Open AccessPurification and characterization of two extracellular β‐glucosidases from Aspergillus nidulans
Author(s) -
Kwon KiSun,
Gyoo Kang Hyung,
Chil Hah Yung
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05454.x
Subject(s) - cellobiose , isoelectric point , glucosidases , aspergillus nidulans , chemistry , enzyme , michaelis–menten kinetics , biochemistry , hydrolysis , aspergillus , cellulose , chromatography , cellulase , enzyme assay , stereochemistry , biology , microbiology and biotechnology , mutant , gene
Two β‐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‐δ‐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.