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.

Methods and compositions for bleaching a dye in solution

Abstract: The present invention provides methods and compositions for bleaching a dye in solution comprising contacting, in an aqueous solution, the dye with a composition comprising a laccase and an enhancing agent of the formula: in which A is: and B is H, or C1-C4 unbranched alkyl wherein said alkyl may contain ether groups, and one, two, three, four of R2, R3, R4, R5 and R6 are H, NH2, COOH, SO3H, CN, CH3, COCH3, NO2, OCH3, NR7R8, COOR9, or NOH—CO—R10, wherein R7, R8, R9 and R10 are C1-C2 unbranched alkyl, and one, two, three, four or five of R2, R3, R4, R5 and R6 is NH2, COOH, SO3H, CN, CH3, COCH3, NO2, OCH3, NR7R8, COOR9, or NOH—CO—R10, wherein R7, R8, R9 and R10 are C1-C2 unbranched alkyl

Mechanism of Protein Kinetic Stabilization by Engineered Disulfide Crosslinks

Abstract: The impact of disulfide bonds on protein stability goes beyond simple equilibrium thermodynamics effects associated with the conformational entropy of the unfolded state. Indeed, disulfide crosslinks may play a role in the prevention of dysfunctional association and strongly affect the rates of irreversible enzyme inactivation, highly relevant in biotechnological applications. While these kinetic-stability effects remain poorly understood, by analogy with proposed mechanisms for processes of protein aggregation and fibrillogenesis, we propose that they may be determined by the properties of sparsely-populated, partially-unfolded intermediates. Here we report the successful design, on the basis of high temperature molecular-dynamics simulations, of six thermodynamically and kinetically stabilized variants of phytase from Citrobacter braakii (a biotechnologically important enzyme) with one, two or three engineered disulfides. Activity measurements and 3D crystal structure determination demonstrate that the engineered crosslinks do not cause dramatic alterations in the native structure. The inactivation kinetics for all the variants displays a strongly non-Arrhenius temperature dependence, with the time-scale for the irreversible denaturation process reaching a minimum at a given temperature within the range of the denaturation transition. We show this striking feature to be a signature of a key role played by a partially unfolded, intermediate state/ensemble. Energetic and mutational analyses confirm that the intermediate is highly unfolded (akin to a proposed critical intermediate in the misfolding of the prion protein), a result that explains the observed kinetic stabilization. Our results provide a rationale for the kinetic-stability consequences of disulfide-crosslink engineering and an experimental methodology to arrive at energetic/structural descriptions of the sparsely populated and elusive intermediates that play key roles in irreversible protein denaturation.

The antimicrobial lysine-peptoid hybrid LP5 inhibits DNA replication and induces the SOS response in Staphylococcus aureus

Abstract: Background: The increase in antibiotic resistant bacteria has led to renewed interest in development of alternative antimicrobial compounds such as antimicrobial peptides (AMPs), either naturally-occurring or synthetically-derived. Knowledge of the mode of action (MOA) of synthetic compounds mimicking the function of AMPs is highly valuable both when developing new types of antimicrobials and when predicting resistance development. Despite many functional studies of AMPs, only a few of the synthetic peptides have been studied in detail. Results: We investigated the MOA of the lysine-peptoid hybrid, LP5, which previously has been shown to display antimicrobial activity against Staphylococcus aureus. At concentrations of LP5 above the minimal inhibitory concentration (MIC), the peptoid caused ATP leakage from bacterial cells. However, at concentrations close to the MIC, LP5 inhibited the growth of S. aureus without ATP leakage. Instead, LP5 bound DNA and inhibited macromolecular synthesis. The binding to DNA also led to inhibition of DNA gyrase and topoisomerase IV and caused induction of the SOS response. Conclusions: Our data demonstrate that LP5 may have a dual mode of action against S. aureus. At MIC concentrations, LP5 binds DNA and inhibits macromolecular synthesis and growth, whereas at concentrations above the MIC, LP5 targets the bacterial membrane leading to disruption of the membrane. These results add new information about the MOA of a new synthetic AMP and aid in the future design of synthetic peptides with increased therapeutic potential.

Methods of Increasing the Cellulolytic Enhancing Activity of a Polypeptide

Abstract: The present invention relates to methods of increasing the activity of a GH61 polypeptide having cellulolytic enhancing activity, comprising: adding a divalent copper cation to a composition comprising the GH61 polypeptide having cellulolytic enhancing activity, wherein the presence of the divalent copper cation and the GH61 polypeptide having cellulolytic enhancing activity increases degradation or conversion of a cellulosic material by an enzyme composition compared to the GH61 polypeptide having cellulolytic enhancing activity without the divalent copper cation. The present invention also relates to compositions, methods for degrading or converting a cellulosic material, and methods for producing a fermentation product.