Purification and some properties of a xylanase from Aspergillus sydowii MG49.
نویسندگان
چکیده
Aspergillus sydowii MG49 produces a 30-kDa exosplitting xylobiohydrolase during growth on xylan. A specific chemical modification and substrate protection analysis of purified xylanase provided evidence that tryptophan and carboxy and amino groups are present at the catalytic site of this enzyme. Thermal inactivation of the xylanase occurs because of irreversible polymolecular aggregation, which is slower in the presence of glycerol.
منابع مشابه
Thermotolerant and mesophylic fungi from sugarcane bagasse and their prospection for biomass-degrading enzyme production
Nineteen fungi and seven yeast strains were isolated from sugarcane bagasse piles from an alcohol plant located at Brazilian Cerrado and identified up to species level on the basis of the gene sequencing of 5.8S-ITS and 26S ribosomal DNA regions. Four species were identified: Kluyveromyces marxianus, Aspergillus niger, Aspergillus sydowii and Aspergillus fumigatus, and the isolates were screene...
متن کاملXylanase Production under Solid State Fermentation by Aspergillus niger
Central composite orthogonal design was applied to quantify relations of xylanase production, loss of dry matter and change of pH with four critical variables during solid state fermentation of a mixture of wheat bran and wheat straw on which Aspergillus niger CCUG 33991 was cultivated. The studied variables included the percentage of wheat straw, temperature, moisture content, and fermentati...
متن کاملPurification, biochemical characterization and structural modelling of alkali-stable β-1,4-xylan xylanohydrolase from Aspergillus fumigatus R1 isolated from soil
BACKGROUND Aspergillus fumigatus R1 produced xylanase under submerged fermentation which degrades the complex hemicelluloses contained in agricultural substrates. Xylanases have gained considerable attention because of their tremendous applications in industries. The purpose of our study was to purify xylanase and study its biochemical properties. We have predicted the secondary structure of pu...
متن کاملPurification and Characterization of a Low Molecular Weight Xylanase from Solid-state Cultures of Aspergillus Fumigatus Fresenius
A xylan-degrading enzyme (xylanase II) was purified to apparent homogeneity from solid-state cultures of Aspergillus fumigatus Fresenius. The molecular weight of xylanase II was found to be 19 and 8.5 kDa, as estimated by SDS-PAGE and gel filtration on FPLC, respectively. The purified enzyme was most active at 55C and pH 5.5. It was specific to xylan. The apparent K m and V max values on solubl...
متن کاملThree-phase partitioning for simultaneous renaturation and partial purification of Aspergillus niger xylanase.
Three-phase partitioning (TPP) is carried out by mixing ammonium sulfate and t-butanol to obtain organic phase, interfacial precipitate and aqueous phase. It is shown that TPP of an 8 M urea/100 mM dithiothreitol-denatured xylanase preparation resulted in simultaneous renaturation and purification. This integrated novel approach gave recovery of 93% enzyme activity with 21-fold purification. Th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Applied and environmental microbiology
دوره 63 2 شماره
صفحات -
تاریخ انتشار 1994