Relevant bibliographies by topics / Alginate lyase

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Academic literature on the topic 'Alginate lyase'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 February 2022

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Journal articles on the topic "Alginate lyase"

1

Yin, Rui, Yan-Jun Yi, Zhuo Chen, Bao-Xun Wang, Xue-Han Li, and Yan-Xia Zhou. "Characterization of a New Biofunctional, Exolytic Alginate Lyase from Tamlana sp. s12 with High Catalytic Activity and Cold-Adapted Features." Marine Drugs 19, no. 4 (March 28, 2021): 191. http://dx.doi.org/10.3390/md19040191.

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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. Although a large number of alginate lyases have been characterized, few can efficiently degrade alginate comprised of mannuronate (M) and guluronate (G) at low temperatures by means of an exolytic mode. In this study, the gene of a new exo-alginate lyase—Alys1—with high activity (1350 U/mg) was cloned from a marine strain, Tamlana sp. s12. When sodium alginate was used as a substrate, the recombinant enzyme showed optimal activity at 35 °C and pH 7.0–8.0. Noticeably, recombinant Alys1 was unstable at temperatures above 30 °C and had a low melting temperature of 56.0 °C. SDS and EDTA significantly inhibit its activity. These data indicate that Alys1 is a cold-adapted enzyme. Moreover, the enzyme can depolymerize alginates polyM and polyG, and produce a monosaccharide as the minimal alginate oligosaccharide. Primary substrate preference tests and identification of the final oligosaccharide products demonstrated that Alys1 is a bifunctional alginate lyase and prefers M to G. These properties make Alys1 a valuable candidate in both basic research and industrial applications.
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Subaryono, Subaryono, Rosmawaty Peranginangin, Maggy Thenawidjaja Suhartono, and Fransiska Rungkat Zakaria. "Alginate Lyases: Sources, Mechanism of Activity and Potencial Application." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 8, no. 3 (December 21, 2013): 105. http://dx.doi.org/10.15578/squalen.v8i3.39.

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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 properties, and polysaccharide structure analysis. The products of alginate lyase, polysaccharide structure analysis, alginate oligosaccharides (AOS) have many biological activities including act as prebiotics, immune modulator, anticoagulation, antioxidant, anticancer, growth promoting activities, promote production of antibiotics and ethanol. In relation to the importance of alginate lyases, their potential aplications and prospect in development of new bioactive products, we present review of the enzymes, sources, mechanism of activity and potential applications. This paper also discussed some new biological engineering in alginate lyase production.
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Wang, Yanan, Xuehong Chen, Xiaolin Bi, Yining Ren, Qi Han, Yu Zhou, Yantao Han, Ruyong Yao, and Shangyong Li. "Characterization of an Alkaline Alginate Lyase with pH-Stable and Thermo-Tolerance Property." Marine Drugs 17, no. 5 (May 24, 2019): 308. http://dx.doi.org/10.3390/md17050308.

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Alginate oligosaccharides (AOS) show versatile bioactivities. Although various alginate lyases have been characterized, enzymes with special characteristics are still rare. In this study, a polysaccharide lyase family 7 (PL7) alginate lyase-encoding gene, aly08, was cloned from the marine bacterium Vibrio sp. SY01 and expressed in Escherichia coli. The purified alginate lyase Aly08, with a molecular weight of 35 kDa, showed a specific activity of 841 U/mg at its optimal pH (pH 8.35) and temperature (45 °C). Aly08 showed good pH-stability, as it remained more than 80% of its initial activity in a wide pH range (4.0–10.0). Aly08 was also a thermo-tolerant enzyme that recovered 70.8% of its initial activity following heat shock treatment for 5 min. This study also demonstrated that Aly08 is a polyG-preferred enzyme. Furthermore, Aly08 degraded alginates into disaccharides and trisaccharides in an endo-manner. Its thermo-tolerance and pH-stable properties make Aly08 a good candidate for further applications.
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Kam, Natania, Yoo Jung Park, Eun Yeol Lee, and Hee Sook Kim. "Molecular identification of a polyM-specific alginate lyase from Pseudomonas sp. strain KS-408 for degradation of glycosidic linkages between two mannuronates or mannuronate and guluronate in alginate." Canadian Journal of Microbiology 57, no. 12 (December 2011): 1032–41. http://dx.doi.org/10.1139/w11-106.

