Novozymes

About: Novozymes is a company organization based out in Copenhagen, Denmark. It is known for research contribution in the topics: Nucleic acid & Polynucleotide. The organization has 2506 authors who have published 2828 publications receiving 89266 citations. The organization is also known as: Novo Enzymes A/S & Novozymes A/S.

Polypeptides having cellobiase activity and polynucleotides encoding same

Abstract: The present invention relates to polypeptides having cellobiase activity and polynucleotides having a nucleotide sequence which encodes for the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid constructs as well as methods for producing and using the polypeptides, such as for producing ethanol from biomass or for shuffling of DNA.

Lipolytic enzyme variants

Abstract: The substrate specificity of a lipolytic enzyme can be modified by making alterations to the amino acid sequence in a defined region of the lipolytic enzyme, so as to increase the level of a desired activity or to decrease the level of an undesired activity. Thus, the inventors have developed lipolytic enzyme variants with a modified amino acid sequence with a substrate specificity which can be tailored for specific uses.

Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas

Abstract: Carbonic anhydrase (CA) is one of nature’s fastest enzymes and can dramatically improve the economics of carbon capture under demanding environments such as coal-fired power plants. The use of CA to accelerate carbon capture is limited by the enzyme’s sensitivity to the harsh process conditions. Using directed evolution, the properties of a β-class CA from Desulfovibrio vulgaris were dramatically enhanced. Iterative rounds of library design, library generation, and high-throughput screening identified highly stable CA variants that tolerate temperatures of up to 107 °C in the presence of 4.2 M alkaline amine solvent at pH >10.0. This increase in thermostability and alkali tolerance translates to a 4,000,000-fold improvement over the natural enzyme. At pilot scale, the evolved catalyst enhanced the rate of CO2 absorption 25-fold compared with the noncatalyzed reaction.

The HvNAC6 transcription factor: a positive regulator of penetration resistance in barley and Arabidopsis

Abstract: Pathogens induce the expression of many genes encoding plant transcription factors, though specific knowledge of the biological function of individual transcription factors remains scarce. NAC transcription factors are encoded in plants by a gene family with proposed functions in both abiotic and biotic stress adaptation, as well as in developmental processes. In this paper, we provide convincing evidence that a barley NAC transcription factor has a direct role in regulating basal defence. The gene transcript was isolated by differential display from barley leaves infected with the biotrophic powdery mildew fungus, Blumeria graminis f.sp. hordei (Bgh). The full-length cDNA clone was obtained using 5′-RACE and termed HvNAC6, due to its high similarity to the rice homologue, OsNAC6. Gene silencing of HvNAC6 during Bgh inoculation compromises penetration resistance in barley epidermal cells towards virulent Bgh. Complementing the effect of HvNAC6 gene silencing, transient overexpression of HvNAC6 increases the occurrence of penetration resistant cells towards Bgh attack. Quantitative RT-PCR shows the early and transient induction of HvNAC6 in barley epidermis upon Bgh infection. Additionally, our results show that the Arabidopsis HvNAC6 homologue ATAF1 is also induced by Bgh and the ataf1-1 mutant line shows decreased penetration resistance to this non-host pathogen. Collectively, these data suggest a conserved role of HvNAC6 and ATAF1 in the regulation of penetration resistance in monocots and dicots, respectively.

A new kinetic model for heterogeneous (or spatially confined) enzymatic catalysis : Contributions from the fractal and jamming (overcrowding) effects

Abstract: Heterogeneous catalysis involves catalysts and reactants separated in different phases. In these systems, the interaction between the reactant and catalyst can be quite different from its homogeneous counterpart, because of the peculiarity of the diffusion and molecular collision processes constricted in spaces with dimension less than three. The fractal theory, developed for mathematic, physical, chemical, and biological processes with inherent irregularity and complexity, can be applied to heterogeneous catalysis. To better understand the heterogeneous enzymatic reactions, a fractal Michaelis kinetics was reformulated, after applying the general fractal formalism to the classical model of homogeneous enzymatic reactions. A kinetic “jamming” effect caused by the overcrowding of enzyme/substrate in confined space was also studied. The new kinetic model was applied to the hydrolysis of cellulose by cellobiohydrolase, a representative heterogeneous biocatalytic system highly fractal due to the strong surface adsorption of the enzyme onto the insoluble substrate as well as to the one-dimensional “processive” enzymatic mechanism. The usefulness of the model for the study and application of other enzymatic reactions was discussed.