Results 31 to 40 of about 3,190 (162)

Alginate Lyases from Alginate-Degrading Vibrio splendidus 12B01 Are Endolytic [PDF]

open access: yesApplied and Environmental Microbiology, 2015
ABSTRACT Alginate lyases are enzymes that degrade alginate through β-elimination of the glycosidic bond into smaller oligomers. We investigated the alginate lyases from Vibrio splendidus 12B01, a marine bacterioplankton species that can grow on alginate as its sole carbon source.
Ahmet H, Badur   +5 more
openaire   +2 more sources

Preparation of Dye-labeled Alginate for the Assay of Alginate Lyase

open access: yesBioscience, Biotechnology, and Biochemistry, 1997
Dabsyl-alginate, the dye-labeled substrate of alginate lyase, was prepared. Low-viscosity alginate, which was prepared by enzymatic degradation of sodium alginate, and tetramethylenediamine were conjugated by reductive amination. Then, dabsyl-Cl was coupled with the primary amino group of the aminobutyl-alginate. The assay for endo-alginate lyase using
YOSHIDA, Shigeki   +4 more
openaire   +1 more source

Role of an Alginate Lyase for Alginate Transport in Mucoid Pseudomonas aeruginosa [PDF]

open access: yesInfection and Immunity, 2005
ABSTRACT The opportunistic pathogen Pseudomonas aeruginosa secretes a capsule-like polysaccharide called alginate that is important for evasion of host defenses, especially during chronic pulmonary disease of patients with cystic fibrosis (CF).
Sumita, Jain, Dennis E, Ohman
openaire   +2 more sources

Alginate synthesis in Pseudomonas aeruginosa: the role of AlgL (alginate lyase) and AlgX [PDF]

open access: yesJournal of Bacteriology, 1996
Previous studies localized an alginate lyase gene (algL) within the alginate biosynthetic gene cluster at 34 min on the Pseudomonas aeruginosa chromosome. Insertion of a Tn501 polar transposon in a gene (algX) directly upstream of algL in mucoid P. aeruginosa FRD1 inactivated expression of algX, algL, and other downstream genes, including algA.
S R, Monday, N L, Schiller
openaire   +2 more sources

Characterization of a New Biofunctional, Exolytic Alginate Lyase from Tamlana sp. s12 with High Catalytic Activity and Cold-Adapted Features

open access: yesMarine Drugs, 2021
Alginate, a major acidic polysaccharide in brown algae, has attracted great attention as a promising carbon source for biorefinery systems. Alginate lyases, especially exo-type alginate lyase, play a critical role in the biorefinery process.
Rui Yin   +5 more
doaj   +1 more source

Screening and identification of marine alginate lyase-producing bacteria and optimization of enzyme production conditions [PDF]

open access: yesZhongguo niangzao
Alginate lyases are mostly derived from marine bacteria with unique living environments. Using sodium alginate as the sole carbon source, a strain with high-yield alginate lyase from 56 strains of marine bacteria was screened using primary screening by ...
HU Mengdi, LI Yaozu, ZHANG Xiaoyong, MO Meiqing, GAO Xiangyang
doaj   +1 more source

Alginate Lyase from Indonesian Bacillus megaterium S245 Shows Activities Toward Polymannuronate and Polyguluronate

open access: yesSqualen, 2017
Screening of alginate lyase producing bacteria associated with seaweed Sargassum crassifolium was carried out, and isolate S245, identified as Bacillus megaterium S245 was found to produce high alginate lyase activity.
Subaryono Subaryono   +4 more
doaj   +1 more source

Properties of Alginate Lyases from Marine Bacteria [PDF]

open access: yesApplied and Environmental Microbiology, 1984
Alginate lyases (EC 4.2.2.3) from two marine bacteria were isolated and partially characterized. A cell-bound lyase from isolate A3 had a molecular weight of approximately 100,000 and cleaved mannuronate blocks, apparently in an exo manner. A lyase recovered from the culture medium of isolate W3 was soluble in saturated ammonium sulfate, cleaved ...
R S, Doubet, R S, Quatrano
openaire   +2 more sources

Functional Exploration of the Polysaccharide Lyase Family PL6. [PDF]

open access: yesPLoS ONE, 2016
Alginate, the main cell-wall polysaccharide of brown algae, is composed of two residues: mannuronic acid (M-residues) and, its C5-epimer, guluronic acid (G-residues).
Sophie Mathieu   +4 more
doaj   +1 more source

Alginate Lyases: Sources, Mechanism of Activity and Potencial Application

open access: yesSqualen, 2013
Alginate lyases are group of enzymes which catalyze depolymerization of alginate into oligosaccharides. Alginate lyase have been widely used in many applications such as in production of bioactive oligosaccharides, control of polysaccharide rheological ...
Subaryono Subaryono   +3 more
doaj   +1 more source

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