Relatedness of Thermomyces lanuginosus strains producing a thermostable xylanase

Singh, Surendra; Reddy, Poovendhree; Haarhoff, Jacques; Biely, Peter; Janse, B.J.H.; Pillay, Balakrishna; Pillay, D.; Prior, Bernard A.

doi:10.1016/s0168-1656(00)00279-0

Cited by 43 publications

(28 citation statements)

References 20 publications

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“…A comparison of xylanase activities found in the culture medium of several T. lanuginosus strains grown in submerged fermentation for 6 days with corncob as the substrate revealed a great variability of enzyme production, ranging from 3,590 U/ml to 361 U/ml (31). The xylanase activity found in semisolid Various bacterial and fungal xylanases have been expressed in different eukaryotic systems, and, in all cases, enzyme expression levels as well as specific activities were much lower than what we obtained in this work (2,13,16,18,25,26,37,38).…”

Section: Discussionmentioning

confidence: 99%

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Optimized Expression of a Thermostable Xylanase from Thermomyces lanuginosus in Pichia pastoris

Damaso

Almeida

Kurtenbach

et al. 2003

Appl Environ Microbiol

101

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Highly efficient production of a Thermomyces lanuginosus IOC-4145 ␤-1,4-xylanase was achieved in Pichia pastoris under the control of the AOX1 promoter. P. pastoris colonies expressing recombinant xylanase were selected by enzymatic activity plate assay, and their ability to secrete high levels of the enzyme was evaluated in small-scale cultures. Furthermore, an optimization of enzyme production was carried out with a 2 3 factorial design. The influence of initial cell density, methanol, and yeast nitrogen base concentration was evaluated, and initial cell density was found to be the most important parameter. A time course profile of recombinant xylanase production in 1-liter flasks with the optimized conditions was performed and 148 mg of xylanase per liter was achieved. Native and recombinant xylanases were purified by gel filtration and characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, circular dichroism spectroscopy, matrix-assisted laser desorption ionization-time of flight-mass spectrometry and physicochemical behavior. Three recombinant protein species of 21.9, 22.1, and 22.3 kDa were detected in the mass spectrum due to variability in the amino terminus. The optimum temperature, thermostability, and circular dichroic spectra of the recombinant and native xylanases were identical. For both enzymes, the optimum temperature was 75°C, and they retained 60% of their original activity after 80 min at 70°C or 40 min at 80°C. The high level of fully active recombinant xylanase obtained in P. pastoris makes this expression system attractive for fermentor growth and industrial applications.

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Section: Discussionmentioning

confidence: 99%

“…Several strains of the thermophilic fungus Thermomyces lanuginosus secrete high levels of xylanases, which are very active and stable at elevated temperatures (9,27,31). Purified and unpurified extracellular xylanase preparations from this fungus have been successfully used for the bleaching of pulps (4,11,20,21).…”

mentioning

confidence: 99%

Optimized Expression of a Thermostable Xylanase from Thermomyces lanuginosus in Pichia pastoris

Damaso

Almeida

Kurtenbach

et al. 2003

Appl Environ Microbiol

101

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“…The optimum growth pH of most strains of T. lanuginosus is 6.5. It is reported to be non-cellulolytic and probably grows commensally with cellulolytic fungi by utilizing the sugar generated by these fungi and possibly using their mycelial breakdown products (Singh et al 2000b;Gramany et al 2015). Some of them are thermostable and very suitable for the industrial applications.…”

Section: Thermostable Chitinasementioning

confidence: 99%

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

et al. 2015

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Chitinases are ubiquitous class of extracellular enzymes, which have gained attention in the past few years due to their wide biotechnological applications. The effectiveness of conventional insecticides is increasingly compromised by the occurrence of resistance; thus, chitinase offers a potential alternative to the use of chemical fungicides. The thermostable enzymes from thermophilic microorganisms have numerous industrial, medical, environmental and biotechnological applications due to their high stability for temperature and pH. Thermomyces lanuginosus produced a large number of chitinases, of which chitinase I and II are successfully cloned and purified recently. Molecular dynamic simulations revealed that the stability of these enzymes are maintained even at higher temperature. In this review article we have focused on chitinases from different sources, mainly fungal chitinase of T. lanuginosus and its industrial application.

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“…was cultivated in the inorganic salt medium as described in [24] with 2 g ball-milled cellulose powder PH105 added as the sole carbon source per 500-mL culture flask for 7 days at 200 rpm. The noncomplex cellulase secreting filamentous fungi, such as Trichoderma pseudokoningii S38, Aspergillus niger AN76, and Stachybotrys chartarum S05 were cultivated in bran medium with Mendels salts added for 5 days at 371C [25,26]. The extracellular enzymes were extracted by adding 200 mL dH 2 O per 500-mL culture flask, which was followed by centrifugation at 10 000 rpm for 10 min.…”

Section: Preparation Of the Enzyme Samplesmentioning

confidence: 99%

In situ demonstration and quantitative analysis of the intrinsic properties of glycoside hydrolases

et al. 2011

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Based on digital image analysis techniques and a series of optimizations in native electrophoresis, a new direct method to simultaneously detect the intrinsic properties of each active component in the enzymatic system of glycoside hydrolase was established. The key technique is that the concentration changes of substrate (or product) on the gel can be determined quantitatively by the gray value changes of the corresponding band after electrophoretic separation. In this manner, the catalytic characteristics of each glycoside hydrolase component were demonstrated in situ and were easily determined after immersing the gel in a series of solutions containing substrates or their derivatives. Because of its high throughput, great sensitivity, and convenient operation, this method can be used to demonstrate the natural diversity of glycoside hydrolases and to study spatial and temporal regulation in multienzyme expression systems. Thus, it is an effective approach to study the functional proteomics of glycoside hydrolases.

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Relatedness of Thermomyces lanuginosus strains producing a thermostable xylanase

Cited by 43 publications

References 20 publications

Optimized Expression of a Thermostable Xylanase from Thermomyces lanuginosus in Pichia pastoris

Optimized Expression of a Thermostable Xylanase from Thermomyces lanuginosus in Pichia pastoris

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

In situ demonstration and quantitative analysis of the intrinsic properties of glycoside hydrolases

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