Institution
Novozymes
Company•Copenhagen, Denmark•
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.
Topics: Nucleic acid, Polynucleotide, Fermentation, Lipase, Cellulase
Papers published on a yearly basis
Papers
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27 Sep 1995TL;DR: In this paper, a method of oxidizing a compound with a phenol oxidizing enzyme (e.g., a peroxidase or a laccase) and an enhancing agent such as acetosyringone is described.
Abstract: The present invention relates to a method of oxidizing a compound with a phenol oxidizing enzyme (e.g. a peroxidase or a laccase) and an enhancing agent (e.g. acetosyringone). The invention also relates to a detergent additive and to a detergent composition.
55 citations
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TL;DR: In this article, the authors present a single-use PDE for batch and continuous cultivation of suspended cells which combines the small working volumes known from microwell plates with the versatility of bench-scale reactors.
55 citations
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TL;DR: The ratio of the inlet concentration to the maximum surface capacity is critical for reliable use of the quasi-steady theory, and the results provide users of surface-based biosensors with a tool for correcting experimentally obtained adsorption rate constants.
Abstract: This paper presents a theoretical and computational investigation of convection, diffusion, and adsorption in surface-based biosensors. In particular, we study the transport dynamics in a model geometry of a surface plasmon resonance (SPR) sensor. The work, however, is equally relevant for other microfluidic surface-based biosensors, operating under flow conditions. A widely adopted approximate quasi-steady theory to capture convective and diffusive mass transport is reviewed, and an analytical solution is presented. An expression of the Damko number is derived in terms of the nondimensional adsorption coefficient (Biot number), the nondimensional flow rate (Pe clet number), and the model geometry. Transient dynamics is investigated, and we quantify the error of using the quasi-steady-state assumption for experimental data fitting in both kinetically limited and convection-diffusion- limited regimes for irreversible adsorption, in specific. The results clarify the conditions under which the quasi-steady theory is reliable or not. In extension to the well-known fact that the range of validity is altered under convection-diffusion-limited conditions, we show how also the ratio of the inlet concentration to the maximum surface capacity is critical for reliable use of the quasi-steady theory. Finally, our results provide users of surface-based biosensors with a tool for correcting experimentally obtained adsorption rate constants.
55 citations
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TL;DR: Structural alterations observed in the N298S variant upon chloride ion binding suggest that the chloride ion plays a variety of roles that serve to promote catalysis, and attempts to engineer chloride‐dependence into the chloride‐independent TAKA‐amylase point out the complexity of this system.
Abstract: The mechanism of allosteric activation of α-amylase by chloride has been studied through structural and kinetic experiments focusing on the chloride-dependent N298S variant of human pancreatic α-amylase (HPA) and a chloride-independent TAKA-amylase. Kinetic analysis of the HPA variant clearly demonstrates the pronounced activating effect of chloride ion binding on reaction rates and its effect on the pH-dependence of catalysis. Structural alterations observed in the N298S variant upon chloride ion binding suggest that the chloride ion plays a variety of roles that serve to promote catalysis. One of these is having a strong influence on the positioning of the acid/base catalyst residue E233. Absence of chloride ion results in multiple conformations for this residue and unexpected enzymatic products. Chloride ion and N298 also appear to stabilize a helical region of polypeptide chain from which projects the flexible substrate binding loop unique to chloride-dependent α-amylases. This structural feature also serves to properly orient the catalytically essential residue D300. Comparative analyses show that the chloride-independent α-amylases compensate for the absence of bound chloride by substituting a hydrophobic core, altering the manner in which substrate interactions are made and shifting the placement of N298. These evolutionary differences presumably arise in response to alternative operating environments or the advantage gained in a particular product profile. Attempts to engineer chloride-dependence into the chloride-independent TAKA-amylase point out the complexity of this system, and the fact that a multitude of factors play a role in binding chloride ion in the chloride-dependent α-amylases.
55 citations
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23 Jan 1996TL;DR: In this article, a method involving introducing a DNA construct comprising the DNA sequence of interest into the genome of the recipient cell by transposition and subsequent deletion of a marker gene used for selection of cells having received the DNA construct was proposed.
Abstract: Multicopy strains of gram-positive bacteria carrying multiple copies of a DNA sequence of interest may be constructed by use of a method involving introduction of a DNA construct comprising the DNA sequence of interest into the genome of the recipient cell by transposition and subsequent deletion of a marker gene used for selection of cells having received the DNA construct by a resolution system. The multicopy strains are preferably free from a gene encoding an undesirable marker such as an antibiotic resistance marker.
55 citations
Authors
Showing all 2507 results
Name | H-index | Papers | Citations |
---|---|---|---|
Jens Nielsen | 149 | 1752 | 104005 |
Gary K. Schoolnik | 81 | 233 | 27782 |
Lubbert Dijkhuizen | 75 | 424 | 21761 |
Bauke W. Dijkstra | 72 | 256 | 19487 |
Michel Vert | 69 | 333 | 17899 |
Henning Langberg | 60 | 242 | 11999 |
Harinderjit Gill | 59 | 319 | 12978 |
John M. Woodley | 58 | 420 | 13426 |
Lei Cai | 57 | 374 | 16689 |
Anette Müllertz | 57 | 274 | 10319 |
Peter J. Punt | 52 | 154 | 8846 |
Svein Jarle Horn | 51 | 123 | 9511 |
Martin Hofrichter | 50 | 158 | 7387 |
Eva Stoger | 49 | 127 | 8367 |
Luciano Saso | 45 | 325 | 7672 |