Izvorni znanstveni članak

Hydrolytic Potential of Talaromyces thermophilus β-Xylosidase and Its Use for Continuous Xylose Production

Mohamed Guerfali ; Laboratory of Biomass Valorisation and Protein Production in Eukaryotes, Centre of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, TN-3038 Sfax, Tunisia
Ines Maalej-Achouri ; Laboratory of Biomass Valorisation and Protein Production in Eukaryotes, Centre of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, TN-3038 Sfax, Tunisia
Hafedh Belghith ; Laboratory of Biomass Valorisation and Protein Production in Eukaryotes, Centre of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, TN-3038 Sfax, Tunisia

Sažetak

We report here the enhanced hemicellulase production by a Talaromyces thermophilus strain in a fed-batch fermentation using 3.6-litre laboratory-controlled bioreactor. When grown on wheat bran, this fungus produces a wide spectrum of polysaccharide-hydrolysing enzymes, mainly endo-β-1,4-xylanase (27 U/mL), β-xylosidase (1.4 U/mL), α-L-arabinofuranosidase (1.05 U/mL) and β-D-mannosidase (0.78 U/mL). The β-xylosidase was purified and shown to hydrolyse xylobiose and short xylooligosaccharides, but it was inactive on xylan. It released xylose from xylooligosaccharides with a degree of polymerisation ranging from 2 to 5. Talaromyces thermophilus β-xylosidase activity was unaffected by high glucose or arabinose concentration (0.5 M) and retained 75 % of its original activity in the presence of 133 mM xylose. Chitosan-immobilised β-xylosidase was used in a continuous process of conversion of wheat bran hydrolysate to xylose in a packed bed reactor. Xylose production of 18.6 mg/g was reached after six hours in the bioreactor and was twofold higher than that produced by the free enzyme. The produced xylose was further converted into xylitol using the crude intracellular enzyme of Talaromyces thermophilus.

Ključne riječi

hemicellulases; β-xylosidase; xylose; fed-batch fermentation; xylitol

Hrčak ID:

114464

URI

https://hrcak.srce.hr/114464

Datum izdavanja:

26.12.2013.

Podaci na drugim jezicima: hrvatski

Posjeta: 1.206 *