Abstract: The present invention relates to glucoamylase variants. 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.
Abstract: The present invention relates to cellobiohydrolase variants. 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.
Type:
Grant
Filed:
November 1, 2018
Date of Patent:
March 10, 2020
Assignee:
Novozymes A/S
Inventors:
Kim Borch, Kenneth Jensen, Kristian Krogh, Brett McBrayer, Peter Westh, Jeppe Kari, Johan Olsen, Trine Sorensen, Michael Windhal, Hui Xu
Abstract: Embodiments of the present invention relate to methods for the biosynthesis of di- or trifunctional C7 alkanes in the presence of isolated enzymes or in the presence of a recombinant host cell expressing those enzymes. The di- or trifunctional C7 alkanes are useful as intermediates in the production of nylon-7, nylon-7,x, nylon-x,7, and polyesters.
Type:
Grant
Filed:
March 20, 2017
Date of Patent:
March 3, 2020
Assignee:
INVISTA NORTH AMERICA S.A.R.L.
Inventors:
Paul S. Pearlman, Changlin Chen, Adriana L. Botes, Alex Van Eck Conradie, Benjamin D. Herzog
Abstract: The present invention relates to isolated polypeptides having xylanase activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.
Abstract: A method for producing an L-amino acid is provided. An L-amino acid is produced by culturing a bacterium belonging to the family Enterobacteriaceae and having an L-amino acid-producing ability, wherein the bacterium has been modified so that the activity of aconitase is increased, or the activities of aconitase and acetaldehyde dehydrogenase are increased, in a medium, and collecting the L-amino acid from the medium or cells of the bacterium.
Abstract: Provided is a novel xylanase having high xylanase activity. A protein consisting of an amino acid sequence described in the following (a), (b) or (c) and having xylanase activity: (a) the amino acid sequence set forth in positions 23 to 404 of SEQ ID NO: 2; (b) an amino acid sequence having at least 90% identity to the amino acid sequence set forth in positions 23 to 404 of SEQ ID NO: 2; (c) an amino acid sequence modified from the amino acid sequence set forth in positions 23 to 404 of SEQ ID NO: 2 by deletion, insertion, substitution, or addition of one or more amino acids.
Abstract: A system and method for creating crystals from human acetylcholinesterase. The crystals can then be analyzed using X-ray crystallography. A segment of DNA for human acetylcholinesterase is isolated that includes the codon sequence GAGGGC. A polyhistidine tag is inserted between codon GAG and codon GGC to produce a recombinant acetylcholinesterase construct. The recombinant acetylcholinesterase construct is used to transfect cells on a prepared growth medium. The growing cells secrete a portion of the recombinant acetylcholinesterase construct. The secreted portion is concentrated and the tag cleaved. The concentrate is then buffered and used to form crystals.
Abstract: Provided is ?3 desaturase having high enzymatic activity even at normal temperature. A polypeptide which consists of an amino acid sequence having an identity of 80% or more with the amino acid sequence represented by SEQ ID NO: 2 and has ?3 desaturation activity on C20 fatty acid, and a gene thereof.
Abstract: The present application discloses a PEGylated asparaginase and use thereof. In this application, the polyethylene glycol (PEG) is coupled to the N-terminal amino of 1 or 2 subunits of L-asparaginase, and the molecular weight of the PEG is 30-40 KDa. The PEG is preferably branched and has an aldehyde group serving as an activating group. The PEGylated asparaginase is useful in the preparation of anti-tumor drugs.
Type:
Grant
Filed:
February 3, 2015
Date of Patent:
January 21, 2020
Assignees:
ZONHON BIOPHARMA INSTITUTE INC., GENSUN INSTITUTE OF BIOMEDICINE CO., LTD.
Inventors:
Bruce Yong Ma, Jun Wang, He Wang, Chunlin Xu, Yifei Chen, Yaofang Wang
Abstract: A novel technique for improving secretory production of a heterologous protein by coryneform bacteria is described, as well as a method for secretory production of a heterologous protein. A coryneform bacterium is described that has been modified to have a specific mutation so as to harbor a phoS gene, and when cultured, is able to to produce a heterologous protein by secretory production.
Abstract: The present disclosure provides the sequence of a Paenibacillus polymyxa preproenzyme which is the precursor of a neutral protease, expression thereof in a transformed host organism, and methods for production of the neutral protease, by recombinant means. Further, use of the recombinantly produced neutral protease is disclosed in the field of cell biology, particularly for the purpose of tissue dissociation. The disclosure also includes blends with other proteases. Further disclosed are nucleotide sequences encoding the neutral protease.
Type:
Grant
Filed:
October 26, 2016
Date of Patent:
January 7, 2020
Assignee:
Roche Diagnostics Operations, Inc.
