Glucose endo-enzymes producing

Influences of glucose, cellobiose, sophorose, and cellulose, when they were each used as a C-source, upon the formation of both cell-bound and extracellular cellulases during the growth of this pseudomonad are shown in Figure 1. Glucose supported the bacterium for an excellent growth, but only slightly stimulated the formation of cellulases, and the enzymes produced were distributed almost equally to the cell and the culture medium. In the cellulose and sophorose cultures, the formation of cellulases, particularly that of extracellular component, was enhanced prominently (exo-type synthesis), whereas cellobiose which was a main end-product of enzymatic cellulolysis stimulated the formation of cell-bound component (endo-type synthesis). Thus, an apparent difference in the distribution of extracellular and cell-bound cellulases was noticed between the cultures with cellobiose and sophorose or cellulose. 

Johnson (55) has proposed that cell wall extension in yeasts takes place by the concerted action of a nucleoside diphosphate glucose glucosyl transferase and a glucanase or glucanases, such that the hydrolytic enzyme(s), presumably of an endo-action pattern, produces breaks in the existing glucan network into which new glucosyl units are incorporated. 

A polysaccharide produced in vitro by glucosyltransferases from a species of Streptococcus has been characterized as a (l->3)- -D-glucan by procedures including the action of an enzyme preparation [considered to be a mixture of endo- and exo-(l->3)- -D-glucanases] from a species of Penicillium the enzyme hydrolyzed the polysaccharide to n-glucose. This result explained the resistance, to the action of dextranase, of the... 

A dextran-dextranase system has been used to examine the synergistic effect of exo- and cndo-enzymes acting jointly on polymeric substrates. An endo-dextranase (from Penicillium funiculosum) and an cxo-dextranase (from Streptococcus mitis) produced D-glucose more rapidly from dextrans than the summed effects of the individual enzymes. 

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