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An alginate lyase gene of a newly isolated Pseudomonas sp. strain KS-408 was cloned by using PCR with the specific primers designed from homologous nucleotide sequences. A partial protein sequence of KS-408 alginate lyase was homology-modeled on the basis of the crystal structure of A1-III alginate lyase from Sphingomonas sp. strain A1. The proposed 3-D structure of KS-408 alginate lyase shows that Asn-198, His-199, Arg-246, and Tyr-253 residues are conserved for the catalytic active site. The recombinant KS-408-1F (with signal peptide) and KS-408-2F (without signal peptide) alginate lyases with the (His)6 tag consist of 393 (44.5 kDa) and 372 (42.4 kDa) amino acids with isoelectric points of 8.64 and 8.46, respectively. The purified recombinant KS-408 alginate lyase was very stable when it was incubated at 40 °C for 30 min. Alginate oligosaccharides produced by the KS-408-2F alginate lyase were purified on a Bio-Gel P2 column and analyzed by thin-layer chromatography, fast-protein liquid chromatography, and electrospray ionization mass spectrometry. 1H NMR data showed that the KS-408-2F alginate lyase cleaved the glycosidic linkages between two mannuronates (mannuronate-β(1–4)-mannuronate) or mannuronate and guluronate (mannuronate-β(1–4)-guluronate), indicating that the KS-408 alginate lyase is a polyM-specific lyase.
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Zhuang, Jingjing, Keke Zhang, Xiaohua Liu, Weizhi Liu, Qianqian Lyu, and Aiguo Ji. "Characterization of a Novel PolyM-Preferred Alginate Lyase from Marine Vibrio splendidus OU02." Marine Drugs 16, no. 9 (August 22, 2018): 295. http://dx.doi.org/10.3390/md16090295.

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Alginate lyases are enzymes that degrade alginate into oligosaccharides which possess a variety of biological activities. Discovering and characterizing novel alginate lyases has great significance for industrial and medical applications. In this study, we reported a novel alginate lyase, AlyA-OU02, derived from the marine Vibrio splendidus OU02. The BLASTP searches showed that AlyA-OU02 belonged to polysaccharide lyase family 7 (PL7) and contained two consecutive PL7 domains, which was rare among the alginate lyases in PL7 family. Both the two domains, AlyAa and AlyAb, had lyase activities, while AlyAa exhibited polyM preference, and AlyAb was polyG-preferred. In addition, the enzyme activity of AlyAa was much higher than AlyAb at 25 °C. The full-length enzyme of AlyA-OU02 showed polyM preference, which was the same as AlyAa. AlyAa degraded alginate into di-, tri-, and tetra-alginate oligosaccharides, while AlyAb degraded alginate into tri-, tetra-, and penta-alginate oligosaccharides. The degraded products of AlyA-OU02 were similar to AlyAa. Our work provided a potential candidate in the application of alginate oligosaccharide production and the characterization of the two domains might provide insights into the use of alginate of this organism.
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Badur, Ahmet H., Sujit Sadashiv Jagtap, Geethika Yalamanchili, Jung-Kul Lee, Huimin Zhao, and Christopher V. Rao. "Alginate Lyases from Alginate-Degrading Vibrio splendidus 12B01 Are Endolytic." Applied and Environmental Microbiology 81, no. 5 (January 2, 2015): 1865–73. http://dx.doi.org/10.1128/aem.03460-14.

