Characterization of a thermostable and alkali-stable α-amylase from deep-sea bacterium Flammeovirga pacifica

Zhou, Guilan; Jin, Min; Cai, Yaping; Zeng, Runying

doi:10.1016/j.ijbiomac.2015.07.042

Cited by 11 publications

(6 citation statements)

References 30 publications

(28 reference statements)

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“…Another agarase belonging to GH50 was encoded by F. pacifica WPAGA1 ORF FlaGM002660, which showed a low amino-acid similarity (40.6%) to the β-agarase in Coraliomargarita akajimensis DSM 45221. Some studies reported that NAOSs are further degraded into neoagarobiose by the GH50-dependent β-agarase (Kim et al, 2010; Zhou et al, 2015). Finally, the glycoside hydrolase belonging to the GH117 family hydrolyses neoagarobiose into D-galactose and AHG (Ha et al, 2011; Hehemann et al, 2012; Pluvinage et al, 2013).…”

Section: Resultsmentioning

confidence: 99%

“…Previous studies showed that Flammeovirga bacteria can degrade various polysaccharides, especially agar, a typical polysaccharide derived from red seaweeds (Hou et al, 2015; Zhou et al, 2015). Flammeovirga bacteria have been proposed to possess a characteristic genomic basis for complex-polysaccharide usage and could thus adapt and survive in the marine environment.…”

Section: Discussionmentioning

confidence: 99%

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Genome Sequencing Reveals the Complex Polysaccharide-Degrading Ability of Novel Deep-Sea Bacterium Flammeovirga pacifica WPAGA1

Gao

Jin

et al. 2017

Front. Microbiol.

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Flammeovirga pacifica strain WPAGA1 is a Gram-negative, polysaccharide-degrading bacterium isolated from the marine sediment of the West Pacific Ocean. This strain is a cosmopolitan marine bacterium that uses complex polysaccharides as exclusive source of carbon and energy and plays a key role in the marine carbon cycle. Genome sequence analysis of strain WPAGA1 revealed that the assembled fine genome contains 6,610,326 bp with 32.89% G+C content, 5036 open reading frames (ORFs) and abundant genomic elements. Amongst these ORFs, 1022 genes encoding carbohydrate enzymes were found in the F. pacifica WPAGA1 genome. In addition, abundant putative enzymes involved in degrading polysaccharide were found. These enzymes include amylase, xylosidase, cellulase, alginate lyase, pectate lyase, rhamnogalacturonan lyase, chitinase, carrageenase, heparinase and fucosidase. To further investigate the use of these polysaccharides in strain WPAGA1, a schematic of various polysaccharide-degrading metabolic pathways were deduced from the genome sequence. This study showed that strain WPAGA1 may serve as a potential candidate for research of glycometabolism and have potential biotechnological and industrial applications and play key roles in the marine carbon cycle.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Genome Sequencing Reveals the Complex Polysaccharide-Degrading Ability of Novel Deep-Sea Bacterium Flammeovirga pacifica WPAGA1

Gao

Jin

et al. 2017

Front. Microbiol.

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“…The temperature effects on Aga4436 activity were investigated by conducting the enzymatic activity assay in PBS buffer (pH 7.4) at different temperatures ranging from 30 to 80 °C. The temperature effects on the thermostability of recombinant Aga4436 were studied by monitoring the remaining enzyme activity after incubating the Aga4436 in PBS buffer (pH 7.4) at different temperatures (30 °C, 24,25 The effects of pH on the stability of Aga4436 were evaluated by preincubating Aga4436 in pH 3.0−10.6 solutions at 50 °C for 60 min followed by assaying the residual activity.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Expression and Characterization of a Novel Thermostable and pH-Stable β-Agarase from Deep-Sea Bacterium Flammeovirga Sp. OC4

Chen

Hou

Jin

et al. 2016

J. Agric. Food Chem.

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A novel gene (aga4436), encoding a potential agarase of 456 amino acids, was identified in the genome of deep-sea bacterium Flammeovirga sp. OC4. Aga4436 belongs to the glycoside hydrolase 16 β-agarase family. Aga4436 was expressed in Escherichia coli as a fusion protein and purified. Recombinant Aga4436 showed an optimum agarase activity at 50-55 °C and pH 6.5, with a wide active range of temperatures (30-80 °C) and pHs (5.0-10.0). Notably, Aga4436 retained more than 90%, 80%, and 35% of its maximum activity after incubation at 30 °C, 40 °C, and 50 °C for 144 h, respectively, which exhibited an excellent thermostability in medium-high temperatures. Besides, Aga4436 displayed a remarkable tolerance to acid and alkaline environments, as it retained more than 70% of its maximum activity at a wide range of pHs from 3.0 to 10.0 after incubation in tested pHs for 60 min. These desirable properties of Aga4436 could make Aga4436 attractive in the food and nutraceutical industries.

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“…Thermostable amylolytic enzymes are one of the most interesting groups of enzymes for industrial processes, as they are important for the hydrolysis of starch at high temperatures, promoting the reactions and reducing the risk of contamination [66]. Several thermostable amylases have been reported from deep-sea microorganisms [51,52,67], some of which have been developed into products. For example, Fuelzyme ® , a product from Verenium Corporation (San Diego, CA, USA), utilises an alpha-amylase from the thermophile Thermococcus sp., which was isolated from a deep-sea hydrothermal vent.…”

Section: Deep-sea Thermophilic Enzymesmentioning

confidence: 99%

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

et al. 2019

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The deep sea, which is defined as sea water below a depth of 1000 m, is one of the largest biomes on the Earth, and is recognised as an extreme environment due to its range of challenging physical parameters, such as pressure, salinity, temperature, chemicals and metals (such as hydrogen sulphide, copper and arsenic). For surviving in such extreme conditions, deep-sea extremophilic microorganisms employ a variety of adaptive strategies, such as the production of extremozymes, which exhibit outstanding thermal or cold adaptability, salt tolerance and/or pressure tolerance. Owing to their great stability, deep-sea extremozymes have numerous potential applications in a wide range of industries, such as the agricultural, food, chemical, pharmaceutical and biotechnological sectors. This enormous economic potential combined with recent advances in sampling and molecular and omics technologies has led to the emergence of research regarding deep-sea extremozymes and their primary applications in recent decades. In the present review, we introduced recent advances in research regarding deep-sea extremophiles and the enzymes they produce and discussed their potential industrial applications, with special emphasis on thermophilic, psychrophilic, halophilic and piezophilic enzymes.Nearly three-quarters of the Earth's surface area is covered by ocean, the average depth of which is 3800 m, implying that the vast majority of our planet comprises deep-sea environments. The deep sea is one of the most mysterious and unexplored environments on the Earth, and it supports diverse microbial communities that play important roles in biogeochemical cycles [1]. The deep sea is also recognised as an extreme environment, as it is characterised by the absence of sunlight and the presence of predominantly low temperatures and high hydrostatic pressures, and these environmental conditions become even more challenging in particular habitats, such as deep-sea hydrothermal vents with their extremely high temperatures of >400 • C, deep hypersaline anoxic basins (DHABs) with their extremely high salinities and abysses of up to 11 km depth with their extremely high pressures.Deep-sea extremophiles are living organisms that can survive and proliferate in deep-sea environments that have extreme physical (pressure and temperature) and geochemical (pH, salinity and redox potential) conditions that are lethal to other organisms. The majority of deep-sea extremophiles belong to the prokaryotes, which are microorganisms in the domains of Archaea and Bacteria [2,3].These extremophilic microorganisms are functionally diverse and widely distributed in taxonomy [4], and they are classified into thermophiles (55 • C to 121 • C), psychrophiles (−2 • C to 20 • C), halophiles (2-5 M NaCl or KCl), piezophiles (>500 atmospheres), alkalophiles (pH > 8), acidophiles (pH < 4) and metalophiles (high concentrations of metals, e.g., copper, zinc, cadmium and arsenic) according to the extreme environments in which they grow and the extreme conditions they can tolerate. Ma...

show abstract

Characterization of a thermostable and alkali-stable α-amylase from deep-sea bacterium Flammeovirga pacifica

Cited by 11 publications

References 30 publications

Genome Sequencing Reveals the Complex Polysaccharide-Degrading Ability of Novel Deep-Sea Bacterium Flammeovirga pacifica WPAGA1

Genome Sequencing Reveals the Complex Polysaccharide-Degrading Ability of Novel Deep-Sea Bacterium Flammeovirga pacifica WPAGA1

Expression and Characterization of a Novel Thermostable and pH-Stable β-Agarase from Deep-Sea Bacterium Flammeovirga Sp. OC4

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

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