Browsing by Author "STEINER, J"

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    BETA-GLUCOSIDASE FROM PENICILLIUM-PURPUROGENUM - PURIFICATION AND PROPERTIES
    (1992) HIDALGO, M; STEINER, J; EYZAGUIRRE, J
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    CULTURE CONDITIONS FOR ENHANCED CELLULASE PRODUCTION BY A NATIVE STRAIN OF PENICILLIUM-PURPUROGENUM
    (1994) STEINER, J; SOCHA, C; EYZAGUIRRE, J
    A cellulolytic wild-type strain of Penicillium purpurogenum was isolated from a soil sample in southern Chile. It grew best at 28-degrees-C from an inoculum of 4 x 10(7) spores/100 ml medium. Highest endoglucanase activity was with Sigmacell as carbon source and corn steep liquor as nitrogen source. Wheat bran enhanced the production of endoglucanase and beta-glucosidase. The enzymes in the crude supernatants were stable up to 50-degrees-C and between pH 4.4 and 5.6 for 48 h.
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    PENICILLIUM-PURPUROGENUM PRODUCES SEVERAL XYLANASES - PURIFICATION AND PROPERTIES OF 2 OF THE ENZYMES
    (1995) BELANCIC, A; SCARPA, J; PEIRANO, A; DIAZ, R; STEINER, J; EYZAGUIRRE, J
    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.