2003
DOI: 10.1590/s1517-83822003000200007
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Production and purification of an Endo–1,4-beta-Xylanase from Humicola grisea var. thermoidea by electroelution

Abstract: Humicola grisea var. thermoidea produces two forms of extracellular xylanase. The component form 1 was purified using the electroelution method, due to the very small production of this extracellular enzyme. The apparent molecular mass was 61.8 kDa by SDS-PAGE.

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Cited by 7 publications
(1 citation statement)
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“…The ion exchange resins DEAE-Trisacryl and S-Sepharose were also used with differente buffers and pHs, however, xylanase did not link to any of them under the assay conditions, suggesting that this enzyme was a glycoprotein (Boyer, 1993). The purification of this enzyme could be done through electroelution technique, used by Monti et al (2003) to purify the form I xylanase from Humicola grisea var. thermoidea.…”
Section: Chromatographic Separation Of the Hydrolysis Productsmentioning
confidence: 99%
“…The ion exchange resins DEAE-Trisacryl and S-Sepharose were also used with differente buffers and pHs, however, xylanase did not link to any of them under the assay conditions, suggesting that this enzyme was a glycoprotein (Boyer, 1993). The purification of this enzyme could be done through electroelution technique, used by Monti et al (2003) to purify the form I xylanase from Humicola grisea var. thermoidea.…”
Section: Chromatographic Separation Of the Hydrolysis Productsmentioning
confidence: 99%