http://repositorio2.unb.br/jspui/handle/10482/25480| File | Size | Format | |
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| ARTIGO_PurificationCharacterizationLow.pdf | 297,63 kB | Adobe PDF | View/Open |
| Title: | Purification and characterization of a low molecular weight xylanase from solid-state cultures of Aspergillus fumigatus Fresenius |
| Other Titles: | Purificação e caracterização de uma xilanase de baixo peso molecular de culturas de estado sólido de Aspergillus fumigatus Fresenius |
| Authors: | Silva, Claudio Henrique Cerri e Puls, Jurgen Sousa, Marcelo Valle de Ferreira Filho, Edivaldo Ximenes |
| Assunto:: | Hemicelulose Xilanase Enzimas |
| Issue Date: | 1999 |
| Publisher: | Sociedade Brasileira de Microbiologia |
| Citation: | SILVA, Claudio Henrique Cerri e et al. Purification and characterization of a low molecular weight xylanase from solid-state cultures of Aspergillus fumigatus Fresenius. Revista de Microbiologia, v. 30, n. 2, p. 114-119, 1999. DOI: https://doi.org/10.1590/S0001-37141999000200005. Disponível em: https://www.scielo.br/j/rm/a/N9R5cpJwrDwGSwMdtJkhWHw/?lang=en#. Acesso em: 10 set. 2021. |
| Abstract: | Uma enzima xilanolítica (xilanase II) foi purificada a partir de culturas de estado sólido de Aspergillus fumigatus Fresenius. O peso molecular de xilanase II foi estimado em 19 e 8,5 kDa por SDS-PAGE e FPLC, respectivamente. A enzima purificada apresentou maior atividade a 55°C e pH 5,5, além de hidrolisar especificamente xilana. Os valores aparentes de Km e Vmax de xilanas solúveis e insolúveis, isoladas de cereal e madeira, mostrou que xilanase IIa foi mais ativa em xilana solúvel de madeira. Estudos sobre produtos de hidrólise de xilanas e xilooligômeros por xilanase II em HPLC revelou que a enzima liberou uma variedade de xilooligômeros (xilobiose-xilohexose) e uma pequena quantidade de xilose a partir de xilooligômeros, apresentando atividade de transferase. |
| Abstract: | A xylan-degrading enzyme (xylanase II) was purified to apparent homogeneity from solid-state cultures of Aspergillus fumigatus Fresenius. The molecular weight of xylanase II was found to be 19 and 8.5 kDa, as estimated by SDS-PAGE and gel filtration on FPLC, respectively. The purified enzyme was most active at 55 °C and pH 5.5. It was specific to xylan. The apparent Km and Vmax values on soluble and insoluble xylans from oat spelt and birchwood showed that xylanase II was most active on soluble birchwood xylan. Studies on hydrolysis products of various xylans and xylooligomers by xylanase II on HPLC showed that the enzyme released a range of products from xylobiose to xylohexaose, with a small amount of xylose from xylooligomers, and presented transferase activity. |
| Licença:: | Revista de Microbiologia - This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY NC). Fonte: https://www.scielo.br/j/rm/a/N9R5cpJwrDwGSwMdtJkhWHw/?lang=en#. Acesso em: 10 set. 2021. |
| DOI: | https://dx.doi.org/10.1590/S0001-37141999000200005 |
| Appears in Collections: | Artigos publicados em periódicos e afins |
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