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.

Rate-limiting step and substrate accessibility of cellobiohydrolase Cel6A from Trichoderma reesei.

Abstract: The cellobiohydrolase (CBH) Cel6A is an important component of enzyme cocktails for industrial degradation of lignocellulosic biomass. However, the kinetics of this enzyme acting on its natural, insoluble substrate remains sparsely investigated. Here, we studied Cel6A from Trichoderma reesei with respect to adsorption, processivity, and kinetics both in the steady-state and pre-steady-state regimes, on microcrystalline and amorphous cellulose. We found that slow dissociation (koff ) was limiting the overall reaction rate, and we suggest that this leads to an accumulation of catalytically inactive complexes in front of obstacles and irregularities on the cellulose surface. The processivity number of Cel6A was low on both investigated substrates (5-10), and this suggested a rugged surface with short obstacle-free path lengths. The turnover of the inner catalytic cycle (the reactions of catalysis in one processive step) was too fast to be fully resolved, but a minimum value of about 20 s-1 could be established. This is among the highest values reported hitherto for a cellulase, and it underscores the catalytic efficiency of Cel6A. Conversely, we found that Cel6A had a poor ability to recognize attack sites on the cellulose surface. On amorphous cellulose, for example, Cel6A was only able to initiate hydrolysis on about 4% of the sites to which it could adsorb. This probably reflects high requirements of Cel6A to the architecture of the site. We conclude that compared to the other CBH, Cel7A, secreted by T. reesei, Cel6A is catalytically more efficient but less capable of attacking a broad range of structurally distinct sites on the cellulose surface. ENZYMES: TrCel6A, nonreducing end-acting cellobiohydrolase (EC3.2.1.91) from Trichoderma reesei; TrCel7A, reducing end-acting cellobiohydrolase (EC3.2.1.176) from T. reesei.

Particles comprising active compounds

Abstract: The present invention relates to a particle comprising an enzyme and a polymer wherein the enzyme and polymer are present as a mixture in the particle and the polymer is substantially soluble in an aqueous solution having an ionic strength of 0 mol/kg and insoluble in an aqueous solution having an ionic strength of more than 1 mol/kg according to method 1 of the invention. The invention aksi relates to a process for the preparation of the particles, to a composition comprising the particles and to the use of the composition for cleaning clothes.

Fungall cell wall degrading enzyme

Abstract: A novel fungal enzyme having lysozyme activity has been isolated. The invention further relates to a fungal polypeptide having lysozyme activity and belonging to the GH25 family, wherein the enzyme is selected from the group consisting of (a) a polypeptide comprising an amino acid sequence, which has at least 80% identity with amino acids 1 to 233 of SEQ ID NO:2; (b) a polypeptide comprising an amino acid sequence, which has at least 80% identity with the polypeptide encoded by the lysozyme encoding part of the nucleotide sequence inserted into a plasmid present in strain DSM 16084; (c) a polypeptide which is encoded by a nucleotide sequence which hybridizes under high stringency conditions with a polynucleotide probe consisting of the complementary strand of nucleotides 84 to 782 of SEQ ID NO:1; or (d) a fragment of (a), (b) or (c) that has lysozyme activity.

Exploring d -xylose oxidation in Saccharomyces cerevisiae through the Weimberg pathway

Abstract: Engineering of the yeast Saccharomyces cerevisiae towards efficient d-xylose assimilation has been a major focus over the last decades since d-xylose is the second most abundant sugar in nature, and its conversion into products could significantly improve process economy in biomass-based processes. Up to now, two different metabolic routes have been introduced via genetic engineering, consisting of either the isomerization or the oxido-reduction of d-xylose to d-xylulose that is further connected to the pentose phosphate pathway and glycolysis. In the present study, cytosolic d-xylose oxidation was investigated instead, through the introduction of the Weimberg pathway from Caulobacter crescentus in S. cerevisiae. This pathway consists of five reaction steps that connect d-xylose to the TCA cycle intermediate α-ketoglutarate. The corresponding genes could be expressed in S. cerevisiae, but no growth was observed on d-xylose indicating that not all the enzymes were functionally active. The accumulation of the Weimberg intermediate d-xylonate suggested that the dehydration step(s) might be limiting, blocking further conversion into α-ketoglutarate. Although four alternative dehydratases both of bacterial and archaeon origins were evaluated, d-xylonate accumulation still occurred. A better understanding of the mechanisms associated with the activity of dehydratases, both at a bacterial and yeast level, appears essential to obtain a fully functional Weimberg pathway in S. cerevisiae.

Bacillus amyloliquefaciens strain

Abstract: The present disclosure relates to a strain of Bacillus amyloliquefaciens bacteria that hyperproduces amylase enzyme and protease enzyme. The strain is also suitable for producing lipase for the degradation of oleaginous materials such as fats, greases and cooking oils. The strain also has excellent fungicidal and/or fungistatic qualities. The strain of the present disclosure and the enzymes produced thereby have a number of applications, including agricultural uses, laundry and dish detergents, drain cleaners and spot removers, and among other things, baking applications.