ABSTRACT
Fungal strains degrading plant biomass available from the Russian National Collection of Industrial Microorganisms (VKPM) have been screened for the xyloglucanase activity. Under conditions of submerged cultivation, the thermophilic strains Sporotrichum thermophile VKPM F-972, Myceliophthora thermophila VKPM F-244, and Sporotrichum pruinosum VKPM F-235 produced extracellular xyloglucanases with optimal activity at 60°C, pH 5.0. 88-100% of the initial enzyme activity was retained after l-h incubation at 50°C; 79-84% of the activity was retained after l-h incubation at 60°C. S. thermophile VKPM F-972, M. thermophila VKPM F-244, and S. pruinosum VKPM F-235 strains may be used as the gene sources for construction of highly active producers of the thermostable xyloglucanases.
Subject(s)
Fungal Proteins/chemistry , Glycoside Hydrolases/chemistry , Hot Temperature , Sordariales/enzymology , Sporothrix/enzymology , Enzyme Stability , Fungal Proteins/metabolism , Glycoside Hydrolases/metabolism , RussiaABSTRACT
Electrophoretically homogeneous proteolytic enzyme with molecular weight 31,500 and pI 3.75 was obtained from a culture medium of Streptomyces 771 by chromatography on N-benzyl chitin adsorbent, subsequent chromatography on CM-cellulose, and preparative isofocusing and chromatography on Sephadex G-75. The enzyme hydrolyzes N-benzoyl-DL-arginine-p-nitroanilide N-benzoyl-DL-lysine-p-nitro-anilide N-benzoyl-DL-arginine ethyl ester, and Na-caseinate. It also exhibits pronounced thrombolytic activity. The activity of the enzyme was suppressed by soya bean inhibitor, but remained unaffected by chelating agents and phenylmethylsulfonyl fluoride. The enzyme was immobilized on aldehyde dextran, and some kinetic parameters of the immobilized enzyme were determined. The thrombolytic activity of native and immobilized enzyme was studied as well.
