Purification and characterization of a cellulase from the giant snail Achatina fulica.
A cellulase with activity as a cellobiohydrolase [EC3.2.1.91] was purified from the intestinal juice of the giant snail Achatina fulica. The enzyme (M(r) = about 23,000, and pI = about 5.3) also had a weak beta-glucosidase activity. The amino acid sequence of the N-terminal 20 amino acids was analyzed, and no similarity was noted for sequences of other known cellobiohydrolases.
Maeda
I
I
Department of Chemistry, Kyushu University, Fukuoka, Japan.
Shimohigashi
Y
Y
Kihara
H
H
Ohno
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002480:Cellulase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D043366:Cellulose 1,4-beta-Cellobiosidase; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007422:Intestines / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012908:Snails / Q000378:metabolism
D002480:Cellulase; D043366:Cellulose 1,4-beta-Cellobiosidase