Laurinavichius V A, Kulis Iu Iu
Prikl Biokhim Mikrobiol. 1977 May-Jun;13(3):443-8.
The immobilization of alpha-chymotrypsin, trypsin and invertase on hydrated oxides of tin, titanium and aluminium was investigated. The degree at which the enzymes were bound upon immobilization was 83.2-2.6%. The amount of bound proteins was 64.2 mg/g carrier. The specific activity of enzymes reached the highest level in the case of hydrated tin oxide and amounted to 76.8%, 49.9% and 99.6%, of activity of native alpha-chymotrypsin, trypsin and invertase, respectively. The thermal stability of immobilized proteases was considerably higher and that of immobilized invertase was significantly lower than that of native enzymes. The pH optimum of immobilized enzymes shifted by 0.6-2.6 units towards the alkaline region.
研究了α-糜蛋白酶、胰蛋白酶和转化酶在水合氧化锡、氧化钛和氧化铝上的固定化情况。酶在固定化时的结合程度为83.2 - 2.6%。结合蛋白质的量为64.2 mg/g载体。在水合氧化锡的情况下，酶的比活性达到最高水平，分别相当于天然α-糜蛋白酶、胰蛋白酶和转化酶活性的76.8%、49.9%和99.6%。固定化蛋白酶的热稳定性显著更高，而固定化转化酶的热稳定性明显低于天然酶。固定化酶的最适pH向碱性区域偏移了0.6 - 2.6个单位。
