chromatography and differential scanning calorimetry ( DSC ). The enzymatic stability of collagen was evaluated using different enzymes, while the ability to form fibrils in vitro was assessed by morphological observation of collagen fibrils and turbidity testing. RESULTS The Δ H values, in‐solution molecular aggregation and the stability to enzymatic hydrolysis of GCS collagen decreased irreversibly and progressively with the duration of heat treatment at 33 °C, which was the onset endothermic temperature obtained from the DSC curve. A strong positive linear correlation between the enzymatic sensitivity of collagen and the degree of thermal denaturation was found. A decrease in fibril diameter and D‐periodicity length with denaturation could also be observed in the SEM and TEM images. CONCLUSION The onset endothermic temperature ( T o ) rather than the denaturation temperature ( T d ) is the threshold temperature for configurational stability of GCS collagen in acidic solution, and the biological properties would obviously change if the collagen was heat treated at this temperature. © 2014 Society of Chemical Industry