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ABSTRACTAlginate lyases are enzymes that degrade alginate through β-elimination of the glycosidic bond into smaller oligomers. We investigated the alginate lyases fromVibrio splendidus12B01, a marine bacterioplankton species that can grow on alginate as its sole carbon source. We identified, purified, and characterized four polysaccharide lyase family 7 alginates lyases, AlyA, AlyB, AlyD, and AlyE, fromV. splendidus12B01. The four lyases were found to have optimal activity between pH 7.5 and 8.5 and at 20 to 25°C, consistent with their use in a marine environment. AlyA, AlyB, AlyD, and AlyE were found to exhibit a turnover number (kcat) for alginate of 0.60 ± 0.02 s−1, 3.7 ± 0.3 s−1, 4.5 ± 0.5 s−1, and 7.1 ± 0.2 s−1, respectively. TheKmvalues of AlyA, AlyB, AlyD, and AlyE toward alginate were 36 ± 7 μM, 22 ± 5 μM, 60 ± 2 μM, and 123 ± 6 μM, respectively. AlyA and AlyB were found principally to cleave the β-1,4 bonds between β-d-mannuronate and α-l-guluronate and subunits; AlyD and AlyE were found to principally cleave the α-1,4 bonds involving α-l-guluronate subunits. The four alginate lyases degrade alginate into longer chains of oligomers.
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Li, Qian, Fu Hu, Benwei Zhu, Yun Sun, and Zhong Yao. "Biochemical Characterization and Elucidation of Action Pattern of a Novel Polysaccharide Lyase 6 Family Alginate Lyase from Marine Bacterium Flammeovirga sp. NJ-04." Marine Drugs 17, no. 6 (May 31, 2019): 323. http://dx.doi.org/10.3390/md17060323.

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Alginate lyases have been widely used to prepare alginate oligosaccharides in food, agricultural, and medical industries. Therefore, discovering and characterizing novel alginate lyases with excellent properties has drawn increasing attention. Herein, a novel alginate lyase FsAlyPL6 of Polysaccharide Lyase (PL) 6 family is identified and biochemically characterized from Flammeovirga sp. NJ-04. It shows highest activity at 45 °C and could retain 50% of activity after being incubated at 45 °C for 1 h. The Thin-Layer Chromatography (TLC) and Electrospray Ionization Mass Spectrometry (ESI-MS) analysis indicates that FsAlyPL6 endolytically degrades alginate polysaccharide into oligosaccharides ranging from monosaccharides to pentasaccharides. In addition, the action pattern of the enzyme is also elucidated and the result suggests that FsAlyPL6 could recognize tetrasaccharide as the minimal substrate and cleave the glycosidic bonds between the subsites of −1 and +3. The research provides extended insights into the substrate recognition and degradation pattern of PL6 alginate lyases, which may further expand the application of alginate lyases.
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Pilgaard, Bo, Marlene Vuillemin, Jesper Holck, Casper Wilkens, and Anne S. Meyer. "Specificities and Synergistic Actions of Novel PL8 and PL7 Alginate Lyases from the Marine Fungus Paradendryphiella salina." Journal of Fungi 7, no. 2 (January 25, 2021): 80. http://dx.doi.org/10.3390/jof7020080.

