Literature DB >> 14756627

Recombinant endo-beta-1,4-xylanase from Penicillium canescens.

O A Sinitsyna1, A V Gusakov, O N Okunev, V A Serebryany, E A Vavilova, Yu P Vinetsky, A P Sinitsyn.   

Abstract

Recombinant endo-beta-1,4-xylanase (Xyl-31rec, 31 kD, pI 8.2-9.3, the tenth family of glycosyl hydrolases) was isolated from the culture liquid of Penicillium canescens (strain with the amplified homologous xylanase gene) by chromatofocusing on Mono P and hydrophobic chromatography on phenyl-Superose. It is shown that the biochemical and kinetic parameters, substrate specificity, stability, and other properties of the recombinant and native enzymes are almost the same. It was found that Xyl-31rec can be used for biobleaching of cellulose, the recombinant P. canescens strains providing a high yield of extracellular Xyl-31rec (up to 800-900 U/ml of culture liquid) and not secreting cellulases.

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Year:  2003        PMID: 14756627     DOI: 10.1023/b:biry.0000011652.52741.d6

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  1 in total

1.  Effective Zearalenone Degradation in Model Solutions and Infected Wheat Grain Using a Novel Heterologous Lactonohydrolase Secreted by Recombinant Penicillium canescens.

Authors:  Larisa Shcherbakova; Alexandra Rozhkova; Dmitrii Osipov; Ivan Zorov; Oleg Mikityuk; Natalia Statsyuk; Olga Sinitsyna; Vitaly Dzhavakhiya; Arkady Sinitsyn
Journal:  Toxins (Basel)       Date:  2020-07-25       Impact factor: 4.546

  1 in total

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