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.

A cellulase preparation comprising an endoglucanase enzyme

Abstract: A cellulase preparation consisting essentially of a homogeneous endoglucanase component which is immunoreactive with an antibody raised against a highly purified ∩43kD endoglucanase derived from Humicola insolens, DSM 1800, or which is homogeneous to said ∩43kD endoglucanase, may be employed in the treatment cellulose-containing fabrics for harshness reduction or colour clarification or to provide a localized variation in the colour of such fabrics, or it may be employed in the treatment of paper pulp.

Plectasin, a Fungal Defensin, Targets the Bacterial Cell Wall Precursor Lipid II

Abstract: Host defense peptides such as defensins are components of innate immunity and have retained antibiotic activity throughout evolution. Their activity is thought to be due to amphipathic structures, which enable binding and disruption of microbial cytoplasmic membranes. Contrary to this, we show that plectasin, a fungal defensin, acts by directly binding the bacterial cell-wall precursor Lipid II. A wide range of genetic and biochemical approaches identify cell-wall biosynthesis as the pathway targeted by plectasin. In vitro assays for cell-wall synthesis identified Lipid II as the specific cellular target. Consistently, binding studies confirmed the formation of an equimolar stoichiometric complex between Lipid II and plectasin. Furthermore, key residues in plectasin involved in complex formation were identified using nuclear magnetic resonance spectroscopy and computational modeling.

Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose).

Abstract: Intrinsically disordered proteins can phase separate from the soluble intracellular space, and tend to aggregate under pathological conditions. The physiological functions and molecular triggers of liquid demixing by phase separation are not well understood. Here we show in vitro and in vivo that the nucleic acid-mimicking biopolymer poly(ADP-ribose) (PAR) nucleates intracellular liquid demixing. PAR levels are markedly induced at sites of DNA damage, and we provide evidence that PAR-seeded liquid demixing results in rapid, yet transient and fully reversible assembly of various intrinsically disordered proteins at DNA break sites. Demixing, which relies on electrostatic interactions between positively charged RGG repeats and negatively charged PAR, is amplified by aggregation-prone prion-like domains, and orchestrates the earliest cellular responses to DNA breakage. We propose that PAR-seeded liquid demixing is a general mechanism to dynamically reorganize the soluble nuclear space with implications for pathological protein aggregation caused by derailed phase separation.

Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species

Abstract: Bacillus licheniformis is a Gram-positive, spore-forming soil bacterium that is used in the biotechnology industry to manufacture enzymes, antibiotics, biochemicals and consumer products. This species is closely related to the well studied model organism Bacillus subtilis, and produces an assortment of extracellular enzymes that may contribute to nutrient cycling in nature. We determined the complete nucleotide sequence of the B. licheniformis ATCC 14580 genome which comprises a circular chromosome of 4,222,336 base-pairs (bp) containing 4,208 predicted protein-coding genes with an average size of 873 bp, seven rRNA operons, and 72 tRNA genes. The B. licheniformis chromosome contains large regions that are colinear with the genomes of B. subtilis and Bacillus halodurans, and approximately 80% of the predicted B. licheniformis coding sequences have B. subtilis orthologs. Despite the unmistakable organizational similarities between the B. licheniformis and B. subtilis genomes, there are notable differences in the numbers and locations of prophages, transposable elements and a number of extracellular enzymes and secondary metabolic pathway operons that distinguish these species. Differences include a region of more than 80 kilobases (kb) that comprises a cluster of polyketide synthase genes and a second operon of 38 kb encoding plipastatin synthase enzymes that are absent in the B. licheniformis genome. The availability of a completed genome sequence for B. licheniformis should facilitate the design and construction of improved industrial strains and allow for comparative genomics and evolutionary studies within this group of Bacillaceae.

Non-toxic, non-toxigenic, non-pathogenic Fusarium expression system and promoters and terminators for use therein

Abstract: The invention is related to a non-toxic, non-toxigenic, non-pathogenic recombinant Fusarium, e.g., Fusarium graminearum host cell comprising a nucleic acid sequence encoding a heterologous protein operably linked to a promoter. The invention further relates to a method for the production of recombinant proteins using such Fusarium host cells. The invention also relates to a promoter and terminator sequence which may be used in such cells.