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Alginate is an anionic polysaccharide abundantly present in the cell walls of brown macroalgae. The enzymatic depolymerization is performed solely by alginate lyases (EC 4.2.2.x), categorized as polysaccharide lyases (PLs) belonging to 12 different PL families. Until now, the vast majority of the alginate lyases have been found in bacteria. We report here the first extensive characterization of four alginate lyases from a marine fungus, the ascomycete Paradendryphiella salina, a known saprophyte of seaweeds. We have identified four polysaccharide lyase encoding genes bioinformatically in P. salina, one PL8 (PsMan8A), and three PL7 alginate lyases (PsAlg7A, -B, and -C). PsMan8A was demonstrated to exert exo-action on polymannuronic acid, and no action on alginate, indicating that this enzyme is most likely an exo-acting polymannuronic acid specific lyase. This enzyme is the first alginate lyase assigned to PL8 and polymannuronic acid thus represents a new substrate specificity in this family. The PL7 lyases (PsAlg7A, -B, and -C) were found to be endo-acting alginate lyases with different activity optima, substrate affinities, and product profiles. PsAlg7A and PsMan8A showed a clear synergistic action for the complete depolymerization of polyM at pH 5. PsAlg7A depolymerized polyM to mainly DP5 and DP3 oligomers and PsMan8A to dimers and monosaccharides. PsAlg7B and PsAlg7C showed substrate affinities towards both polyM and polyG at pH 8, depolymerizing both substrates to DP9-DP2 oligomers. The findings elucidate how P. salina accomplishes alginate depolymerization and provide insight into an efficient synergistic cooperation that may provide a new foundation for enzyme selection for alginate degradation in seaweed bioprocessing.
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Wei, Wei, Xin Zhang, Zhaozhi Hou, Xinyu Hu, Yuan Wang, Caizheng Wang, Shujing Yang, Henglin Cui, and Lin Zhu. "Microbial Regulation of Deterioration and Preservation of Salted Kelp under Different Temperature and Salinity Conditions." Foods 10, no. 8 (July 26, 2021): 1723. http://dx.doi.org/10.3390/foods10081723.

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High salinity is an effective measure to preserve kelp, but salted kelp can still deteriorate after long-term preservation. In order to clarify the key conditions and microbial behavior of salted kelp preservation, 10% (S10), 20% (S20), and 30% (S30) salt concentrations were evaluated at 25 °C (T25) and 4 °C (T4). After 30 days storage, these salted kelps showed different states including rot (T25S10), softening (T25S20), and undamaged (other samples). By detecting polysaccharide lyase activity and performing high-throughput sequencing of the prokaryotic 16S rRNA sequence and metagenome, we found that deteriorated kelps (T25S10 and T25S20) had significantly higher alginate lyase activity and bacterial relative abundance than other undamaged samples. Dyella, Saccharophagus, Halomonas, Aromatoleum, Ulvibacter, Rhodopirellula, and Microbulbifer were annotated with genes encoding endonuclease-type alginate lyases, while Bacillus and Thiobacillus were annotated as the exonuclease type. Additionally, no alginate lyase activity was detected in undamaged kelps, whose dominant microorganisms were halophilic archaea without alginate lyase-encoding genes. These results indicated that room-temperature storage may promote salted kelp deterioration due to the secretion of bacterial alginate lyase, while ultra-high-salinity and low-temperature storage can inhibit bacterial alginate lyase and promote the growth of halophilic archaea without alginate lyase, thus achieving the preservation of salted kelp.
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Xu, Fei, Xiu-Lan Chen, Xiao-Hui Sun, Fang Dong, Chun-Yang Li, Ping-Yi Li, Haitao Ding, Yin Chen, Yu-Zhong Zhang, and Peng Wang. "Structural and molecular basis for the substrate positioning mechanism of a new PL7 subfamily alginate lyase from the arctic." Journal of Biological Chemistry 295, no. 48 (September 23, 2020): 16380–92. http://dx.doi.org/10.1074/jbc.ra120.015106.

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Alginate lyases play important roles in alginate degradation in the ocean. Although a large number of alginate lyases have been characterized, little is yet known about those in extremely cold polar environments, which may have unique mechanisms for environmental adaptation and for alginate degradation. Here, we report the characterization of a novel PL7 alginate lyase AlyC3 from Psychromonas sp. C-3 isolated from the Arctic brown alga Laminaria, including its phylogenetic classification, catalytic properties, and structure. We propose the establishment of a new PM-specific subfamily of PL7 (subfamily 6) represented by AlyC3 based on phylogenetic analysis and enzymatic properties. Structural and biochemical analyses showed that AlyC3 is a dimer, representing the first dimeric endo-alginate lyase structure. AlyC3 is activated by NaCl and adopts a novel salt-activated mechanism; that is, salinity adjusts the enzymatic activity by affecting its aggregation states. We further solved the structure of an inactive mutant H127A/Y244A in complex with a dimannuronate molecule and proposed the catalytic process of AlyC3 based on structural and biochemical analyses. We show that Arg82 and Tyr190 at the two ends of the catalytic canyon help the positioning of the repeated units of the substrate and that His127, Tyr244, Arg78, and Gln125 mediate the catalytic reaction. Our study uncovers, for the first time, the amino acid residues for alginate positioning in an alginate lyase and demonstrates that such residues involved in alginate positioning are conserved in other alginate lyases. This study provides a better understanding of the mechanisms of alginate degradation by alginate lyases.
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Dissertations / Theses on the topic "Alginate lyase"

