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Novozymes

CompanyCopenhagen, 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.


Papers
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Journal ArticleDOI
TL;DR: The purification of TAase from human placentral microsomes to homogeneity, exhibiting varying degrees of specificity to several classes of PA confirming the structure-activity relationship for the microsome-bound TAase, is reported, and it is envisaged that CRTAase plays an important role in protein modification by way of acetylation independent of Acetyl CoA.
Abstract: We have earlier shown that a unique membrane-bound enzyme mediates the transfer of acetyl group(s) from polyphenolic peracetates (PA) to functional proteins, which was termed acetoxy drug: protein transacetylase (TAase) because it acted upon several classes of PA. Here, we report the purification of TAase from human placentral microsomes to homogeneity with molecular mass of 60 kDa, exhibiting varying degrees of specificity to several classes of PA confirming the structure-activity relationship for the microsome-bound TAase. The TAase catalyzed protein acetylation by a model acetoxy drug, 7,8-diacetoxy-4-methyl coumarin (DAMC) was established by the demonstration of immunoreactivity of the acetylated target protein with anti-acetyl lysine antibody. TAase activity was severely inhibited in calcium-aggregated microsomes as well as when Ca2+ was added to purified TAase, suggesting that TAase could be a calcium binding protein. Furthermore, the N-terminal sequence analysis of purified TAase (EPAVYFKEQFLD) using Swiss Prot Database perfectly matched with calreticulin (CRT), a major microsomal calcium binding protein of the endoplasmic reticulum (ER). The identity of TAase with CRT was substantiated by the observation that the purified TAase avidly reacted with commercially available antibody raised against the C-terminus of human CRT (13 residues peptide, DEEDATGQAKDEL). Purified TAase also showed Ca2+ binding and acted as a substrate for phosphorylation catalyzed by protein kinase C (PKC), which are hallmark characteristics of CRT. Further, purified placental CRT as well as the commercially procured pure CRT yielded significant TAase catalytic activity and were also found effective in mediating the acetylation of the target protein NADPH cytochrome P-450 reductase by DAMC as detected by Western blot using anti-acetyl lysine antibody. These observations for the first time convincingly attribute the transacetylase function to CRT. Hence, this transacetylase function of CRT is designated calreticulin transacetylase (CRTAase). We envisage that CRTAase plays an important role in protein modification by way of acetylation independent of Acetyl CoA.

31 citations

Patent
06 Jul 2012
TL;DR: The present invention relates to variants of alpha amylase as mentioned in this paper, and also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polyn nucleotides; and methods of using the variants.
Abstract: The present invention relates to variants of alpha amylase The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants

31 citations

Journal ArticleDOI
TL;DR: In this article, a dual up-pumping combination of the Hayward Tyler B2 (former APV-B2 or simply B2), a high solidity ratio hydrofoil impeller, was retrofitted to a pilot scale fermentor based on cited reference studies of the impeller performance.

31 citations

Journal ArticleDOI
TL;DR: Analysis of a range of kinetic parameters consistently indicated that the B2 loop, covering the substrate-binding subsites −3 and −4 in TrC Cel7A, was a key determinant for the difference in CBH- or EG-like behavior between TrCel7A and TrCEL7B.

31 citations

Journal ArticleDOI
05 Jan 2018-PLOS ONE
TL;DR: The compositions of essential oils from Spanish marjoram grown in several bioclimatic zones of Murcia were studied to determine their absolute and relative concentrations using gas chromatography-mass spectrometry and the results underline the potential use of these EOs in manufactured products, such as foodstuff, cosmetics and pharmaceuticals.
Abstract: The compositions of essential oils (EOs) from Spanish marjoram (Thymus mastichina L.) grown in several bioclimatic zones of Murcia (SE Spain) were studied to determine their absolute and relative concentrations using gas chromatography-mass spectrometry. 1,8-Cineole and linalool were the main components, followed by α-pinene, β-pinene and α-terpineol. (-)-Linalool, (+)-α-terpineol and (+)-α-pinene were the most abundant enantiomers. When the antioxidant capacities of T. mastichina EOs and their compounds were measured by five methods, EOs and linalool, linalyl acetate, α-terpinene and γ-terpinene, among others, showed antioxidant activities. All four T. mastichina EOs inhibited both lipoxygenase and acetylcholinesterase activities, and they might be useful for further research into inflammatory and Alzheimer diseases. Bornyl acetate and limonene showed the highest lipoxygenase inhibition and 1,8-cineole was the best acetylcholinesterase inhibitor. Moreover, these EOs inhibited the growth of Escherichia coli, Staphylococcus aureus and Candida albicans due to the contribution of their individual compounds. The results underline the potential use of these EOs in manufactured products, such as foodstuff, cosmetics and pharmaceuticals.

31 citations


Authors

Showing all 2507 results

NameH-indexPapersCitations
Jens Nielsen1491752104005
Gary K. Schoolnik8123327782
Lubbert Dijkhuizen7542421761
Bauke W. Dijkstra7225619487
Michel Vert6933317899
Henning Langberg6024211999
Harinderjit Gill5931912978
John M. Woodley5842013426
Lei Cai5737416689
Anette Müllertz5727410319
Peter J. Punt521548846
Svein Jarle Horn511239511
Martin Hofrichter501587387
Eva Stoger491278367
Luciano Saso453257672
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20229
202181
202070
201998
2018102
2017135