4.2.2.3: mannuronate-specific alginate lyase
This is an abbreviated version!
For detailed information about mannuronate-specific alginate lyase, go to the full flat file.
Word Map on EC 4.2.2.3
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4.2.2.3
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polysaccharide
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lyases
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oligosaccharide
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depolymerization
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polyg
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biotechnology
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seaweed
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colicins
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mucoid
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trisaccharide
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uronic
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sphingomonas
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alginate-degrading
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exolytic
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pseudoalteromonas
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tetrasaccharide
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beta-elimination
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macroalgae
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saccharification
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laminaria
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holins
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mannuronan
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saccharophagus
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exo-type
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phix174
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sargassum
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medicine
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degradans
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murein
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microbulbifer
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alginate-based
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endolysins
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abalone
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haliotis
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polysaccharide-degrading
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analysis
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agriculture
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degradation
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molecular biology
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biofuel production
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food industry
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synthesis
- 4.2.2.3
- polysaccharide
- lyases
- oligosaccharide
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depolymerization
- polyg
- biotechnology
- seaweed
- colicins
- mucoid
- trisaccharide
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uronic
- sphingomonas
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alginate-degrading
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exolytic
- pseudoalteromonas
- tetrasaccharide
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beta-elimination
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macroalgae
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saccharification
- laminaria
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holins
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mannuronan
- saccharophagus
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exo-type
- phix174
- sargassum
- medicine
- degradans
- murein
- microbulbifer
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alginate-based
- endolysins
- abalone
- haliotis
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polysaccharide-degrading
- analysis
- agriculture
- degradation
- molecular biology
- biofuel production
- food industry
- synthesis
Reaction
Synonyms
(poly alpha-l-guluronate) lyase, A1 alginate lyase, A1-II, A1-III, A1-IV', A1m, A1mU, A9mC, A9mL, A9mT, AAlyase, AkAly30, AL2, alg, ALG-5, Alg-A, Alg17C, Alg2A, Alg7D, AlgA, AlgB, AlgE7, AlgI, alginase I, alginate lyase, alginate lyase A, alginate lyase A1-II, alginate lyase A1-II', alginate lyase A1-III, alginate lyase AlyPEEC, alginate lyase Atu3025, alginate lyase B, alginate lyase C, alginate lyase I, alginate lyase VI, alginate lyase1-III, AlgL, ALY, ALY-1, Aly-SJ02, Aly1, Aly2, Aly28, Aly30, Aly32, Aly33, Aly35, Aly7B, AlyA, AlyA1, AlyA2, AlyA3, AlyA5, AlyB, AlyDW11, ALYIII, alyPEEC, AlyPI, AlyPM, AlyQ, AlyV5, AlyVI, Atu3025, AXE80_11190, CL2, EC 4.2.99.4, endo-type alginate lyase, endolytic poly(M) lyase, endolytic polymannuronate lyase, exotype alginate lyase, HdAlex, hdalex-1, HdAly, KJ-2 alginate lyase, LbAly28, lyase AlyA, lyase, alginate, Lysis protein, M block-specific polymannuronate lyase, mannuronate alginate lyase, MJ-3 alginate lyase, More, MY04_2544, NIS_0185, Oal17A, oligoalginate lyase, PL-5 alginate lyase, PM lyase, poly(1,4-beta-D-mannuronide) lyase, poly(beta-D-1,4-mannuronide) lyase, Poly(beta-D-mannuronate) lyase, poly(M) lyase, poly(M)lyase, Poly(mana) alginate lyase, poly(mana)alginate lyase, polymannuronate lyase, polyMG-specific alginate lyase, protein PA1167, SP2, V12B01_24254, V12B01_24259, WP_053404615
ECTree
4.2.2.3 mannuronate-specific alginate lyaseAdvanced search results
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Application on EC 4.2.2.3 - mannuronate-specific alginate lyase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
analysis
biofuel production
biotechnology
degradation
food industry
medicine
molecular biology
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this is the first report that yeast cells displaying alginate lyase are used to produce different lengths of oligosaccharides from alginate
synthesis
additional information
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use of recombinant abalone alginate lyase and beta-1,4-endoglucanase for protoplast isolation from Laminaria japonica. In Laminaria japonica blades pretreated with proteinase K and incubated in artificial seawater containing alginate lyase and beta-1,4-endoglucanase, the protoplast number is increased up to 5000000 protoplasts/g fresh weight. These cells are mostly derived from the epidermal layer rather than the cortical layer. Results suggest that at least three enzymes, alginate lyase, cellulase, and protease, are essential for effective protoplast isolation from Laminaria japonica
agriculture
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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
agriculture
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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
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analysis
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the enzyme, wild-type and mutant variants, can be used for alginate fine structure elucidation
analysis
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the enzyme, wild-type and mutant variants, can be used for alginate fine structure elucidation
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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
biofuel production
Saccharophagus degradans 2-40 / ATCC 43961
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Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
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biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
Azotobacter vinelandii phage
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
-
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
Dollabella auricola
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
Fucus spp.
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
Ishige sp.
