[Carboxylic proteinase from Trichoderma lignorum].
A carboxylic proteinase has been isolated from a commercial preparation of Trichoderma lignorum used as a source of cellulolytic enzymes. The purification procedure included precipitation by (NH4)2SO4 (65% saturation), gel-filtration through Acrylex P-10, affinity chromatography on gramicidin S bound to an inorganic matrix, gel-filtration through Acrylex P-10, affinity chromatography on bacitracin-Sepharose and separation on Ultrogel AcA 54 followed by gel-filtration through Sephadex G-50. A 400-fold purification of enzyme was achieved, the enzyme yield being 7,2%. The molecular weight of carboxylic proteinase as determined by gel-filtration is 33 000; its amino acid composition is found to be similar to that of carboxylic proteinases isolated from other fungal species. The enzyme is stable within the pH range of 3,0-6,0. The enzyme was fully inhibited by the specific inhibitors of carboxyliec proteinases-N-diazoacetyl-N'-2,4-dinitrophenylethylenediamine and pepstatin.
D000596:Amino Acids / Q000032:analysis; D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D013045:Species Specificity; D014242:Trichoderma / Q000201:enzymology*
D000596:Amino Acids; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases
Karboksil'naia proteinaza iz Trichoderma lignorum.