Glucans enzymic degradation

Pullulanase Enzyme degrading pnUnlan, a branched starch pullulanase catalyzes the hydrolysis of the a-l,6-glncosidic linkage in a-glucans. Pullulanase preferentially hydrolyzes pnUnlan while isoamylase has a preference for glycogen and amylopectin. See WaUenfels, K Bender, H and Rached, J.R., Pnllnlanase from Aerobacter aerogenes production in a cell-bound state. Pnrification and properties of the enzymes, Biochem. Biophys. Res. 

IV. PARASITISM. Lysis by hydrolytic enzymes excreted by microorganisms is a well-known feature of mycoparasitism. Chitinase and P-l,3 glucanase (laminarase) are particularly important enzymes secreted by fungal mycoparasites capable of degrading the fungal cell wall components, chitin, and P-1,3 glucan (131-134). 

Microorganisms use several types of extracellular enzymes to degrade cellulose to glucose exoglucanases (l,4-/ -D-glucan cellobiohydrolases,... 

Functionally, starch can be considered as a polysaccharide synthesized in a manner permitting its efficient degradation. Hence, biosynthesis of the starch granule is a delicate balance between efficient packing of the glucan chains and the possibility of breaking these structures at degradation. To complete this enzymatically catalyzed process in the potato tuber, a multitude of different enzyme activities are required. 

Attempts to produce cellulose from UDP-Glc using enzymes of isolated plasma membranes from higher plants have usually yielded the ( -1,3-linked glucan (callose) instead. This is a characteristic polysaccharide of plant wounds which, as healing occurs, is degraded and replaced by cellulose.140144 Callose... 

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