Synergistic interactions among β‐laminarinase, β‐1,4‐glucanase, and β‐glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus during hydrolysis of β‐1,4‐, β‐1,3‐, and mixed‐linked polysaccharides

Driskill, Lance E.; Bauer, Michael W.; Kelly, Robert M.

doi:10.1002/(sici)1097-0290(1999)66:1<51::aid-bit5>3.3.co;2-b

Cited by 5 publications

(6 citation statements)

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“…These profiles suggest two possible mode of action: 1) if only one glycosyl hydrolase or polysaccharide lyase is involved in the depolymerization of the polysaccharide, it appears to directly release low molecular weight polysaccharide. Nevertheless, the size of the degradation products is not suitable with a classical exolytic enzyme (Stone et al 2008); 2) if two or more enzymes are active, they may act with a synergistic mode of action leading directly to low molecular weight polysaccharides (Driskill et al 1999a). The use of PNP substrates led to the detection of three strong exo---fucosidases.…”

Section: Discussionmentioning

confidence: 99%

Exopolysaccharide biosynthesis and biodegradation by a marine hydrothermal Alteromonas sp. strain

Lelchat

Cozien

Costaouëc³

et al. 2014

Appl Microbiol Biotechnol

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Alteromonas macleodii subsp. fijiensis biovar deepsane is a deep-sea ecotype exopolysaccharide-producing bacteria isolated from the polychaete annelid Alvinella pompejana. The high molecular weight biopolymer HYD657 produced by this strain, is the first marine exopolysaccharide (EPS) to be commercialized for cosmetic use. Depolymerization methods are necessary to elucidate the complete structure of this EPS and to generate potentially bioactive oligosaccharides. Enzymatic methods are useful for elucidating polysaccharide structure because they specifically cleave glycosidic bonds and do not require harsh chemical conditions. The HYD657 EPS is structurally complex and no commercially available enzymes are able to effectively degrade it. Here, we present the first results on the endogenous enzymatic depolymerization of a marine EPS of biotechnological interest by the producing strain. Enzymatic activity was detected in the bacterial lysate and was able to decrease the apparent molecular size of the EPS, releasing mainly oligosaccharides. The reduced form of the native polysaccharide showed a slightly modified osidic composition, particularly in terms of molar ratio. Several exoglycosidase activities were measured in the bacterial lysate using paranitrophenyl-osides.

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Section: Discussionmentioning

confidence: 99%

Exopolysaccharide biosynthesis and biodegradation by a marine hydrothermal Alteromonas sp. strain

Lelchat

Cozien

Costaouëc³

et al. 2014

Appl Microbiol Biotechnol

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“…A variety of thermostable poly(oligo)maltosaccharide‐modifying enzymes have been identified and characterized, which include α‐amylases (Laderman et al , 1993; Dong et al , 1997a), amylopullulanases (Dong et al , 1997b), cyclodextrin glucanotransferases (Tachibana et al , 1999; Rashid et al , 2002a), 4‐α‐glucanotransferases (Jeon et al , 1997), maltodextrin phosphorylases (Mizanur et al , 2008), cyclodextrinases (Hashimoto et al , 2001), and branching enzymes (Murakami et al , 2006). In addition, many enzymes that cleave β‐1,3‐ or β‐1,4‐glycosidic bonds have been studied such as β‐glucosidases, β‐galactosidases, β‐mannosidases, endo‐β‐1,3‐glucanases, chitinases, and β‐glucosaminidases (Kengen et al , 1993; Voorhorst et al , 1995; Bauer et al , 1996; Gueguen et al , 1997; Driskill et al , 1999; Matsui et al , 2000). Based on genome sequence predictions, members of the Thermococcales each harbor over 30 protease/peptidase‐related genes (Ward et al , 2002), and many of their protein products have been examined (Halio et al , 1996; Voorhorst et al , 1996; Story et al , 2005).…”

