Purification and Characterization of endo-(1→4)-β-xylanase fromGeotrichum candidum 3C

Rodionova, N. A.; Dubovaya, N. V.; Eneiskaya, E. V.; Martinovich, L. I.; Gracheva, I. M.; Am, Bezborodov

doi:10.1007/bf02731889

Cited by 10 publications

(5 citation statements)

References 5 publications

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“…The G. candidum strain 3C itself was found and isolated from a rotting rope ( 5 ). Previous studies demonstrated that this strain possesses high cellulolytic and xylanolytic activities ( 6 , 7 ). So, this fungus holds great promise for biotechnology; however, there are no genome sequences of G. candidum strains available at the present time.…”

Section: Genome Announcementmentioning

confidence: 89%

Draft Genome Sequence of Geotrichum candidum Strain 3C

et al. 2014

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Section: Genome Announcementmentioning

confidence: 89%

Draft Genome Sequence of Geotrichum candidum Strain 3C

et al. 2014

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“…Stable Aliquots were withdrawn and residual enzyme activities were measured under standard assay conditions. The non-heated enzyme was taken as 100 % xylanases at acidic pH (pH 3.0-5.0) have been reported in strains such as Acidobacterium capsulatum, B. aerophilus KGJ2, and Penicillium occitanis Pol 6 [29][30][31]. The influence of temperature on the xylanase activity was examined at pH 4.0, and the results showed that the enzyme activity has an optimum temperature of 50°C (Fig.…”

Section: Effect Of Ph and Temperature On Activity And Stabilitymentioning

confidence: 99%

Biological Activities of Xylooligosaccharides Generated from Garlic Straw Xylan by Purified Xylanase from Bacillus mojavensis UEB-FK

Kallel¹,

Driss²,

Châabouni

et al. 2014

Appl Biochem Biotechnol

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A newly isolated Bacterium strain named UEB-FK was selected from Tunisian Sahara, exhibiting the highest clear zone on agar plates containing oat spelt xylan by staining with Congo red. On the basis of 16S rDNA sequence analysis, this strain was identified as Bacillus mojavensis. This strain produced extracellular xylanase. Xylanase from the strain was purified to homogeneity and had an apparent molecular weight of 14 kDa. The K m and V max values of the purified xylanase on oat spelt xylan were 3.85 mg/mL and 250.02 U/mg, respectively. The optimum pH and temperature for the enzyme were found to be 4.0 and 50 °C, respectively, and the enzyme exhibited significant heat stability. In addition, the enzyme was found to be stable in a wide range of pH (3-9). The main hydrolysis products yielded from garlic straw-extracted xylan were xylobiose and xylotriose. The antioxidant and antibacterial activities of xylan oligosaccharide (XOS) were investigated. As regards to the in vitro antioxidant activities, the XOS showed a important DPPH (1,1-diphenyl-2-picrylhydrazyl) scavenging activity (IC50 = 0.45 mg/mL) and a high β-carotene bleaching (IC50 = 2.2 mg/mL). Furthermore, XOS had a high antimicrobial activity against Klebsiella pneumoniae, Enterococcus faecalis, Bacillus thuringiensis, and Pseudomonas aeruginosa.

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“…The filamentous yeast‐like fungus Geotrichum candidum strain 3C was isolated from a rotting rope and found to have high cellulolytic and xylanolytic activities . As early as the 1970s, it was shown that the G. candidum 3C cellulase complex was more efficient than that of well‐studied Trichoderma sp.…”

Section: Introductionmentioning

confidence: 99%

“…The cellulases of G. candidum 3C were initially characterized, but unfortunately, the enzymes have been undeservedly forgotten for decades. Nevertheless, an enzyme preparation from this fungus, ‘Cellokandin G10x’ , has been used in the pulp and paper industry for waste paper utilization , and applied research has been carried out on G. candidum 3C to improve the process of bleaching of softwood and hardwood kraft pulp . Interestingly, G. candidum and related species have been found to be able to degrade various natural and artificial materials, and to be responsible for biodeterioration and destroying the information pits in compact discs .…”

Section: Introductionmentioning

confidence: 99%

Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C

et al. 2015

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The ascomycete Geotrichum candidum is a versatile and efficient decay fungus that is involved, for example, in biodeterioration of compact discs; notably, the 3C strain was previously shown to degrade filter paper and cotton more efficiently than several industrial enzyme preparations. Glycoside hydrolase (GH) family 7 cellobiohydrolases (CBHs) are the primary constituents of industrial cellulase cocktails employed in biomass conversion, and feature tunnel-enclosed active sites that enable processive hydrolytic cleavage of cellulose chains. Understanding the structure-function relationships defining the activity and stability of GH7 CBHs is thus of keen interest. Accordingly, we report the comprehensive characterization of the GH7 CBH secreted by G. candidum (GcaCel7A). The bimodular cellulase consists of a family 1 cellulosebinding module (CBM) and linker connected to a GH7 catalytic domain that shares 64% sequence identity with the archetypal industrial GH7 CBH of Hypocrea jecorina (HjeCel7A). GcaCel7A shows activity on Avicel cellulose similar to HjeCel7A, with less product inhibition, but has a lower temperature optimum (50°C versus 60-65°C, respectively). Five crystal structures, with and without bound thio-oligosaccharides, show conformational diversity of tunnel-enclosing loops, including a form with partial tunnel collapse at subsite -4 not reported previously in GH7. Also, the first O-glycosylation site in a GH7 crystal structure is reported -on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface. The GcaCel7A structures indicate higher loop flexibility than HjeCel7A, in accordance with sequence modifications. However, GcaCel7A retains small fluctuations in molecular simulations, suggesting high processivity and low endo-initiation probability, similar to HjeCel7A.

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Purification and Characterization of endo-(1→4)-β-xylanase fromGeotrichum candidum 3C

Cited by 10 publications

References 5 publications

Draft Genome Sequence of Geotrichum candidum Strain 3C

Draft Genome Sequence of Geotrichum candidum Strain 3C

Biological Activities of Xylooligosaccharides Generated from Garlic Straw Xylan by Purified Xylanase from Bacillus mojavensis UEB-FK

Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C

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