Purification and characterization of two extracellular beta-glucosidases from Aspergillus nidulans.
Two beta-glucosidases, P-I and P-II, were purified from the culture filtrate of Aspergillus nidulans. The M(r) values of P-I and P-II were about 125,000 and 50,000, respectively. The isoelectric point, optimal pH and temperature, Michaelis constants for several substrates and inhibition constants for glucose and glucono-delta-lactone of each enzyme were determined. We conclude that the high affinity toward cellobiose and low inhibition by glucose of these enzymes may offer significant advantages in improving cellulose hydrolysis.
Kwon
K S
KS
Department of Microbiology, Seoul National University, Korea.
Kang
H G
HG
Hah
Y C
YC
D001233:Aspergillus nidulans / Q000201:enzymology*; D002475:Cellobiose; D005942:Gluconates / Q000494:pharmacology; D005947:Glucose / Q000494:pharmacology; D007526:Isoelectric Point; D007700:Kinetics; D007783:Lactones; D008970:Molecular Weight; D013379:Substrate Specificity; D001617:beta-Glucosidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D005942:Gluconates; D007783:Lactones; D002475:Cellobiose; D001617:beta-Glucosidase; D005947:Glucose; C010730:beta-glucono-1,5-lactone