Immobilization of ATP on Bovine $\beta$- Caseins by Using Transglutaminase

효소법에 의한 ATP의 Bovine $\beta$-Casein에의 고정화

  • 윤세억 (전북대학교 농과대학 식품공학과) ;
  • 박선영김명곤 (전북대학교 농과대학 식품공학과 전북대학교 농과대학 식품공학과)
  • Published : 1990.11.01


ATP analogs were immobilized or bovine caseins by the action of transglutaminase. The ATP analogs immobilized on the caseins were enzymatically active and interconverten by kinases. The immobilized ATP was dephosphorylated to the corresponding ADP by hexokinase and rephosphorylated to the ATP in solid form by acetate kinase. Under the conditions chosen, about 55% of the immobilized ATP was dephosphorylated and about 80% of the resulted ADP was rephosphorylated. Bovine $\beta$-casein was more useful than $\alpha$sf-casein as a carrier and C8-substituted ATP analognwas more effective than N6-substituted one in immobilization. Michaelis constant of C8-substituted ATP analog immobilized on $\beta$-casein was similar to that of free form of ATP and that of ATP analog. The immobilized ATP was much more stable than free ATP and its analog, while maximum velocity was reduced to 37% of the free ATP analog. The immobilized ATP was recovered almost completely by calcium precipitation.