4.2.2.3 additional information preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation 4.2.2.3 alginate the alginate oligomers prepared by the lyase show growth-promoting activity on the roots of banana plantlets (Streptomyces sp. A5 is isolated from banana rhizosphere) 4.2.2.3 additional information the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm 4.2.2.3 alginate the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production 4.2.2.3 alginate the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.11 4.2.2.3 alginate the biological function of AlgL to degrade alginates that fail to become exported out of the cell and thereby become stranded in the periplasmic space. At high levels of alginate synthesis in the absence of AlgL, such stranded polymers may accumulate in the periplasm to such an extent that the integrity of the cell is lost, leading to toxic effects 4.2.2.3 additional information the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview 4.2.2.3 additional information the enzyme is an endolytic polymannuronate lyase 4.2.2.3 alginate the enzyme is involved in alginate production