Inventors:
Thomas Greiner-Stoeffele, Stefan Schoenert
Abstract: The present disclosure relates to a novel pyruvate dehydrogenase variant, a polynucleotide encoding the pyruvate dehydrogenase variant, a microorganism of the genus Corynebacterium producing L-amino acid, which includes the pyruvate dehydrogenase variant, and a method for producing an L-amino acid using the microorganism.
Type:
Grant
Filed:
March 15, 2016
Date of Patent:
January 7, 2020
Assignee:
CJ CHEILJEDANG CORPORATION
Inventors:
Lan Huh, Jun Ok Moon, Hyun Won Bae, Hyung Joon Kim, Sung Ki Song
Abstract: The present invention relates to alpha-amylase variants having an improved stability as compared to the parent alpha-amylase. The invention further relates to use of the variants, compositions comprising the variants, and methods of producing the variants.
Abstract: This invention relates generally to the discovery of novel recombinant forms of ?-hexosyl-transferases (BHT) and uses thereof to produce galacto-oligosaccharides (GOS) or as food additives.
Type:
Grant
Filed:
September 12, 2017
Date of Patent:
December 24, 2019
Assignee:
North Carolina State University
Inventors:
Jose M. Bruno-Barcena, Suzanne Dagher, Maria Azcarate-Peril
Abstract: A method of producing a lipid, containing the steps of culturing a transformant obtained by introducing a gene encoding the following protein (a) or (b) into cyanobacteria, and producing a lipid: (a) a protein consisting of the amino acid sequence set forth in SEQ ID NO: 1; and (b) a protein consisting of an amino acid sequence having 60% or more identity with the amino acid sequence of the protein (a), and having ?-ketoacyl-ACP synthase activity.
Abstract: ?-Glu-Val synthetase suitable for generating ?-Glu-Val, and a method for producing ?-Glu-Val-Gly using the same are provided. By using ?-Glu-Val synthetase showing a ratio of ?-glutamylvaline synthetase activity to ?-glutamylglycine synthetase activity of 2.0 or higher, such as ?-Glu-Val synthetase of Kocuria rosea (AJ3132), ?-Glu-Val-Gly is produced from Glu, Val, and Gly as raw materials.
Abstract: The present invention relates to a recombinant microbial host for the production of xylitol, the recombinant microbial host containing a nucleic acid sequence encoding an NAD+-specific D-arabitol 4-oxidoreductase (EC 1.1.1.11) using D-arabitol as substrate and producing D-xylulose as product, and a nucleic acid sequence encoding an NADPH-specific xylitol dehydrogenase using D-xylulose as substrate and producing xylitol as product.
Type:
Grant
Filed:
June 17, 2015
Date of Patent:
December 3, 2019
Assignee:
ROQUETTE FRERES
Inventors:
Astrid Schaefer, Melanie Diefenbacher, Yiming Chang, Sumire Honda Malca, Markus Schwab, Sophie Defretin, Tania Gerard, Arnaud Heysen, Friederike Thor
Abstract: The invention relates to novel 3-hydroxysteroid dehydrogenase mutants, to the sequences which code for these enzyme mutants, to processes for the preparation of the enzyme mutants and to their use in enzymatic conversions of cholic acid compounds, in particular in the preparation of ursodeoxycholic acid (UDCA); subject-matter of the invention is also novel processes for the synthesis of UDCA using enzyme mutants; and the preparation of UDCA using recombinant, multiply modified microorganisms.
Abstract: A lyase has an amino acid sequence selected from SEQ ID NOs: 1, 2 and 3, wherein the amino acid isoleucine in position no. 468 in the protein ApPDC-E469G, which is modified with respect to the wild type from Acetobacter pasteurianus, is replaced by an amino acid which occupies less space than isoleucine.
Type:
Grant
Filed:
August 27, 2015
Date of Patent:
November 5, 2019
Assignee:
FORSCHUNGSZENTRUM JUELICH GMBH
Inventors:
Doerte Rother, Martina Pohl, Torsten Sehl, Lisa Marx, Robert Westphal
Abstract: The present disclosure provides a variant tyrosine hydroxylase that provides for increased production of L-DOPA in a host cell that expresses the tyrosine hydroxylase. The present disclosure provides nucleic acids encoding the variant tyrosine hydroxylase, and host cells genetically modified with the nucleic acids. The present disclosure provides methods of making L-DOPA in a host cell. The present disclosure provides methods of making a benzylisoquinoline alkaloid (BIA), or a BIA precursor. The present disclosure provides methods of detecting L-DOPA level in a cell. The present disclosure provides methods of identifying tyrosine hydroxylase variants that provide for increased L-DOPA production; and methods of identifying gene products that provide for increased tyrosine production.
Type:
Grant
Filed:
September 24, 2015
Date of Patent:
October 29, 2019
Assignees:
THE REGENTS OF THE UNIVERSITY OF CALIFORNIA, VALORBEC S.E.C.
Inventors:
Vincent J. J. Martin, Lauren Narcross, John E. Dueber, William C. DeLoache, Zachary N. Russ, P. James Scrivens