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ANDRIEU, LAURENCE. "Caracterisation d'une alginate lyase de pseudomonas aeruginosa." Paris 11, 1995. http://www.theses.fr/1995PA112264.

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Pseudomonas aeruginosa est une bacterie pathogene opportuniste pouvant entrainer des infections graves, surtout au niveau des poumons des malades atteints de mucoviscidose. Sous l'effet de facteurs environnementaux, les bacteries vont produire des exopolysaccharides, les alginates, facteur important de la virulence de la bacterie. Les alginates sont des polymeres d'acides d-mannuronique et l-guluronique en liaison 1-4. Ils sont hydrolyses par un enzyme specifique, l'alginate lyase, qui catalyse une reaction de -elimination entre deux residus d-mannurosyl ou l-gulurosyl. Une activite alginolytique a ete mise en evidence chez deux souches mucoides de p. Aeruginosa. Cette activite est portee par une proteine homodimerique de 130 kda, intracellulaire en association avec la face interne de la membrane cytoplasmique. Le gene de structure de l'alginate lyase a ete clone a partir d'une banque d'adn genomique construite dans l'adn du phage lambda gt 11. Le gene algl, porte par un fragment de 4,4 kpb, est exprime chez e. Coli y 1090 en une proteine de 130 kda. Le sous-clonage de fragment de 4,4 kpb dans le gene cat du plasmide pbr 329 nous a permis de construire la carte de restriction du fragment, et de montrer que ce gene introduit chez e. Coli mc 1061, etait exprime, ce qui suggere que le gene a ete clone avec son propre promoteur. Les sous-clonages du fragment entier et de fragments de restriction, puis le clonage de fragments issus de l'hydrolyse controlee de l'insert de 4,4 kpb par la dnase i nous ont permis de determiner la totalite de la sequence nucleotidique. L'analyse de la sequence a revele la presence d'une phase ouverte de lecture de 2052 nucleotides, codant pour une proteine de poids moleculaire predit de 74 kda qui est en accord avec celui du monomere de l'alginate lyase determine par electrophorese sur gel sds, et qui doit correspondre au gene algl. De plus, la presence de sequences de fixation des ribosomes et de l'arn polymerase confirment que le gene algl possede son propre promoteur. Ces resultats montrent que l'alginate lyase mise en evidence est differente de celles caracterises chez d'autres souches de p. Aeruginosa
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2

Malissard, Martine. "Alginate lyase d'une bactérie marine ATCC 433367 : purification, clonage, séquence du gène et expression chez Escherichia coli." Lyon 1, 1993. http://www.theses.fr/1993LYO10243.

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L'alginate, facteur de virulence de p. Aeruginosa, protege la bacterie de la phagocytose et empeche la penetration des antibiotiques. Le but de notre travail etait de selectionner et d'obtenir en grande quantite une alginate lyase montrant une bonne specificite pour l'alginate de p. Aeruginosa. Une premiere enzyme produite par b. Circulans atcc 15518 a ete purifiee. Le rendement est faible et l'analyse de la fraction purifiee met en evidence un complexe indissociable enzyme-polysaccharide. La souche d'e. Coli tc4/pal a3, contient le plasmide pal a3 dans lequel le gene alxm codant pour l'alginate lyase de la bacterie marine atcc 433367 a ete clone, elle est productrice d'alginate lyase. L'enzyme est periplasmique, sa purification a necessite deux etapes. Le rendement est de 17% (0,05 mg/l de culture) et l'activite specifique sur un alginate commercial non acetyle est de 40 unites/mg, elle est deux fois plus importante sur un alginate de p. Aeruginosa acetyle a 46%. Sa masse est de 30 kda par electrophorese en conditions non reductrices. On observe deux fragments de 20 et 10 kda en conditions reductrices, ce qui demontre une proteolyse de la proteine a l'interieur d'un pont disulfure. Le gene alxm a ete sequence, amplifie par pcr, et le fragment resultant a ete clone dans le pet 12a. Le plasmide recombinant a servi a transformer des souches lysogeniques d'e. Coli. La purification de l'enzyme surexprimee comporte une seule etape, le rendement est de 67% (56 mg/l de culture). Des etudes de prediction de structure secondaire et des recherches d'homologie avec trois autres alginate lyases ont ete effectuees
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Boyen, Catherine. "Etude de la paroi cellulaire des pheophycees : approche physicochimique et immunocytologique, preparation d'enzymes de degradation specifiques." Paris 6, 1987. http://www.theses.fr/1987PA066281.

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Etude de la composition osidique d'alginate des genres pelvetia, fucus, arcophyllum, sargassum et laminaria. Preparation et caracterisation des alginates-lyases a partir de divers mollusques marins et d'une bacterie marine. Etude comparee de la regeneration de la paroi du protoplaste et de la mise en place normale de la paroi du zygote de fucus distichus par marquage avec des anticorps monoclonaux
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4

Cross, Bronwen. "Cloning and molecular characterisation of four alginate lyase genes from Vibrio midae SY9 : an enteric bacterium from the abalone Haliotis midae." Doctoral thesis, University of Cape Town, 2010. http://hdl.handle.net/11427/4253.

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Includes abstract.
Includes bibliographical references (leaves 241-268).
Alginate is a linear, un-branched polysaccharide of (1-4)-linked -D-mannuronate (M) and its C-5 epimer, -L-guluronate acid (G). These uronic acids are arranged in three different block types in the alginate polymer; poly-M, poly-G or poly-MG. Alginate lyases are enzymes that utilize a -elimination reaction to depolymerise the alginate polymer resulting in cleavage of the (1-4)-O-glycosidic linkage between monomers and the formation of an unsaturated uronic acid at the new non-reducing terminus. Alginate lyases have been isolated from a wide range of sources including marine invertebrates and marine bacteria, which often produce more than one alginate lyase enzyme. Haliotis midae is the commercially important abalone species found along the South African coast. Over-fishing and poaching of this species has led to a depletion of the naturally occurring populations and closure of the recreational and commercial fisheries. Abalone farming was initiated and has rapidly increased in response to the increasing demand for this delicacy. However, there are many problems associated with abalone aquaculture, the most significant being disease and the slow growth rates of the animals. The use of probiotics in abalone aquaculture is a potential solution to both of these problems.
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尹, 惠珍. "Crystallographic Studies on Structure of Alginate Lyases of Sphingomonas species A1." Doctoral thesis, Kyoto University, 2000. http://hdl.handle.net/2433/181081.

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京都大学
0048
新制・論文博士
博士(農学)
乙第10421号
論農博第2300号
新制||農||805(附属図書館)
学位論文||H12||N3420(農学部図書室)
UT51-2000-F487
(主査)教授 村田 幸作, 教授 熊谷 英彦, 教授 内海 成
学位規則第4条第2項該当
Doctor of Agricultural Science
Kyoto University
DAM
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Chavagnat, Frédéric. "Production d'anticorps monoclonaux anti-alginate : surproduction, structure et activité des alginate lyases bactériennes AlxM et Algi en vue de la préparation d'un complexe anti-alginate contre Pseudomonas aeruginosa." Lyon 1, 1996. http://www.theses.fr/1996LYO10040.

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L'alginate, polymere d'acides mannronique et guluronique, est un facteur de virulence de pseudomonas aeruginosa. Il protege la bacterie de la phagocytose et de l'action des antibiotiques. Le but de mon travail etait d'obtenir des anticorps anti-alginate et de produire en grande quantite des alginate lyases actives sur l'alginate de p. Aeruginosa. Des anticorps monoclonaux igm anti-alginate ont ete obtenus par immunisation de souris avec un conjugue bsa/alginate de p. Aeruginosa. Ils ont ete purifies puis reduits en monomeres pour un couplage avec la peroxydase. Le conjugue fonctionnel obtenu a permis de valider la methode pour la synthese du conjugue alginate lyase/anticorps anti-alginate. L'alginate lyase alxm de la bacterie marine atcc 433367 a ete surproduite chez e. Coli et purifiee en une seule etape: sa masse est de 30 kda, le rendement de purification est de 90% (32 mg/l de culture). Les conditions optimales d'activite de alxm ont ete determinees, puis utilisees pour l'etude de sa specificite. Alxm est une mannuronate lyase, elle produit, par un mecanisme de -elimination avec retention de configuration, un oligomere de dp3 quel que soit le substrat. Ses parametres cinetiques ont ete determines pour des substrats oligomeriques de structure definie. Le gene algi codant pour l'alginate lyase produite par pseudomonas alginovora a ete amplifie par pcr directe et inverse, sequence puis clone dans le vecteur de surexpression pet-22b. L'enzyme surproduite a 18c dans e. Coli, algisur, a ete purifiee en une seule etape par chromatographie d'affinite avec un rendement de 67% (5 mg/l de culture). Conformement a la strategie de surexpression, sa masse de 24635 da correspond a celle de algi additionnee de la sequence poly(his). Algi et algisur ont le meme profil d'activite avec une specificite de type mannuronate lyase. Une etude par hca sur alxm, algi et quatre autres alginate lyases de structures primaires connues a permis de classer ces enzymes deux par deux en trois familles
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7

Thomas, François. "Identification et caractérisation du système alginolytique de la bactérie marine Zobellia galactanivorans." Paris 6, 2011. http://hal.upmc.fr/tel-01110859v1.

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La bactérie marine Zobellia galactanivorans dégrade un grand nombre de polysaccharides de macroalgues. Je me suis intéressé à la dégradation de l'alginate, un composé pariétal des algues brunes. L'annotation du génome a confirmé le potentiel de cette bactérie pour la dégradation de polysaccharides. Z. Galactanivorans possède 7 alginate lyases putatives. Ces gènes sont organisés en deux clusters comprenant d'autres acteurs de la dégradation de l'alginate. J'ai montré que ces clusters sont transcrits au sein d'ARN polycistroniques et constituent des opérons alginolytiques. Une approche transcriptomique ciblée a révélé que l'expression des gènes identifiés dépend de la présence d'alginate. Des analyses de génomique comparative ont montré que cette voie métabolique est conservée chez d'autres bactéries, mettant en évidence des événements de transferts de gènes. La compréhension de l'utilisation de l'alginate a été élargie par un profilage transcriptomique à l'échelle du génome chez Z. Galactanivorans. Il a permis d'identifier d'autres gènes répondant à la présence d'alginate et pouvant participer à la perception, la prise en charge ou la dégradation du substrat. J'ai entrepris une stratégie de clonage sur 21 gènes impliqués dans l'utilisation de l'alginate. Deux nouvelles alginate lyases PL7 de Z. Galactanivorans ont ensuite été surexprimées chez E. Coli, purifiées et cristallisées. Leur spécificité et mode d'action ont été étudiés, menant à l'identification d'AlyA1 comme endo-guluronate lyase et AlyA5 comme exo-guluronate lyase. Leurs structures 3D ont été résolues. Tous les résultats ont été intégrés pour proposer un modèle de système alginolytique chez Z. Galactanivorans
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8

Miyake, Osamu. "Studies on molecular diversity, evolutional process, and X-ray crystal structure of bacterial alginate lyases." Kyoto University, 2004. http://hdl.handle.net/2433/145440.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第11202号
農博第1450号
新制||農||900(附属図書館)
学位論文||H16||N3974(農学部図書室)
22786
UT51-2004-T171
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 村田 幸作, 教授 加藤 暢夫, 教授 井上 國世
学位規則第4条第1項該当
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9

Ogura, Kohei. "X-ray Crystallographic Studies on Reaction Diversity of Alginate Lyases with β-Jelly Roll as a Common Basic Scaffold." Kyoto University, 2010. http://hdl.handle.net/2433/120475.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第15432号
農博第1817号
新制||農||980(附属図書館)
学位論文||H22||N4531(農学部図書室)
27910
京都大学大学院農学研究科食品生物科学専攻
(主査)教授 村田 幸作, 教授 北畠 直文, 教授 三上 文三
学位規則第4条第1項該当
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Beyerodt, Christian [Verfasser], Markus [Akademischer Betreuer] Pietzsch, Reinhard [Akademischer Betreuer] Neubert, and Christoph [Akademischer Betreuer] Syldatk. "Untersuchung zur Produktion und gerichteten Immobilisierung einer Alginat Lyase aus Sphingomonas sp. A1 / Christian Beyerodt ; Markus Pietzsch, Reinhard Neubert, Christoph Syldatk." Halle, 2016. http://d-nb.info/1116950596/34.

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Book chapters on the topic "Alginate lyase"

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Schomburg, Dietmar, and Margit Salzmann. "Alginate lyase." In Enzyme Handbook 1, 909–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_205.

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Gacesa, P., G. S. Leaves, and A. J. Weightman. "Genetic analysis of Klebsiella pneumoniae alginate lyase by transposon Tn10 mutagenesis." In Twelfth International Seaweed Symposium, 571–75. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-4057-4_84.

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Gacesa, Peter, and Richard C. Caswell. "Control and heterologous expression in Escherichia coli of the Klebsiella pneumoniae gene encoding alginate lyase." In Thirteenth International Seaweed Symposium, 661–65. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-2049-1_96.

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Larsen, Bjørn, Kirsti Hoøen, and Kjetill Østgaard. "Kinetics and specificity of alginate lyases." In Fourteenth International Seaweed Symposium, 557–61. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1998-6_74.

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Romeo, Tony, John C. Bromley, and James F. Preston. "Alginate Lyases of Varying Substrate Specificities from Marine Bacteria." In Biomass Energy Development, 303–20. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-0590-4_26.

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Takeshita, S., and T. Oda. "Usefulness of Alginate Lyases Derived from Marine Organisms for the Preparation of Alginate Oligomers with Various Bioactivities." In Marine Enzymes Biotechnology: Production and Industrial Applications, Part II - Marine Organisms Producing Enzymes, 137–60. Elsevier, 2016. http://dx.doi.org/10.1016/bs.afnr.2016.07.003.

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Inoue, Akira. "Characterization of PL-7 Family Alginate Lyases From Marine Organisms and Their Applications." In Marine Enzymes and Specialized Metabolism - Part B, 499–524. Elsevier, 2018. http://dx.doi.org/10.1016/bs.mie.2018.01.030.

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Ojima, Takao, Ryuji Nishiyama, and Akira Inoue. "Production of value-added materials from alginate using alginate lyases and 4-deoxy-l-erythro-5-hexoseulose uronic acid–metabolic enzymes from alginolytic bacteria and marine gastropods." In Enzymatic Technologies for Marine Polysaccharides, 495–510. CRC Press, 2019. http://dx.doi.org/10.1201/9780429058653-22.

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Conference papers on the topic "Alginate lyase"

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Lee, Eun Yeol, and Hee Sook Kim. "Molecular Characterization of Exolytic Alginate Lyase for Saccharification of Alginate into Unsaturated Uronic Acid." In 14th Asia Pacific Confederation of Chemical Engineering Congress. Singapore: Research Publishing Services, 2012. http://dx.doi.org/10.3850/978-981-07-1445-1_626.

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