Melo J S, D'Souza S F
Food Technology and Enzyme Engineering Division, Bhabha Atomic Research Centre, Bombay, India.
Appl Biochem Biotechnol. 1992 Jan-Mar;32:159-70. doi: 10.1007/BF02922156.
Yeast invertase, a glycoprotein, was covalently coupled to Ocimum basilicum seeds either through its protein or carbohydrate moiety. Of the various methods investigated, binding of the enzyme through its carbohydrate moiety resulted in the retention of considerably higher amounts of enzyme activity. Immobilized invertase showed a shift in the pH optimum toward the alkaline side without appreciable change in temperature optimum. However, the immobilized preparation was more thermostable than the free enzyme. Invertase bound to the seeds could be used repeatedly for the hydrolysis of sucrose syrups in a batch process without appreciable loss in activity. The seeds could serve as an inexpensive, ready-to-use, natural pellicular polysaccharide support for immobilizing enzymes.
酵母转化酶是一种糖蛋白，它通过其蛋白质或碳水化合物部分与罗勒种子共价偶联。在所研究的各种方法中，通过其碳水化合物部分结合酶导致保留了相当高的酶活性。固定化转化酶的最适pH向碱性侧移动，而最适温度没有明显变化。然而，固定化制剂比游离酶更耐热。结合到种子上的转化酶可以在分批过程中重复用于蔗糖糖浆的水解，而活性没有明显损失。这些种子可以作为一种廉价、即用型的天然膜状多糖载体来固定酶。
