Dinçer Ayse, Okutucu Burcu, Zihnioğlu Figen, Telefoncu Azmi
a Ege University, Faculty of Science, Biochemistry Department , Bornova , Izmir , Turkey.
Prep Biochem Biotechnol. 2005;35(2):103-111. doi: 10.1081/PB-200054695.
Crude α-glucosidase from Baker's yeast was immobilized in polygalacturonic acid beads and coated with chitosan. Chemical and physical characterization were performed by using p-nitrophenyl-α-D-glucopyranoside (pNPG) as an artificial substrate. Operation, thermal, pH, and strorage stabilities of the free and immobilized enzyme were also examined. The stabilities of immobilized enzyme were found to be better than that of the free enzyme. Furthermore, the hydrolysis rate of the chitosan coated α-glucosidase polygalacturonic acid beads were studied. In conclusion, the enzyme beads appear to have good characteristics and offer the prospect that this system may find application in enzyme immobilization, in addition to controlled drug release studies.
将面包酵母中的粗α-葡萄糖苷酶固定在聚半乳糖醛酸珠中，并用壳聚糖包被。以对硝基苯基-α-D-吡喃葡萄糖苷（pNPG）作为人工底物进行化学和物理表征。还研究了游离酶和固定化酶的操作稳定性、热稳定性、pH稳定性及储存稳定性。发现固定化酶的稳定性优于游离酶。此外，还研究了壳聚糖包被的α-葡萄糖苷酶聚半乳糖醛酸珠的水解速率。总之，酶珠似乎具有良好的特性，并且除了控释药物研究外，还为该系统在酶固定化中的应用提供了前景。
