Studies on xylan degrading enzymes

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

“…have displayed optimal activity in the pH range of pH 4.0 to 5.5. 11,12) Regarding the -D-xylosidase, its optimal pH of 4.0 (Fig. 1B) is similar to that reported for the xylanolytic extract from P. funiculosum 21) and for the purified enzyme from Penicillium wortmanni,…”

“…9,10) In particular, Aspergillus and Trichoderma have been the most extensively studied as xylanase-producing fungi. [10][11][12] In our previous study, selected cellulases that were needed for the complete hydrolysis of the native cellulose to glucose were identified in the multienzymatic system produced by P. funiculosum, and their catalytic properties were characterized. 8) The overall objective of the present study is the characterization, in terms of pH, temperature, thermal stability and other kinetic properties, of selected hemicellulolytic activities expressed in the multi-enzymatic system from P. funiculosum, including endo-1,3-1,4--D-glucanase, endo-1,4--D-xylanase, -L-arabinofuranosidase and -D-xylosidase activities.…”

Cell Wall-associated 1,4- -D-Xylanase in Cryptococcus albidus var. aerius: in situ Characterization of the Activity

“…Similar results were obtained when purified walls (almost Xylanases in yeasts 421 free of P-xylosidase and glucanases) were used as the source of enzyme. These results suggested that the xylanase was an endo-splitting enzyme with a hydrolytic pattern similar to that described by Gorbacheva & Rodionova (1977) for an enzyme from Aspergillus niger able to break down xylans at random giving xylobiose > xylotriose > xylose as end-products.…”

Purification and Properties of Three Types of Xylanases Induced by Methyl β-Xyloside fromStreptomycessp.

“…X-I, X-II-A, and X-II-B had wider ranges of pH stability than those of known xylanases (pH 3.9 ± 1.2 "-I 8.0 ± 1.5). 3,24,[26][27][28][29][30][31][32] There was a strong similarity between X-II-A and X-II-B in chemical, physico-chemical, and enzymatic characters with a single exception of the isoelectric point. X-I was different from X-II-A and X-II-B in many respects, molecular weight, isoelectric point, and pH stability.…”