
%0 Journal Article
%A Jermyn, MA 
%T Fungal Cellulases VI. SUBSTRATE AND INHIBITOR SPECIFICITY OF THE fl-GLUCOSIDASE OF
ST ACHYBOTRYS ATRA
%J Australian Journal of Biological Sciences
%D 1955/12/01
%V 8
%N 4
%P 577-602
%K 
%R https://doi.org/10.1071/BI9550577
%U https://www.publish.csiro.au/paper/BI9550577 
%X 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. 
