Abstract
The condition of immobilization of the partially purified levan fructotransferase and the properties of the immobilized enzyme was investigated. Levan fructotransferase was immobilized on ${\kappa}\;-carrageenan$ beads by entrapment method. The optimal ${\kappa}\;-carrageenan$ concentration was obtained 2%(w/v) (or the matrix. At that time, immobilized enzymes(0.81 units) have relative low activity compare with soluble enzyme(7.7 units). To immobilized and soluble enzyme, optimal activity temperature and pH were measured $55^{\circ}C$, 6.0 in sodium phosphate buffer 20mM solution. If crosslinking agent was added, proper concentration was 0.5%(v/v). At $37^{\circ}C$, immobilized and soluble enzyme converted levan to oligofructose and DFA IV, and the conversion ratio was 32% and 61% at 60 hr.
DFA IV를 생산하는 levan fructotransferase를 ${\kappa}\;-carrageenan$을 이용하여 고정화한 결과 카라기난의 농도가 2%일 때 가장 높은 활성을 나타내었다. 이 때에 고정화 담체에 포괄되어지는 효소의 활성도는 0.81 units으로서 soluble enzyme 7.7 units에 비해 상대적으로 낮은 활성을 보여주었다. 고정화 및 soluble enzyme의 최고 활성온도와 최적 pH는 동일하게 $55^{\circ}C$, pH6.0 이었다. 가교제를 처리할 경우에 적당한 농도는 0.5%로 생각되어진다. $37^{\circ}C$에서 시간에 따른 고정화 및 soluble enzyme의 DFA IV 생산량을 HPLC로 분석한 결과 60시간 이후의 전환률이 각각 32%, 61%로 나타났다.