Section: Thermococcalesmentioning

confidence: 99%

Model organisms for genetics in the domain Archaea: methanogens, halophiles,ThermococcalesandSulfolobales

et al. 2011

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The tree of life is split into three main branches: eukaryotes, bacteria, and archaea. Our knowledge of eukaryotic and bacteria cell biology has been built on a foundation of studies in model organisms, using the complementary approaches of genetics and biochemistry. Archaea have led to some exciting discoveries in the field of biochemistry, but archaeal genetics has been slow to get off the ground, not least because these organisms inhabit some of the more inhospitable places on earth and are therefore believed to be difficult to culture. In fact, many species can be cultivated with relative ease and there has been tremendous progress in the development of genetic tools for both major archaeal phyla, the Euryarchaeota and the Crenarchaeota. There are several model organisms available for methanogens, halophiles, and thermophiles; in the latter group, there are genetic systems for Sulfolobales and Thermococcales. In this review, we present the advantages and disadvantages of working with each archaeal group, give an overview of their different genetic systems, and direct the neophyte archaeologist to the most appropriate model organism.

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“…Hyperthermophilic microorganisms thrive in high-temperature (60−110 °C) terrestrial and marine habitats at conditions that were previously regarded as incompatible with life. , Proteins from such microorganisms are stable at extreme temperatures and have attracted research interest not only due to important applications in biotechnology and biocatalysis but also because they are stable and active under conditions in which “normal” proteins are denatured. LamA is an extracellular endo-β1,3-glucanase from the hyperthermophilic Pyrococcus furiosus which hydrolyzes β1,3-linked glucose polysaccharides. , It is the most heat-stable endoglucanase reported until now and displays optimal enzymatic activity at 104 °C with substantially long deactivation time.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of an Endoglucanase from the HyperthermophilicPyrococcusfuriosuson Hydrophobic (Polystyrene) and Hydrophilic (Silica) Surfaces Increases Protein Heat Stability

Koutsopoulos

Oost

2004

Langmuir

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The interaction of an endoglucanase from the hyperthermophilic microorganism Pyrococcus furiosus with two types of surfaces, that is, hydrophobic polystyrene and hydrophilic silica, was investigated, and the adsorption isotherms were determined. The adsorbed hyperthermostable enzyme did not undergo loss of biological activity. A model was proposed for the mechanism of interaction of the enzyme with the surface based on the shape of the adsorption isotherm, the morphological characteristics of the enzyme, and the thermodynamic parameters of the system. The enzyme was irreversibly immobilized at the solid/liquid interface even at high temperatures, and most interestingly, it acquired further heat stabilization upon adsorption. The denaturation temperature increased from 108 degrees C in solution to 116 degrees C upon adsorption on hydrophilic silica particles. Adsorption on the hydrophobic polystyrene surface even shifted the denaturation temperature to 135 degrees C, the most extreme experimentally determined protein denaturation temperature ever reported. Maintenance of the biological function particularly at high temperatures is important for the development of solid substrate immobilized enzymes for applications in biocatalysis and biotechnology. This also presents an additional stabilization mechanism employed by nature where the extracellular hyperthermostable enzyme remains folded and active at the extreme temperatures of its natural environment by adsorption on the surface of rocks and other materials appearing in the surroundings of the microorganism.

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Synergistic interactions among β‐laminarinase, β‐1,4‐glucanase, and β‐glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus during hydrolysis of β‐1,4‐, β‐1,3‐, and mixed‐linked polysaccharides

Cited by 5 publications

References 0 publications

Exopolysaccharide biosynthesis and biodegradation by a marine hydrothermal Alteromonas sp. strain

Exopolysaccharide biosynthesis and biodegradation by a marine hydrothermal Alteromonas sp. strain

Model organisms for genetics in the domain Archaea: methanogens, halophiles,ThermococcalesandSulfolobales

Adsorption of an Endoglucanase from the HyperthermophilicPyrococcusfuriosuson Hydrophobic (Polystyrene) and Hydrophilic (Silica) Surfaces Increases Protein Heat Stability

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