Molecular biology of xylan degradation

Thomson, Jennifer A.

doi:10.1111/j.1574-6968.1993.tb05864.x

Cited by 140 publications

(63 citation statements)

References 129 publications

(168 reference statements)

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“…The largest renewable carbon source on earth is the cell wall of plants, which consist primarily of cellulose, hemicellulose, pectin and lignin [1]. Among these components, hemicellulose is the second-most abundant fraction after cellulose [2].…”

Section: Introductionmentioning

confidence: 99%

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Wang

et al. 2012

Indian J Microbiol

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A xylanase gene (xynZF-2) from the Aspergillus niger XZ-3S was cloned and expressed in Escherichia coli. The coding region of the gene was separated by only one intron with the 68 bp in length. It encoded 225 amino acid residues of a protein with a calculated molecular weight of 24.04 kDa plus a signal peptide of 18 amino acids. The amino acid sequence of the xynZF-2 gene had a high similarity with those of family 11 of glycosyl hydrolases reported from other microorganisms. The mature peptide encoding cDNA was subcloned into pET28a(?) expression vector. The resultant recombinant plasmid pET-28a-xynZF-2 was transformed into E. coli BL21(DE3), and finally the recombinant strain BL21/xynZF-2 was obtained. A maximum activity of 42.33 U/mg was gained from cellular of E. coli BL21/xynZF-2 induced by IPTG. The optimum temperature and pH for recombinant enzyme which has a good stability in alkaline conditions were 40°C and 5.0, respectively. Fe 3? had an active effect on the enzyme obviously.

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Section: Introductionmentioning

confidence: 99%

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Wang

et al. 2012

Indian J Microbiol

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“…Complete hydrolysis of xylan requires cooperative actions from multiple groups of xylanolytic enzymes [57][58][59]. The enzymes involved in hydrolysis of the main chain of xylan are β-d-xylanase which attacks the polysaccharide backbone, and β-d-xylosidase, which hydrolyzes xylooligosaccharides to xylose [60].…”

Section: Effect Of Alkali Pretreatmentmentioning

confidence: 99%

Potential of Agricultural Residues and Hay for Bioethanol Production

Chen

Sharma-Shivappa

Keshwani

et al. 2007

Appl Biochem Biotechnol

157

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Production of bioethanol from agricultural residues and hays (wheat, barley, and triticale straws, and barley, triticale, pearl millet, and sweet sorghum hays) through a series of chemical pretreatment, enzymatic hydrolysis, and fermentation processes was investigated in this study. Composition analysis suggested that the agricultural straws and hays studied contained approximately 28.62-38.58% glucan, 11.19-20.78% xylan, and 22.01-27.57% lignin, making them good candidates for bioethanol production. Chemical pretreatment with sulfuric acid or sodium hydroxide at concentrations of 0.5, 1.0, and 2.0% indicated that concentration and treatment agent play a significant role during pretreatment. After 2.0% sulfuric acid pretreatment at 121°C/15 psi for 60 min, 78.10-81.27% of the xylan in untreated feedstocks was solubilized, while 75.09-84.52% of the lignin was reduced after 2.0% sodium hydroxide pretreatment under similar conditions. Enzymatic hydrolysis of chemically pretreated (2.0% NaOH or H 2 SO 4 ) solids with Celluclast 1.5 LNovozym 188 (cellobiase) enzyme combination resulted in equal or higher glucan and xylan conversion than with Spezyme® CP-xylanase combination. The glucan and xylan conversions during hydrolysis with Celluclast 1.5 L-cellobiase at 40 FPU/g glucan were 78.09 to 100.36% and 74.03 to 84.89%, respectively. Increasing the enzyme loading from 40 to 60 FPU/g glucan did not significantly increase sugar yield. The ethanol yield after fermentation of the hydrolyzate from different feedstocks with Saccharomyces cerevisiae ranged from 0.27 to 0.34 g/g glucose or 52.00-65.82% of the theoretical maximum ethanol yield.

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“…Generally, such biomass is composed of approximately 40% cellulose, 20-30% lignin and 20-30% hemicellulose, the most abundant of which is xylan [3]. Xylanases, acting on polymeric xylan chains by hydrolysing the osidic bond between xylose subunits, randomly generate smaller xyloolgiosaccharides [4]. The enzymatic degradation of xylan has numerous industrial and commercial applications, including use in animal feed supplementation, Kraft bleaching, paper manufacturing, municipal waste treatment and in the treatment of lignocellulosic materials for bioethanol production [5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Purification and characterisation of a xylanase from Thermomyces lanuginosus and its functional expression by Pichia pastoris

Gaffney

Carberry

Doyle

et al. 2009

Enzyme and Microbial Technology

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a b s t r a c tA xylanase produced by Thermomyces lanuginosus 195 by solid state fermentation (SSF) was purified 9.3-fold from a crude koji extract, with a 7.6% final yield. The purified xylanase (with an estimated mass of 22 kDa by SDS-PAGE) retained 18% relative activity when treated for 10 min at 100• C and approximately 90% relative activity when incubated at pH values ranging from 6 to 10. Xylanase activity in the purified preparation was significantly enhanced following treatment with manganese and potassium chlorides (p < 0.05) but significantly reduced by calcium, cobalt and iron (p < 0.05). The purified enzyme was also shown to be exclusively xylanolytic. The gene encoding xylanase activity from T. lanuginosus 195 was functionally expressed by Pichia pastoris. MALDI-ToF mass spectrometry and zymography were employed to confirm functional recombinant expression. Maximum xylanase titres were achieved following 120 h induction of the recombinant culture, yielding 26.8 U/mL. Achieving functional protein expression facilitates future efforts to optimise the cultivation conditions for heterologous xylanase production.

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Molecular biology of xylan degradation

Cited by 140 publications

References 129 publications

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Potential of Agricultural Residues and Hay for Bioethanol Production

Purification and characterisation of a xylanase from Thermomyces lanuginosus and its functional expression by Pichia pastoris

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