Autolytic degradation of chicken intestinal proteins.
Data on the exhaustive degradation of chicken intestinal proteins by endogenous proteases, which could be utilized as a means to prepare protein hydrolysate, is reported in the present paper. Chicken intestine possesses proteolytic activities (cathepsin B, D, H, L, aminopeptidases and alkaline proteases) comparable to that in organ tissues like liver and spleen, which could degrade the tissue proteins extensively. The autolytic degradation was found to be optimum at pH 2.5 and 60 degrees C. Analysis by SDS-PAGE showed a time dependent degradation of proteins to low molecular weight (<10 kDa) products. Kinetic studies employing specific inhibitors indicated that the degradation (90-94%) of proteins at acidic pH is governed largely by pepstatin sensitive proteases. The acidic extract of the tissue was found to hydrolyse albumin, casein and soybean proteins efficiently. Results point to the possible application of tissue autolysis for obtaining protein hydrolysates from chicken intestine. Chicken intestine could also serve as a potential source of much needed proteolytic enzymes for food and pharmaceutical applications.
Jamdar
S N
SN
Food Technology Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400 085, India.
Harikumar
P
P
D000818:Animals; D001329:Autolysis / Q000378:metabolism*; D019149:Bioreactors; D002645:Chickens / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004798:Enzymes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007422:Intestines / Q000201:enzymology*; D007700:Kinetics; D011492:Protein Hydrolysates / Q000096:biosynthesis*; D011506:Proteins / Q000378:metabolism*; D030262:Soybean Proteins / Q000302:isolation & purification / Q000378:metabolism; D013696:Temperature
D004798:Enzymes; D011492:Protein Hydrolysates; D011506:Proteins; D030262:Soybean Proteins