earticle

영어

The kinetic characteristics of an invertase immobilized covalently on porous silica have been appraised for the applicability of porous silica to immobilization supports of enzymes. The invertase was covalently bound with glutaraldehyde on 3-aminopropyltriethoxy-silane-activated porous silica to give a maximum loading of 120mg invertase per 1 gram of dry silica and 26.9 to 70.2% retention of original activity. The porous structure of silica seems to be suitable for enzyme immobilization, judging from the observed results of high immobilization capacity and comparably satisfactory retention of enzyme activity.

한국어

고정화단체로 제조된 다공성실리카를 3-aminopropyl-triethoxysilaneacetone 용액으로 표면처리하고 glutaraldehyde로 전화당효소를 공유결합시켜 진화당효소의 고정 화함량과 고정화활성도를 평가한 겨로가, 고정화함량 1200mg/ g, 활성도 26.9~ 70.2%로 우수한 고정화특성은 나타내였으며, 다상성살리카가 고정화담체로 활용되기 위한 구조직 특성을 가진 것으로 평가된다.