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Institution

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: This comprehensive work highlights the superiority of medium MW hyaluronic acid for topical ophthalmic formulations based on their physico-chemical and biological properties, tolerance and handling.
Abstract: This work presents a comparative study of various hyaluronic acids (HA) produced by fermentation of either Bacillus subtilis or Streptococcus towards the selection of an optimal molecular weight (MW) HA for the preparation of topical ophthalmic formulations. The influence of HA MW on water binding capacity, sterile filtration, rheological properties, precorneal residence time and ocular tolerance of ophthalmic solutions was investigated. Molecular weight did not affect hydration of hyaluronic acid according to differential scanning calorimetry (DSC). In general, medium MW HA (0.6-1 MDa) resulted in solutions that were superior in terms of sterile filtration and kinematic viscosity requirements compared to high MW HA (>1 MDa). Moreover, all HA-based solutions exhibited well-defined viscoelastic properties that depend on MW. Gamma scintigraphic data indicated that HA MW at 0.1% concentration (w/v) and HA origin did not significantly affect the corneal residence time on rabbit eyes. A 0.3% solution of high MW HA had a prolonged residence time in the precorneal area compared to a medium MW HA at the same concentration. Finally, an in vivo ocular irritation test based on confocal laser scanning ophthalmoscopy (CLSO) conclusively showed the excellent tolerance of both Bacillus-derived HA and Streptococcus-derived HA after topical instillation onto the corneal surface. Overall, this comprehensive work highlights the superiority of medium MW hyaluronic acid for topical ophthalmic formulations based on their physico-chemical and biological properties, tolerance and handling. Such solutions are expected to enhance tear film stability, to allow for maximum comfort, and to exhibit high residence times, while being biocompatible and easy to sterile filter.

47 citations

Patent
07 Jul 1998
TL;DR: A xyloglucanase having a relative xylucanases activity of at least 50% at pH 7 and either no or an insignificant cellulolytic activity is obtainable e.g. from a strain of Bacillus.
Abstract: A xyloglucanase having a relative xyloglucanase activity of at least 50% at pH 7 and either no or an insignificant cellulolytic activity is obtainable e.g. from a strain of Bacillus. A xyloglucanase comprising an amino acid sequence as shown in positions 30-261 of SEQ ID NO:2 or homologues may be derived from eg Bacillus licheniformis , ATCC 14580, and may be encoded by polynucleotide molecules comprising a nucleotide sequence as shown in SEQ ID NO:1 from nucleotide 88 to nucleotide 783; and a xyloglucanase comprising an amino acid sequence as shown in positions 1-537 of SEQ ID NO:4 or homologues may be derived from eg B. agaradhaerens , NCIMB 40482, and may be encoded by polynucleotide molecules comprising a nucleotide sequence as shown in SEQ ID NO:3 from nucleotide 1 to nucleotide 1611. The xyloglucanases are useful e.g. in cleaning compositions and for treatment of cellulosic fibres.

47 citations

Journal ArticleDOI
TL;DR: This work proposes a method applying first order integral analysis to fed‐batch data based on either the bound glycerol or free fatty acid content in the oil which greatly simplifies the modeling process and gives an indication of the effect of mixing at the various scales.
Abstract: In this work, we demonstrate the scale-up from an 80 L fed-batch scale to 40 m(3) along with the design of a 4 m(3) continuous process for enzymatic biodiesel production catalyzed by NS-40116 (a liquid formulation of a modified Thermomyces lanuginosus lipase). Based on the analysis of actual pilot plant data for the transesterification of used cooking oil and brown grease, we propose a method applying first order integral analysis to fed-batch data based on either the bound glycerol or free fatty acid content in the oil. This method greatly simplifies the modeling process and gives an indication of the effect of mixing at the various scales (80 L to 40 m(3) ) along with the prediction of the residence time needed to reach a desired conversion in a CSTR. Suitable process metrics reflecting commercial performance such as the reaction time, enzyme efficiency, and reactor productivity were evaluated for both the fed-batch and CSTR cases. Given similar operating conditions, the CSTR operation on average, has a reaction time which is 1.3 times greater than the fed-batch operation. We also showed how the process metrics can be used to quickly estimate the selling price of the enzyme. Assuming a biodiesel selling price of 0.6 USD/kg and a one-time use of the enzyme (0.1% (w/woil ) enzyme dosage); the enzyme can then be sold for 30 USD/kg which ensures that that the enzyme cost is not more than 5% of the biodiesel revenue. Biotechnol. Bioeng. 2016;113: 1719-1728. © 2016 Wiley Periodicals, Inc.

47 citations

Journal ArticleDOI
TL;DR: In this article, mutations at subfamily-specific positions were used to introduce amidase activity into Candida antarctica lipase B (CALB) and molecular modeling was implemented to evaluate influence of selected residues on binding and catalytic conversion of amide substrate by corresponding library of mutants.
Abstract: Superfamily of alpha-beta hydrolases is one of the largest groups of structurally related enzymes with diverse catalytic functions. Bioinformatic analysis was used to study how lipase and amidase catalytic activities are implemented into the same structural framework. Subfamily-specific positions--conserved within lipases and peptidases but different between them--that were supposed to be responsible for functional discrimination have been identified. Mutations at subfamily-specific positions were used to introduce amidase activity into Candida antarctica lipase B (CALB). Molecular modeling was implemented to evaluate influence of selected residues on binding and catalytic conversion of amide substrate by corresponding library of mutants. In silico screening was applied to select reactive enzyme-substrate complexes that satisfy knowledge-based criteria of amidase catalytic activity. Selected CALB variants with substitutions at subfamily-specific positions Gly39, Thr103, Trp104, and Leu278 were produced and showed significant improvement of experimentally measured amidase activity. Based on these results, we suggest that value of subfamily-specific positions should be further explored in order to develop a systematic tool to study structure-function relationship in enzymes and to use this information for rational enzyme engineering.

47 citations

Patent
26 Feb 1999
TL;DR: In this paper, the structure similarities and differences between the structure of Novamyl and the reported structures of CGTases were discovered and based on this they have constructed variants of maltogenic alpha-amylase having CGTase activity.
Abstract: The inventors have discovered some striking, and not previously predicted structural similarities and differences between the structure of Novamyl and the reported structures of CGTases, and based on this they have constructed variants of maltogenic alpha-amylase having CGTase activity and variants of CGTase having maltogenic alpha-amylase activity. Further, on the basis of sequence homology between Novamyl® and CGTases, the inventors have constructed hybrid enzymes with one or more improvements to specific properties of the parent enzymes, using recombinant DNA methodology.

47 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