Purification of the cellulase complex produced by Penicillium camemberti and its partial characterization.
Three cellulase components (FP-ase, CMC-ase and cellobiase) were purified by affinity binding on Avicel followed by Sephadex G-25, DEAE-Sepharose, DEAE-cellulose and Sephadex G-100 chromatography from the culture filtrate of the newly isolated strain Penicillium camemberti. The isolated enzymes had the properties of cellobiohydrolase, endo-1,4-beta-D-glucanase and cellobiase and their respective molar masses were 99, 87 and 61 kDa as determined by molecular sieve chromatography on Sephadex G-100. The amino acid composition of each fraction was also determined.
Jun
C W
CW
Institute of Industrial Microbiology, Korean Academy of Sciences, Pchen-Song.
Min
M Z
MZ
Sel
K M
KM
D000596:Amino Acids / Q000032:analysis; D050260:Carbohydrate Metabolism; D002480:Cellulase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D010407:Penicillium / Q000201:enzymology*; D013055:Spectrophotometry, Infrared
D000596:Amino Acids; D002482:Cellulose; D002480:Cellulase