[Properties of immobilized acid proteinase from Aspergillus awamori]. / Issledovanie svoistv immobilizovannoi kisloi proteinazy iz Aspergillus awamori.

pH-optimum, thermal stability and storage stability of immobilized acid proteinase from Aspergillus awamori obtained by covalent binding on silochrome through glutaraldehyde were studied. Acid proteinase immobilization was found to shift towards the acid range by a unit. Thermal stability of the immobilized preparation was lower than that of the native enzyme.

[Optimization of immobilization conditions for acid proteinase from Aspergillus awamori]. / Optimizatsiia uslovii immobilizatsii kisloi proteinazy iz Aspergillus awamori.

To optimize the immobilization conditions for acid proteinase from Aspergillus awamori by covalent binding through glutaraldehyde, experiments were carried out using the Box-Wilson method. The optimization process was assessed on the basis of absolute activity A, coefficient of activity retention gamma and their product A gamma. The following conditions can be recommended: glutaraldehyde concentration 50--60 mg/g, enzyme concentration not less than 40 mg/g, time of glutaraldehyde treatment 2--2.5 hrs, immobilization time 2 hrs, pH about 4.0, and temperature 35--40 degrees C. Under these conditions A=220--230 U/g, gamma = 23--24% Agamma = 5,000--6,000.