
TY  - JOUR
A1  - Jermyn, MA 
T1  - Fungal Cellulases VI. SUBSTRATE AND INHIBITOR SPECIFICITY OF THE fl-GLUCOSIDASE OF
ST ACHYBOTRYS ATRA
JF  - Australian Journal of Biological Sciences
JO  - Aust. Jnl. Of Bio. Sci.
Y1  - 1955
VL  - 8
IS  - 4
SP  - 577
EP  - 602
KW  - 
UR  - https://doi.org/10.1071/BI9550577 
N2  - A large number of compounds with glycosidic linkages have been tested as substrates for the ,8-glucosidase of Stachybotrys atm. The enzyme appears to be specific for ,8-glucosides and all configurational alterations to the D-glucopyranose ring or substitutions in it lead to non-substrates; phenyl-fl-thioglucoside is a substrate, however. Aryl-,8-glucosides have a higher affinity for the enzyme than alkyl-,8-glucosides and no hydrolysis of cellobiose by the enzyme can be demonstrated. arrha-Substitution in aryl-fl-glucosides leads to a marked decrease in the affinity between enzyme and substrate. 
ER  -

