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Enzymatic extraction and characterisation of a thermostable collagen from swim bladder of rohu ( Labeo rohita )
Author(s) -
Gaurav Kumar Pal,
Nidheesh Thadathil,
Govindaraju Karadka,
Suresh Puthanveetil Velappan
Publication year - 2016
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.7884
Subject(s) - swim bladder , chemistry , fibril , extraction (chemistry) , scanning electron microscope , chromatography , fourier transform infrared spectroscopy , labeo , polyacrylamide gel electrophoresis , nuclear chemistry , biochemistry , enzyme , materials science , biology , fish <actinopterygii> , chemical engineering , fishery , engineering , composite material
BACKGROUND The fish swim bladder is considered as a potential source of realistic collagen. Currently, processing of the Indian major carp rohu ( Labeo rohita ) generates an enormous quantity of non‐edible by‐products, including swim bladders, which are discarded as waste with no commercial value. In the present study, collagen was prepared from rohu swim bladder and its physicochemical and fibril‐forming capacities were assessed. RESULTS The collagen isolated from rohu swim bladder was characterised as type I, containing α 1 and α 2 chains with triple helical structure by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, fourier transform infrared spectroscopy and amino acid analysis. The extracted collagen denaturation temperature was found to be 42.16 °C by differential scanning calorimetry analysis and also exhibited a high solubility in the presence of low NaCl concentrations (0–0.6 mol L −1 ). The extracted collagen exhibited a high fibril‐formation capacity at a NaCl concentration of 1.5 mol L −1 . Examination of the microstructure of collagen by scanning electron microscopy ( SEM ) showed a porous, sheet‐like film and a multilayered structure. The fibril formation capacity of collagen was also confirmed using SEM analysis. CONCLUSION The rohu swim bladder type I collagen was successfully extracted using an enzymatic method with a yield of 465.2 g kg −1 (dry weight basis) and was characterised as a well maintained triple helical structure. The extracted collagen exhibited a high fibril‐forming ability. The results of the present study confirm that utilisation of rohu swim bladder will open up a new avenue for the better disposal of by‐products and also help to minimise environmental pollution issues. © 2016 Society of Chemical Industry