EC Number   |
Application |
Reference |
|---|
   4.2.2.3 | agriculture |
the alginate oligomers prepared by the lyase from Streptomyces sp. A5 show growth-promoting activity on the roots of banana plantlets. Encapsulation method using alginate microbeads to inoculate beneficial streptomycete strains might be beneficial to the root growth of banana plantlets |
-, 680308 |
| 4.2.2.3 | analysis |
the enzyme, wild-type and mutant variants, can be used for alginate fine structure elucidation |
-, 715553 |
| 4.2.2.3 | biofuel production |
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production |
-, 729056 |
| 4.2.2.3 | biotechnology |
a new highly specific and sensitive capillary electrophoresis method for the determination of the total alginic acid (AA) content in pharmaceutical formulations is described by means of capillary electrophoresis at 230 nm after treatment with alginate lyase and separation of unsaturated products, DELTA-oligomers (DELTA-HexA-[HexA]n), in particular, DP3 (DELTA-HexA-HexA-HexA) and DP4 (DELTAHexA-HexA-HexA-HexA). The capillary electrophoresis method is applied to the determination of AA content of both solid and liquid formulations that also contain antacid ingredients, mainly aluminium, sodium and potassium bicarbonate, and emulsifying and flavouring agents |
692062 |
| 4.2.2.3 | biotechnology |
controlled mono-PEGylation of A1-III alginate lyase mutant A53C produces a conjugate with wild type levels of activity. The PEGylated mutant exhibits enhanced solution phase kinetics with bacterial alginate. In vitro binding studies with both enzyme-specific antibodies, from immunized New Zealand white rabbits, and a single chain antibody library, derived from a human volunteer show that the PEGylated enzyme is substantially less immunoreactive. More than 90% of adherent, mucoid, Pseudomonas aeruginosa biofilms are removed from abiotic surfaces following a one h treatment with the PEGylated mutant, whereas the wild type enzyme removes only 75% of biofilms in parallel studies |
716698 |
| 4.2.2.3 | biotechnology |
most of Pseudomonas strains have copious alginates enclosing the bacteria cells, which makes it difficult to transfer exogenous DNA into the cells during transformation. Pretreatment of Pseudomonas sp. QDA with alginate lyase before electroporation increases transformation efficiency approximately 10000fold than without pretreatment of alginate lyase, and a high transformation efficiency nearly the same as that of alginate production deficient mutant is obtained. Among the alginate lyases tested, AL2 is the most effective enzyme for pretreatment. This electroporation procedure is also efficient for Pseudomonas aeruginosa FRD1 (mucoid) and PAO1 (non-mucoid) |
679551 |
| 4.2.2.3 | biotechnology |
the algino-oligosaccharides show an elicitor activity stimulating the accumulation of phytoalexin and inducing phenylalanine ammonia lyase in soybean cotyledon, and antimicrobial activity on Pseudomonas aeruginosa |
692811 |
| 4.2.2.3 | biotechnology |
the bacterium A7 is shown to be alginate lyase-producing in genus Gracilibacillus and effective in degrading alginate to oligosaccharides in wakame during composting process |
693942 |
| 4.2.2.3 | biotechnology |
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields |
-, 648532 |
| 4.2.2.3 | degradation |
alginate lyase is probably not suitable for hydrolysis of microcapsules in the presence of cells, in order to achieve high cell density and high productivity. However, the high activity may be useful for releasing cells from alginate beads or AG/PLL microcapsules |
678903 |
