ENZYMATIC RECOVERY OF COD FRAME PROTEINS WITH CRUDE PROTEINASE FROM TUNA PYLORIC CECA

To recover efficiently proteins from fish frame that is remained on bo ne portions after filleting fish in fish processing manufactory, the e nzymatic recovery by hydrolysis was applied. The enzyme was a crude pr oteinase partially purified from tuna Thunnus thynnus pyloric caeca. T una pyloric caeca crude proteinase (TPCCP) showed the highest hydrolyt ic activity for BAEE (N-benzoyl-L-arginine ethyl ester), synthetic sub strate of trypsin. The optimum activity condition of TPCCP for fish (c od; Gadus macrocephalus) frame proteins, the deboned proteins isolated from fish frame, was known as pH 10 at 45-50 degrees C. The hydrolysi s reaction for cod frame by TPCCP was attained to an end after 12 h in cubation in the above condition. Under the optimum reaction conditions for the same enzyme concentration, the degree of hydrolysis by TPCCP on time course was similar to those by purified proteinases such as ch ymotrpysin, pronase E, papain, etc. After the cod frame was treated wi th TPCCP for 12 h at 50 degrees C, all tissues, mainly muscle proteins , were readily digested from fish bone and approximately 80% of the to tal soluble protein was hydrolyzed. Therefore, it appeared that the pr otein from fish frame as fish processing waste could be efficiently re covered with TPCCP.