PENICILLIUM-PURPUROGENUM PRODUCES SEVERAL XYLANASES - PURIFICATION AND PROPERTIES OF 2 OF THE ENZYMES
Author | dc.contributor.author | Belancic, Andrea | |
Author | dc.contributor.author | Scarpa, Juan | es_CL |
Author | dc.contributor.author | Peirano, Alessandra | es_CL |
Author | dc.contributor.author | Díaz, René | es_CL |
Author | dc.contributor.author | Steiner, Jeannette | es_CL |
Author | dc.contributor.author | Eyzaguirre, Jaime | es_CL |
Admission date | dc.date.accessioned | 2011-07-18T18:39:53Z | |
Available date | dc.date.available | 2011-07-18T18:39:53Z | |
Publication date | dc.date.issued | 1995-07-15 | |
Cita de ítem | dc.identifier.citation | JOURNAL OF BIOTECHNOLOGY 41 (1): 71-79 | es_CL |
Identifier | dc.identifier.issn | 0168-1656 | |
Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/121412 | |
General note | dc.description | Artículo de publicación ISI | es_CL |
Abstract | dc.description.abstract | The fungus Penicillium purpurogenum produces several extracellular xylanases. The two major forms (xylanases A and B) have been purified and characterized. After ammonium sulfate precipitation and chromatography in Bio-Gel P 100, xylanase A was further purified by means of DEAE-cellulose, hydroxylapatite and CM-Sephadex, and xylanase B by DEAE-cellulose and CM-Sephadex. Both xylanases showed apparent homogeneity in SDS-polyacrylamide gel electrophoresis. Xylanase A (33 kDa) has an isoelectric point of 8.6, while xylanase B (23 kDa) is isoelectric at pH 5.9. Antisera against both enzymes do not cross-react. The amino terminal sequences of xylanases A and B show no homology. The results obtained suggest that the enzymes are produced by separate genes and they may perform different functions in xylan degradation. | es_CL |
Lenguage | dc.language.iso | en | es_CL |
Publisher | dc.publisher | ELSEVIER SCIENCE BV | es_CL |
Keywords | dc.subject | P-PURPUROGENUM | es_CL |
Título | dc.title | PENICILLIUM-PURPUROGENUM PRODUCES SEVERAL XYLANASES - PURIFICATION AND PROPERTIES OF 2 OF THE ENZYMES | es_CL |
Document type | dc.type | Artículo de revista |
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