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.

Preserving accuracy in GenBank

Abstract: GenBank, the public repository for nucleotide and protein sequences, is a critical resource for molecular biology, evolutionary biology, and ecology. While some attention has been drawn to sequence errors ([1][1]), common annotation errors also reduce the value of this database. In fact, for

Kakadumycins, novel antibiotics from Streptomyces sp NRRL 30566, an endophyte of Grevillea pteridifolia.

Abstract: An endophytic streptomycete (NRRL 30566) is described and partially characterized from a fern-leaved grevillea (Grevillea pteridifolia) tree growing in the Northern Territory of Australia. This endophytic streptomycete produces, in culture, novel antibiotics – the kakadumycins. Methods are outlined for the production and chemical characterization of kakadumycin A and related compounds. This antibiotic is structurally related to a quinoxaline antibiotic, echinomycin. Each contains, by virtue of their amino acid compositions, alanine, serine and an unknown amino acid. Other biological, spectral and chromatographic differences between these two compounds occur and are given. Kakadumycin A has wide spectrum antibiotic activity, especially against Gram-positive bacteria, and it generally displays better bioactivity than echinomycin. For instance, against Bacillus anthracis strains, kakadumycin A has minimum inhibitory concentrations of 0.2–0.3 μg ml−1 in contrast to echinomycin at 1.0–1.2 μg ml−1. Both echinomycin and kakadumycin A have impressive activity against the malarial parasite Plasmodium falciparum with LD50s in the range of 7–10 ng ml−1. In macromolecular synthesis assays both kakadumycin A and echinomycin have similar effects on the inhibition of RNA synthesis. It appears that the endophytic Streptomyces sp. offer some promise for the discovery of novel antibiotics with pharmacological potential.

Evaluating the Potential for Enzymatic Acrylamide Mitigation in a Range of Food Products Using an Asparaginase from Aspergillus oryzae

Abstract: Asparaginase, an enzyme that hydrolyzes asparagine to aspartic acid, presents a potentially very effective means for reducing acrylamide formation in foods via removal of the precursor, asparagine, from the primary ingredients. An extracellular asparaginase amenable to industrial production was cloned and expressed in Aspergillus oryzae. This asparaginase was tested in a range of food products, including semisweet biscuits, ginger biscuits, crisp bread, French fries, and sliced potato chips. In dough-based applications, addition of asparaginase resulted in reduction of acrylamide content in the final products of 34−92%. Enzyme dose, dough resting time, and water content were identified as critical parameters. Treating French fries and sliced potato chips was more challenging as the solid nature of these whole-cut products limits enzyme−substrate contact. However, by treating potato pieces with asparaginase after blanching, the acrylamide levels in French fries could be lowered by 60−85% and that in potato...