TY - JOUR
T1 - Penicillium purpurogenum produces several xylanases
T2 - Purification and properties of two of the enzymes
AU - Belancic, Andrea
AU - Scarpa, Juan
AU - Peirano, Alessandra
AU - Díaz, René
AU - Steiner, Jeannette
AU - Eyzaguirre, Jaime
PY - 1995/7/15
Y1 - 1995/7/15
N2 - 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.
AB - 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.
KW - Amino acid sequence, similarity
KW - Enzyme purification
KW - P. purpurogenum
KW - Xylanase
UR - http://www.scopus.com/inward/record.url?scp=0029084593&partnerID=8YFLogxK
U2 - 10.1016/0168-1656(95)00057-W
DO - 10.1016/0168-1656(95)00057-W
M3 - Article
C2 - 7640003
AN - SCOPUS:0029084593
VL - 41
SP - 71
EP - 79
JO - Journal of Biotechnology
JF - Journal of Biotechnology
SN - 0168-1656
IS - 1
ER -