tailieunhanh - Báo cáo Y học: Isolation, enzymatic properties, and mode of action of an exo-1,3-b-glucanase from Trichoderma viride

An exo-1,3-b-glucanase has been isolated from cultural filtrate of Trichoderma viride AZ36. The N-terminal sequence of the purified enzyme (m ¼ 61 ^ 1 kDa) showed no significant homology to other known glucanases. The 1,3-b-glucanase displayed high activity against laminarins, curdlan, and 1,3-b-oligoglucosides, but acted slowly on 1,3-1,4-b-oligoglucosides. No significant activity was detected against high molecular mass 1,3-1,4-bglucans. The enzyme carried out hydrolysis with inversion of the anomeric configuration. Whereas only glucose was released from the nonreducing terminus during hydrolysis of 1,3-b-oligoglucosides, transient accumulation of gentiobiose was observed during hydrolysis of laminarins | Eur. J. Biochem. 268 6123-6131 2001 FEBS 2001 Isolation enzymatic properties and mode of action of an exo-1 3-p-glucanase from Trichoderma viride Anna A. Kulminskaya1 Karl K. Thomsen Konstantin A. Shabalin1 Irina A. Sidorenko1 Elena V. Eneyskaya1 Andrew N. Savel ev3 and Kirill N. Neustroev1 1 Petersburg Nuclear Physics Institute Russian Academy of Science Russia 2Carlsberg Laboratory Department of Physiology Copenhagen Denmark 3St Petersburg Technical University Biophysics Department Russia An exo-1 3-p-glucanase has been isolated from cultural filtrate of Trichoderma viride AZ36. The N-terminal sequence of the purified enzyme m 61 1 kDa showed no significant homology to other known glucanases. The 1 3-p-glucanase displayed high activity against laminarins curdlan and 1 3-p-oligoglucosides but acted slowly on 1 3-1 4-p-oligoglucosides. No significant activity was detected against high molecular mass 1 3-1 4-p-glucans. The enzyme carried out hydrolysis with inversion of the anomeric configuration. Whereas only glucose was released from the nonreducing terminus during hydrolysis of 1 3-p-oligoglucosides transient accumulation of gentiobiose was observed during hydrolysis of laminarins. The gentiobiose was subsequently degraded to glucose. The Michaelis constants Km and Vmax have been determined for the hydrolysis of 1 3-p-oligoglucosides with degrees of polymerization ranging from 2 to 6. Based on these data binding affinities for subsites were calculated. Substrate binding site contained at least five binding sites for sugar residues. Keywords exo-1 3-p-glucanase Trichoderma viride anomerity of hydrolysis. Enzymes hydrolyzing 1 3-p-D-glucans occur in a variety of organisms 1 . 1 3-p-Glucanases hydrolyze the O-glyco-sidic linkages of 1 3-p-linked glucans and are classified according to their mode of action. The exo-1 3-p-glucanases EC sequentially release glucose residues from the nonreducing terminus of a substrate while the endo-1 3-p-glucanases EC .

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