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
Alginovibrio aquatilis
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
Azotobacter phage A31
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
Azotobacter phage A22
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
biotechnology
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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)
biotechnology
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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
biotechnology
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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
biotechnology
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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
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
biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
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biotechnology
Vibrio sinaloensis Alg-A
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
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biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
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biotechnology
Bacillus sp. (in: Bacteria) ATB-1015
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
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biotechnology
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use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
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degradation
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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
degradation
enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata
degradation
enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata
degradation
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
degradation
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
food industry
the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate
food industry
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the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate
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medicine
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enzyme is a target for design of chemotherapeutics in the treatment of cystis fibrosis caused by infection with alginate producing Pseudomonas aeruginosa
medicine
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once mucoid strains of Pseudomonas aeruginosa have become established in the respiratory tracts of cystic fibrosis patients they can rarely be eliminated by antibiotic treatment alone. Coadministration of antibiotics with alginate lyase, which degrades the exopolysaccharide produced by mucoid strains of pseudomonas aeruginosa might benefit cystic fibrosis patients by increasing the efficacy of antibioticin the respiratory tract
medicine
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alginate hydrogels can be enzymatically degraded in a controlled and tunable fashion by incorporating poly(lactide-co-glycolide) microspheres loaded with alginate lyase into alginate hydrogels. Neural progenitor cells can be cultured and expanded in vitro in this degradable alginate hydrogel system. A significant increase in the expansion rate of neural progenitor cells cultured in degrading alginate hydrogels versus neural progenitor cells cultured in standard, i.e. non-degrading, alginate hydrogels. Degradable alginate hydrogels encapsulating stem cells may be widely applied to develop novel therapies for tissue regeneration
medicine
it might be possible to use alginate lyase AlgL as an adjuvant therapeutic medicine for the treatment of disease associated with Pseudomonas aeruginosa infection
medicine
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treatment with AlgL improves killing of the mucoid strain PA-489121 of Pseudomonas aeruginosa, the coadministration of DNase and AlgL is essential for enhanced activity in reducing biofilm growth and sputum bacterial counts
medicine
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
medicine
alginate lyases are promising therapeutic candidates for treating mucoid Pseudomonas aeruginosa infections. In particular, the enzymes' ability to degrade alginate, a key component of mucoid biofilm matrix, has been the presumed mechanism by which they disrupt biofilms and enhance antibiotic efficacy, but invitro modeling shows that alginate lyase dispersion of Pseudomonas aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity
medicine
alginate lyases are promising therapeutic candidates for treating mucoid Pseudomonas aeruginosa infections. In particular, the enzymes' ability to degrade alginate, a key component of mucoid biofilm matrix, has been the presumed mechanism by which they disrupt biofilms and enhance antibiotic efficacy, but invitro modeling shows that alginate lyase dispersion of Pseudomonas aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity
medicine
site-specific mono-PEGylation of genetically engineered A1-III alginate lyase yields an enzyme with enhanced performance relative to therapeutically relevant metrics. Over 90% of adherent, mucoid, Pseudomonas aeruginosa biofilms are removed from abiotic surfaces following a one h treatment with the PEGylated variant, whereas the wild-type enzyme removes only 75% of biofilms
medicine
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it might be possible to use alginate lyase AlgL as an adjuvant therapeutic medicine for the treatment of disease associated with Pseudomonas aeruginosa infection
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medicine
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enzyme is a target for design of chemotherapeutics in the treatment of cystis fibrosis caused by infection with alginate producing Pseudomonas aeruginosa
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synthesis
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alginate production is improved by use of the constructed mutant strain SML2, due to enzyme-deficiency the alginate production reaches a higher level and the alginate polymers have a higher molecular weight
synthesis
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enzyme-catalyzed gel-sol transition of calcium-alginate obtained by internal gelling strategy with the help of an entrapped alginate lyase. Alginate molecules and enzyme-produced oligoalginates shorten the gel time of physical gelatin gels (5% and 1.5%), probably due to local protein concentration increase. Interpenetrated networks composed of calcium-alginate and of gelatin are obtained only if elongation of gelatin helices inside a pre-existing calcium-alginate network could occur and only for low gelatin concentration (1.5%). The physical gelatin network is almost reversible inside the alginate one. Both networks can be obtained in the presence of alginate lyase, but gel-sol transition of calcium-alginate cannot be obtained in the presence of gelatin
synthesis
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aly-SJ02 may be a good tool to produce dimers and trimers from alginate
synthesis
the recombinant MJ-3 alginate lyase can be used as a biocatalyst for saccharification of alginate since it can efficiently degrade poly-M block, poly-G block, poly-MG block, alginate oligosaccharides, and alginate into alginate monosaccharides
synthesis
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
synthesis
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the recombinant MJ-3 alginate lyase can be used as a biocatalyst for saccharification of alginate since it can efficiently degrade poly-M block, poly-G block, poly-MG block, alginate oligosaccharides, and alginate into alginate monosaccharides
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synthesis
Saccharophagus degradans 2-40 / ATCC 43961
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Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
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