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See detailCold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis
Hoyoux, A.; Jennes, I.; Dubois, P. et al

in Applied and Environmental Microbiology (2001), 67(4), 1529-35

The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of ... [more ▼]

The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of the purified enzyme indicate that the beta-galactosidase subunit is composed of 1,038 amino acids with a calculated M(r) of 118,068. This beta-galactosidase shares structural properties with Escherichia coli beta-galactosidase (comparable subunit mass, 51% amino sequence identity, conservation of amino acid residues involved in catalysis, similar optimal pH value, and requirement for divalent metal ions) but is characterized by a higher catalytic efficiency on synthetic and natural substrates and by a shift of apparent optimum activity toward low temperatures and lower thermal stability. The enzyme also differs by a higher pI (7.8) and by specific thermodynamic activation parameters. P. haloplanktis beta-galactosidase was expressed in E. coli, and the recombinant enzyme displays properties identical to those of the wild-type enzyme. Heat-induced unfolding monitored by intrinsic fluorescence spectroscopy showed lower melting point values for both P. haloplanktis wild-type and recombinant beta-galactosidase compared to the mesophilic enzyme. Assays of lactose hydrolysis in milk demonstrate that P. haloplanktis beta-galactosidase can outperform the current commercial beta-galactosidase from Kluyveromyces marxianus var. lactis, suggesting that the cold-adapted beta-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants. [less ▲]

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See detailEnzyme Activity Determination on Macromolecular Substrates by Isothermal Titration Calorimetry: Application to Mesophilic and Psychrophilic Chitinases
Lonhienne, T.; Baise, Etienne ULg; Feller, Georges ULg et al

in Biochimica et Biophysica Acta (2001), 1545(1-2), 349-56

Isothermal titration calorimetry has been applied to the determination of the kinetic parameters of chitinases (EC 3.2.1.14) by monitoring the heat released during the hydrolysis of chitin glycosidic ... [more ▼]

Isothermal titration calorimetry has been applied to the determination of the kinetic parameters of chitinases (EC 3.2.1.14) by monitoring the heat released during the hydrolysis of chitin glycosidic bonds. Experiments were carried out using two different macromolecular substrates: a soluble polymer of N-acetylglucosamine and the insoluble chitin from crab shells. Different experimental temperatures were used in order to compare the thermodependence of the activity of two chitinases from the psychrophile Arthrobacter sp. TAD20 and of chitinase A from the mesophile Serratia marcescens. The method allowed to determine unequivocally the catalytic rate constant k(cat), the activation energy (E(a)) and the thermodynamic activation parameters (DeltaG(#), DeltaH(#), DeltaS(#)) of the chitinolytic reaction on the soluble substrate. The catalytic activity has also been determined on insoluble chitin, which displays an effect of substrate saturation by chitinases. On both substrates, the thermodependence of the activity of the psychrophilic chitinases was lower than that observed with the mesophilic counterpart. [less ▲]

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See detailCalorimetric characterization of mutants from a cold-active alpha-amylase
D'Amico, Salvino; Gerday, Charles ULg; Feller, Georges ULg

Poster (2001)

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See detailStructural determinants of cold adaptation and stability in a psychrophilic enzyme
D'Amico, Salvino; Gerday, Charles ULg; Feller, Georges ULg

Conference (2001)

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See detailPsychrophiles and their cold-active enzymes
Gerday, Charles ULg; Feller, Georges ULg

Conference (2001)

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See detailA novel family 8 xylanase : characteristics and evolutionary aspects
Collins, Tony; Meuwis, Marie-Alice ULg; Feller, Georges ULg et al

Poster (2001)

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See detailHow to rapidly increase the overproduction of a recombinant enzyme?
Georlette, Daphné; D'Amico, Salvino; Anderlei, T. et al

Poster (2001)

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See detailCold-adapted enzymes: an unachieved symphony
D'Amico, Salvino ULg; Claverie, P.; Collins, T. et al

in Storey, K. B.; Storey, J. M. (Eds.) Cell and Molecular Responses to Stress vol.2. Protein adaptations and signal transduction, (2001)

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See detailCrystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase
Mandelman, D.; Bentahir, M.; Feller, Georges ULg et al

in Acta Crystallographica Section D-Biological Crystallography (2001), 57(Pt 11), 1666-8

The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and ... [more ▼]

The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and decreased thermostability relative to its mesophilic counterpart. Herein, the preliminary crystallization and structure solution of psychrophilic PGK in its native form and cocrystallized with 3-phosphoglyceric acid (3-PGA) and the ATP analogue adenylyl imidophosphate (AMP-PNP) is reported. The complexed form of PGK crystallized in 2-3 d at 290 K, whereas the native form of the enzyme required 8-12 months. Morphologically, both crystal forms are similar and X-ray diffraction experiments indicate that the crystals are isomorphous. The crystals diffracted to a resolution of 2.0 A and belong to the space group P3(2). with unit-cell parameters a = b = 58.5, c = 85.4 A. [less ▲]

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See detailCold-adapted enzymes
Georlette, D.; Bentahir, M.; Claverie, P. et al

in Bulte, J.; DeCuyper, M. (Eds.) Focus on Biotechnology – Physics and Chemistry Basis for Biotechnology (2001)

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See detailPsychrophilic Enzymes: Revisiting the Thermodynamic Parameters of Activation May Explain Local Flexibility
Lonhienne, T.; Gerday, Charles ULg; Feller, Georges ULg

in Biochimica et Biophysica Acta (2000), 1543(1), 1-10

Basic theoretical and practical aspects of activation parameters are briefly reviewed in the context of cold-adaptation. In order to reduce the error impact inherent to the transition state theory on the ... [more ▼]

Basic theoretical and practical aspects of activation parameters are briefly reviewed in the context of cold-adaptation. In order to reduce the error impact inherent to the transition state theory on the absolute values of the free energy (DeltaG(#)), enthalpy (DeltaH(#)) and entropy (DeltaS(#)) of activation, it is proposed to compare the variation of these parameters between psychrophilic and mesophilic enzymes, namely Delta(DeltaG(#))(p-m), Delta(DeltaH(#))(p-m) and Delta(DeltaS(#))(p-m). Calculation of these parameters from the available literature shows that the main adaptation of psychrophilic enzymes lies in a significant decrease of DeltaH(#), therefore leading to a higher k(cat), especially at low temperatures. Moreover, in all cases including cold-blooded animals, DeltaS(#) exerts an opposite and negative effect on the gain in k(cat). It is argued that the magnitude of this counter-effect of DeltaS(#) can be reduced by keeping some stable domains, while increasing the flexibility of the structures required to improve catalysis at low temperature, as demonstrated in several cold-active enzymes. This enthalpic-entropic balance provides a new approach explaining the two types of conformational stability detected by recent microcalorimetric experiments on psychrophilic enzymes. [less ▲]

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See detailStructural Similarities and Evolutionary Relationships in Chloride-Dependent Alpha-Amylases
D'Amico, Salvino ULg; Gerday, Charles ULg; Feller, Georges ULg

in Gene (2000), 253(1), 95-105

The alpha-amylase sequences contained in databanks were screened for the presence of amino acid residues Arg195, Asn298 and Arg/Lys337 forming the chloride-binding site of several specialized alpha ... [more ▼]

The alpha-amylase sequences contained in databanks were screened for the presence of amino acid residues Arg195, Asn298 and Arg/Lys337 forming the chloride-binding site of several specialized alpha-amylases allosterically activated by this anion. This search provides 38 alpha-amylases potentially binding a chloride ion. All belong to animals, including mammals, birds, insects, acari, nematodes, molluscs, crustaceans and are also found in three extremophilic Gram-negative bacteria. An evolutionary distance tree based on complete amino acid sequences was constructed, revealing four distinct clusters of species. On the basis of multiple sequence alignment and homology modeling, invariable structural elements were defined, corresponding to the active site, the substrate binding site, the accessory binding sites, the Ca(2+) and Cl(-) binding sites, a protease-like catalytic triad and disulfide bonds. The sequence variations within functional elements allowed engineering strategies to be proposed, aimed at identifying and modifying the specificity, activity and stability of chloride-dependent alpha-amylases. [less ▲]

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See detailStructural, Kinetic, and Calorimetric Characterization of the Cold-Active Phosphoglycerate Kinase from the Antarctic Pseudomonas Sp. Tacii18
Bentahir, Mostafa; Feller, Georges ULg; Aittaleb, Mohamed et al

in Journal of Biological Chemistry (2000), 275(15), 11147-53

The gene encoding the phosphoglycerate kinase (PGK) from the Antarctic Pseudomonas sp. TACII18 has been cloned and found to be inserted between the genes encoding for glyceraldhyde-3-phosphate ... [more ▼]

The gene encoding the phosphoglycerate kinase (PGK) from the Antarctic Pseudomonas sp. TACII18 has been cloned and found to be inserted between the genes encoding for glyceraldhyde-3-phosphate dehydrogenase and fructose aldolase. The His-tagged and the native recombinant PGK from the psychrophilic Pseudomonas were expressed in Escherichia coli. The wild-type and the native recombinant enzymes displayed identical properties, such as a decreased thermostability and a 2-fold higher catalytic efficiency at 25 degrees C when compared with the mesophilic PGK from yeast. These properties, which reflect typical features of cold-adapted enzymes, were strongly altered in the His-tagged recombinant PGK. The structural model of the psychrophilic PGK indicated that a key determinant of its low stability is the reduced number of salt bridges, surface charges, and aromatic interactions when compared with mesophilic and thermophilic PGK. Differential scanning calorimetry of the psychrophilic PGK revealed unusual variations in its conformational stability for the free and substrate-bound forms. In the free form, a heat-labile and a thermostable domain unfold independently. It is proposed that the heat-labile domain acts as a destabilizing domain, providing the required flexibility around the active site for catalysis at low temperatures. [less ▲]

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See detailCold-Adapted Enzymes: From Fundamentals to Biotechnology
Gerday, Charles ULg; Aittaleb, Mohamed; Bentahir, Mostafa et al

in Trends in Biotechnology (2000), 18(3), 103-7

Psychrophilic enzymes produced by cold-adapted microorganisms display a high catalytic efficiency and are most often, if not always, associated with high thermosensitivity. Using X-ray crystallography ... [more ▼]

Psychrophilic enzymes produced by cold-adapted microorganisms display a high catalytic efficiency and are most often, if not always, associated with high thermosensitivity. Using X-ray crystallography, these properties are beginning to become understood, and the rules governing their adaptation to cold appear to be relatively diverse. The application of these enzymes offers considerable potential to the biotechnology industry, for example, in the detergent and food industries, for the production of fine chemicals and in bioremediation processes. [less ▲]

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