Purification and characterization of two d-xylanases from Trichoderma harzianum

Tan, Larry U. L.; Wong, Ken K. Y.; Yu, Edward; Saddler, John N.

doi:10.1016/0141-0229(85)90041-9

Cited by 78 publications

(20 citation statements)

References 22 publications

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“…These K m values are comparable to those reported for xylanases from C. Wmi [14], but lower than those reported for xylanases from Clostridium acetobutylicum [18] and T. harzianum [38]. The C. Xavigena xylanases of 35 kDa [27] and 56 kDa [23] showed K m and V max values of 3.3 mg/ml and 333 IU/ mg, and 1.2 mg/ml and 322 IU/mg, respectively.…”

Section: Kinetic Parameterssupporting

confidence: 84%

“…Interestingly, Xyl36 and Xyl53 from C. Xavigena CDBB-531 displayed optimal activity at temperature values 7-25°C higher than those observed (40-45°C) for xylanases from C. Wmi [14] and C. uda [31]. There are few reports of thermophilic xylanases isolated from a mesophilic microorganism such as C. Xavigena CDBB-531; there are only two reports for xylanases with optimal temperatures of 65°C from the mesophilic microorganisms Trichoderma harzianum [38] and Streptomyces sp. [44].…”

Section: Puriwcation Of Xyl36 Xyl53 and Zymogram Analysismentioning

confidence: 97%

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Purification and characterization of two sugarcane bagasse-absorbable thermophilic xylanases from the mesophilic Cellulomonas flavigena

Santiago-Hernández

Vega-Estrada

Montes-Horcasitas

et al. 2007

J Ind Microbiol Biotechnol

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We report the purification and characterization of two thermophilic xylanases from the mesophilic bacteria Cellulomonas flavigena grown on sugarcane bagasse (SCB) as the only carbon source. Extracellular xylanase activity produced by C. flavigena was found both free in the culture supernatant and associated with residual SCB. To identify some of the molecules responsible for the xylanase activity in the substrate-bound fraction, residual SCB was treated with 3 M guanidine hydrochloride and then with 6 M urea. Further analysis of the eluted material led to the identification of two xylanases Xyl36 (36 kDa) and Xyl53 (53 kDa). The pI for Xyl36 was 5.0, while the pI for Xyl53 was 4.5. Xyl36 had a Km value of 1.95 mg/ml, while Xyl53 had a Km value of 0.78 mg/ml. In addition to SCB, Xyl36 and Xyl53 were also able to bind to insoluble oat spelt xylan and Avicel, as shown by substrate-binding assays. Xyl36 and Xyl53 showed optimal activity at pH 6.5, and at optimal temperature 65 and 55 degrees C, respectively. Xyl36 and Xyl53 retained 24 and 35%, respectively, of their original activity after 8 h of incubation at their optimal temperature. As far as we know, this is the first study on the thermostability properties of purified xylanases from microorganisms belonging to the genus Cellulomonas.

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Section: Kinetic Parameterssupporting

confidence: 84%

Section: Puriwcation Of Xyl36 Xyl53 and Zymogram Analysismentioning

confidence: 97%

Purification and characterization of two sugarcane bagasse-absorbable thermophilic xylanases from the mesophilic Cellulomonas flavigena

Santiago-Hernández

Vega-Estrada

Montes-Horcasitas

et al. 2007

J Ind Microbiol Biotechnol

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“…Endoxylanases have previously been isolated from commercial preparations of T. viride enzymes (12,15,23) as well as the culture medium of several other Trichoderma species (2,25,32). The overall yields and specific activities provided by our protocol compare favorably with those previous methods.…”

Section: Discussionsupporting

confidence: 61%

Ethylene Biosynthesis-Inducing Xylanase

Dean¹,

Anderson²

1991

Plant Physiol.

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The ethylene biosynthesis-inducing endoxylanase (EIX) from xylan-induced cultures of the fungus, Trichoderma viride, was purified to near homogeneity and compared with the EIX isolated from Cellulysin. Both enzymes migrate as 9.2 kilodalton proteins during gel filtration chromatography under nondenaturing conditions, but the mature polypeptide migrates as a 22 kilodalton band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The amino acid composition of the 22 kilodalton polypeptide is enriched by Gly, Ser, Thr, Trp, and Tyr, but depleted in Ala, Glx, Leu, and Lys. Both proteins lack sulfur-containing amino acids. The protein is glycosylated, and inhibition of EIX synthesis by tunicamycin suggests that at least some of the sugar moieties are linked to asparagine residues. EIX appears to be synthesized initially as a 25 kilodalton precursor protein that is processed to 22 kilodalton during secretion.A factor limiting our understanding of plant defense responses in plant-pathogen interactions has been the paucity of elicitors which have been purified and structurally characterized. Ethylene biosynthesis, one common response of plant tissues to pathogen attack (21), is stimulated by a variety of plant-and pathogen-derived polysaccharides and proteins (4,26,28). Ethylene has been suggested to play a role in activating certain defense responses in some plant tissues (9). This laboratory has previously demonstrated that an endo-B-1,4-xylanase (1,4-f3-D-xylan xylanohydrolase; EC 3.2.1.8) purified from a commercial mixture of fungal enzymes, Cellulysin3, is a potent elicitor ofethylene biosynthesis in tobacco (Nicotiana tabacum L. cv Xanthi) ( 1,12).

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“…The purified enzyme was able to release a small amount of xylose from xylans, suggesting an exo-acting mechanism. Xylose-liberating xylanases have been detected in Microtetraspora flexuosa SIIX, Trichoderma harzianum, and T. viride [2, 20,21]. The enzyme did not show an exo-activity on kraft and sulfite pulps.…”

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of a Low-Molecular-Weight Xylanase Produced by Acrophialophora nainiana

et al. 1999

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A low-molecular-weight xylanase activity (XynI) was isolated from the fungus Acrophialophora nainiana after growth in a solid medium containing wheat bran. XynI was purified to apparent homogeneity by ultrafiltration and gel filtration chromatography. The purified enzyme had a molecular weight value of approx. 17 kDa, as determined by SDS-PAGE. This enzyme was most active at 50 degreesC and pH 6.0. At 50 degreesC the half-life was 150 min. The apparent Km value for birchwood xylan was much lower than the Km value for oat spelt xylan. XynI was activated by L-cysteine, DTE, beta-mercaptoethanol, and L-tryptophan. XynI did not show significant sequence homology with other xylanases. The analysis of hydrolysis products of xylans and wood pulps showed that XynI was able to release xylooligomers ranging from X2 to X3 and X2 to X6, respectively. The enzyme was not active against acetylated xylan. A small amount of xylose was released from deacetylated, birchwood, and oat spelt xylans. The results obtained with enzymatic treatment of Kraft pulp indicated a reduction in the amount of chlorine compounds required for the process and enhanced brightness gain.

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Purification and characterization of two d-xylanases from Trichoderma harzianum

Cited by 78 publications

References 22 publications

Purification and characterization of two sugarcane bagasse-absorbable thermophilic xylanases from the mesophilic Cellulomonas flavigena

Purification and characterization of two sugarcane bagasse-absorbable thermophilic xylanases from the mesophilic Cellulomonas flavigena

Ethylene Biosynthesis-Inducing Xylanase

Purification and Characterization of a Low-Molecular-Weight Xylanase Produced by Acrophialophora nainiana

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