Collect. Czech. Chem. Commun.
1983, 48, 2874-2878
https://doi.org/10.1135/cccc19832874
Immobilization of chymotrypsin (E.C.3.4.21.1), subtilisin (E.C.3.4.21.14) and neutral proteinase from Bacillus subtilis by covalent binding to benzoquinone-activated pearl cellulose
Helena Škachová and Jiří Kučera
Research Institute of Food Technology, 150 38 Prague 5
Abstract
Chymotrypsin (E.C.3.4.21.1), subtilisin (E.C.3.4.21.14), and a neutral proteinase from Bacillus subtilis were immobilized by covalent binding to benzoquinone-activated pearl cellulose. The yield of the immobilized protein was 55% in the case of chymotrypsin and 50% in the case of subtilisin and neutral proteinase from B. subtilis. The determination of activation energy at a low substrate concentration showed that the enzyme activity is limited by diffusion under these conditions. The activity yields are generally very good yet the activity of the enzymes immobilized is relatively low, most likely because of the presence of benzoquinone, as shown in experiments with the immobilization of chymotrypsin by the same technique on supports with different hydrophilicity.
