Activity of extracellular depolymerase secreted by Gliocladium solani strain during "Bionolle®"
Polimery 2008, No 6, 465
The range of activity of extracellular depolymerase secreted by Gliocladium solani strain (Fig. 2), isolated from the soil, was determined. The course of degradation of aliphatic "Bionolle®" polyester, type # 3001, under the influence of this enzyme (Table 1) was studied. Optimum pH value related to its maximal activity equals 5 (Fig. 1). It was found that the enzyme discussed shows wide range of hydrolytic activity, being active towards ester bonds of natural and synthetic polymers as well as towards ester derivatives of short- or long-chain fatty acids (Table 1). Depolymerase attacks better the amorphous phase of polymer than the crystalline one (Fig. 3). It preferentially caused hydrolysis of mainly adipate mers of polyester leaving succinate ones.
Key words: aliphatic polyester, degradation, depolymerase, Gliocladium solani, substrate specifity
S. Łabużek, B. Nowak, J. Pająk, G. Rymarz
Activity of extracellular depolymerase secreted by Gliocladium solani strain during "Bionolle®" polyester degradation