Purification, characterization and structural analysis of an abundant beta-1,3-glucanase from banana fruit.
An abundant, catalytically active beta-1,3-endoglucanase (EC 3.2.1. 39) has been isolated from the pulp of ripe bananas. Biochemical analysis of the purified protein, molecular modelling, and molecular cloning of the corresponding gene indicate that this banana enzyme closely resembles previously characterized plant beta-glucanases with respect to its amino-acid sequence, structure and biological activity. The results described in this paper demonstrate both the occurrence of an abundant active beta-1,3-endoglucanases in fruits and also readdress the question of the possible involvement of these enzymes in the ripening and/or softening process.
Peumans
W J
WJ
Laboratory for Phytopathology, Katholieke Universiteit Leuven, Belgium. Willy.Peumans@agr.kuleuven.ac.be
Barre
A
A
Derycke
V
V
Rougé
P
P
Zhang
W
W
May
G D
GD
Delcour
J A
JA
Van Leuven
F
F
Van Damme
E J
EJ
D000595:Amino Acid Sequence; D002384:Catalysis; D003001:Cloning, Molecular; D004795:Enzyme Stability; D005638:Fruit / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D043326:Glucan 1,3-beta-Glucosidase; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D013696:Temperature; D019862:Zingiberales / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D001617:beta-Glucosidase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase