Two types of bacterial alginate lyases

Kitamikado, Manabu; Tseng, Chao-Huang; Yamaguchi, Kuniko; Nakamura, Takanori

doi:10.1128/aem.58.8.2474-2478.1992

Cited by 44 publications

(17 citation statements)

References 22 publications

(16 reference statements)

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“…Indeed, the activity of alginate lyase from Vibrio. Harveyi-28 enhanced by 24-fold by 1 M NaCl [19]. In the present work, the activity of Aly1281 from P. carrageenovora ASY5 increased by 5.56-fold after addition of 0.7 M NaCl.…”

Section: Salt Activation Of Aly1281supporting

confidence: 54%

“…After 12 h of hydrolysis, the enzymatic degradation products of Aly1281 were analyzed by using TLC and ESI-MS. As shown in Figure 4A,B, the main product of the sodium alginate hydrolysis reaction is di-alginate oligosaccharide, which indicates that Aly1281 is an endo-type alginate lyase. Compared with other alginate lyases from different sources which produced alginate oligosaccharides with broad DP, the degradation products of Aly1281 displayed highly specific degradation [15,19]. Aly510-64 from Vibrio sp.…”

Section: Substrate Specificity and Degradation Pattern Of Aly1281mentioning

confidence: 96%

“…Marine-derived alginate lyases often exhibit considerable salt-tolerance ability or salt-activation effects [3,9,15,18] due to the high-salt marine environment in which the source bacteria are reproduced and evolve. The alginate lyase derived from marine Vibrio Harveyi-28, for example, exhibits a 24-fold increase in activity in 1 M NaCl [19]. Despite the extensive development of alginate lyases and their widely observed salt-regulated properties, investigations into the salt-activation mechanism of alginate lyase are scarce.…”

Section: Introductionmentioning

confidence: 99%

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Characterization and Application of an Alginate Lyase, Aly1281 from Marine Bacterium Pseudoalteromonas carrageenovora ASY5

et al. 2020

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Alginate extracted from widely cultured brown seaweed can be hydrolyzed by alginate lyase to produce alginate oligosaccharides (AOS) with intriguing biological activities. Herein, a novel alginate lyase Aly1281 was cloned from marine bacterium Pseudoalteromonas carrageenovora ASY5 isolated from mangrove soil and found to belong to polysaccharide lyase family 7. Aly1281 exhibited maximum activity at pH 8.0 and 50 °C and have broad substrate specificity for polyguluronate and polymannuronate. Compared with other alginate lyases, Aly1281 exhibited high degradation specificity and mainly produced di-alginate oligosaccharides which displayed good antioxidant function to reduce ferric and scavenge radicals such as hydroxyl, ABTS+ and DPPH. Moreover, the catalytic activity and kinetic performance of Aly1281 were highly improved with the addition of salt, demonstrating a salt-activation property. A putative conformational structural feature of Aly1281 was found by MD simulation analysis for understanding the salt-activation effect.

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Section: Salt Activation Of Aly1281supporting

confidence: 54%

Section: Substrate Specificity and Degradation Pattern Of Aly1281mentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

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Characterization and Application of an Alginate Lyase, Aly1281 from Marine Bacterium Pseudoalteromonas carrageenovora ASY5

et al. 2020

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“…of the alginate lyases, poly(a-lguluronate)lyase [EC 4.2.2.11](GLyase), which is specific to homopolymeric guluronic acid (polyguluronate) and produces 4-deoxy-l-erythro-hex-4-ene pyranosyluronate at the non-reducing terminal sugar residue from polyguluronate, has been purified from various bacterial sources and has been characterized. [1][2][3][4][5][6][7] The enzymes possess distinctive properties depending on its bacterial source; for example, GLyase isolated from a marine bacterium Vibrio sp. is highly tolerant of heat and denaturants; 5 GLyase from Corynebacterium sp.…”

Section: Onementioning

confidence: 99%

Calcium-sensitive extracellular poly(alpha-L-guluronate)lyase from a marine bacterium Pseudomonas sp. strain F6: Purification and some properties

Miyazaki¹,

Obata²,

Iwamoto³

et al. 2001

Fisheries Sci

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Poly(α‐L‐guluronate)lyase, as one of alginate lyases, was purified from the culture medium of a marine bacterium, Pseudomonas sp. strain F6, to an electrophoretically homogeneous state. The enzyme was shown to have a molecular mass of 36 kDa by sodium dodecylsulfate–polyacrylamide gel electrophoresis (SDS‐PAGE), and was most active at around pH 7.5 and was stable between pH 6.5 and pH 8.5. In the thermal stability experiments, the enzyme's activity diminished through an intermediate state with increasing incubation temperatures and was finally lost when heated at 100°C for 15 min. The addition of hen egg‐white lysozyme to the enzyme decreased thermal stability dramatically. The apparent retention of enzyme activity (approximately 50%) was observed after the addition of 6 M guanidine hydrochloride and 8 M urea. Enzyme activity was lost completely with 10 mMSDS, while the ordered structure, which is considered likely to be β‐structure, was markedly created. The similar conformational feature has also been created in marine bacterial and mollusc enzymes and the β‐structure is commonly observed in polyuronate lyases. The divalent cation (Ca2+) promoted the activity of the calcium chelator‐treated enzyme significantly, suggesting that Ca2+ is involved in the formation of the active intermediate between the acidic uronate(s) and amino acid side‐chain(s) of the enzyme.

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“…Two media were used in this work. A minimal media composed per liter of 0.5 g NaCl, 1 g (NH4)2 SO4,; 0.5 g KH2 PO4,; 1.5 g K2HPO4, 1.5; 0.2 g MgSO4,; 20 g agar, (Dong et al, 2008) and an LB liquid medium composed of 1.0% peptone, 0.1% yeast extract, and 3.0% NaCl, pH 7.8 (Kitamikado et al, 1992).…”

Section: Chemicals and Mediamentioning

confidence: 99%

Optimization of medium composition for extra cellular alginate lyases of a marine bacterium

ElAhwany¹,

El-Borai²

2012

Afr. J. Microbiol. Res.

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Among six marine isolates grown on minimal medium, an isolate AA4 was chosen based on its high alginase lyase specific activity (1.69 U/mg biomass), in comparison to other isolates. The isolate AA4 was identified as Bacillus subtilis, based on a partial sequence of the 16S rDNA gene. A 2 n factorial design was applied to elucidate media compositions that significantly affect alginate lyase formation. Sixteen trials were investigated and one with positive levels of yeast extract, peptone, sodium alginate and sodium chloride showed a 15-fold increase in specific enzyme activity. The F ratio revealed that two factors, sodium chloride and alginate, whether separately or combined are positively effective at a 1% level of significance.

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Two types of bacterial alginate lyases

Cited by 44 publications

References 22 publications

Characterization and Application of an Alginate Lyase, Aly1281 from Marine Bacterium Pseudoalteromonas carrageenovora ASY5

Characterization and Application of an Alginate Lyase, Aly1281 from Marine Bacterium Pseudoalteromonas carrageenovora ASY5

Calcium-sensitive extracellular poly(alpha-L-guluronate)lyase from a marine bacterium Pseudomonas sp. strain F6: Purification and some properties

Optimization of medium composition for extra cellular alginate lyases of a marine bacterium

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