PMID: 8948426Jun 15, 1995Paper

Purification and characterization of three extracellular (1-->3)-beta-D-glucan glucohydrolases from the filamentous fungus Acremonium persicinum

The Biochemical Journal
S M PitsonB A Stone

Abstract

Three (1-->3)-beta-D-glucanases (GNs) were isolated from the culture filtrates of the filamentous fungus Acremonium persicinum and purified by (NH4)2SO4 precipitation followed by anion-exchange and gel-filtration chromatography. Homogeneity of the purified proteins was confirmed by SDS/PAGE, isoelectric focusing and N-terminal amino acid sequencing. All three GNs (GN I, II and III) are non-glycosylated, monomeric proteins with apparent molecular masses, estimated by SDS/PAGE, of 81, 85 and 89 kDa respectively. pI values for the three enzymes are 5.3, 5.1, and 4.4 respectively. The pH optimum for GN I is 6.5, and 5.0 for GN II and III. All three purified enzymes displayed stability over the pH range 4.5-10.0. Optimum activities for GN I, II and III were recorded at 65, 55 and 60 degrees C respectively, with both GN II and III having short-term stability up to 50 degrees C and GN I up to 55 degrees C. The purified GNs have high specificity for (1-->3)-beta-linkages and hydrolysed a range of (1-->3)-beta- and (1-->3)(1-->6)-beta-D-glucans, with laminarin from Laminaria digitata being the most rapidly hydrolysed substrate of those tested. K(m) values for GN I, II, and III against L. digitata laminarin were 0.1, 0.23 and 0.22 mg/ml ...Continue Reading

Citations

Feb 23, 2007·FEMS Microbiology Reviews·Kirstee MartinRobert J Seviour
Dec 6, 2001·European Journal of Biochemistry·A A KulminskayaK N Neustroev
Feb 5, 1998·Nature·P LoetscherJ M Dayer
Jul 25, 2007·FEMS Microbiology Letters·Türkân SakinçSören G Gatermann
Jul 15, 2020·International Journal of Biological Macromolecules·Roza V UsoltsevaSvetlana P Ermakova

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