Patent classifications
C12N9/2488
PICHIA PASTORIS STRAINS FOR PRODUCING PREDOMINANTLY HOMOGENEOUS GLYCAN STRUCTURE
Disclosed herein are novel Pichia pastoris strains for expression of exogenous proteins with substantially homogeneous N-glycans. The strains are genetically engineered to include a mutant OCH1 allele which is transcribed into an mRNA coding for a mutant OCH1 gene product (i.e., -1,6-mannosyltransferase, or OCH1 protein). The mutant OCH1protein contains a catalytic domain substantially identical to that of the wild type OCH1 protein, but lacks an N-terminal sequence necessary to target the OCH1 protein to the Golgi apparatus. The strains disclosed herein are robust, stable, and transformable, and the mutant OCH1 allele and the ability to produce substantially homogeneous N-glycans are maintained for generations after rounds of freezing and thawing and after subsequent transformations.
ENZYMES FOR REDUCED IMMUNOLOGICAL STRESS
Compositions suitable for oral administration to an animal comprising at least one immune stress-reducing enzyme in an amount effective to decrease the level of positive acute phase protein in an animal, increase the level of negative acute phase protein in an animal, and/or improve animal growth performance is provided, as are methods using such compositions. The compositions include animal feed compositions, liquid compositions other than animal feed, and solid compositions other than animal feed.
PAENIBACILLUS AND BACILLUS SPP. MANNANASES
The present disclosure relates to endo-beta-mannanases from Paenibacillus and Bacillus spp., polynucleotides encoding such endo-beta-mannanases, compositions containing such mannanases, and methods of use thereof. Compositions containing such endo-beta-mannanases are suitable for use as detergents and cleaning fabrics and hard surfaces, as well as a variety of other industrial applications.
Pichia pastoris strains for producing predominantly homogeneous glycan structure
Disclosed herein are novel Pichia pastoris strains for expression of exogenous proteins with substantially homogeneous N-glycans. The strains are genetically engineered to include a mutant OCH1 allele which is transcribed into an mRNA coding for a mutant OCH1 gene product (i.e., -1,6-mannosyltransferase, or OCH1 protein). The mutant OCH1 protein contains a catalytic domain substantially identical to that of the wild type OCH1 protein, but lacks an N-terminal sequence necessary to target the OCH1 protein to the Golgi apparatus. The strains disclosed herein are robust, stable, and transformable, and the mutant OCH1 allele and the ability to produce substantially homogeneous N-glycans are maintained for generations after rounds of freezing and thawing and after subsequent transformations.
Hydrolysis of mannose-1-phospho-6-mannose linkage to phospho-6-mannose
Described herein are methods and genetically engineered cells useful for uncapping a mannose-6-phosphate residue on an oligosaccharide.
Modified polypeptide having mannanase activity
Disclosed is a modified polypeptide having mannanase activity and a use thereof.
Engineering gut commensal bacteria to express heterologous proteins in their outer membrane vesicles (OMVS) for delivery to the GI-tract
This invention relates to the delivery of heterologous peptides or proteins such as therapeutic peptides, therapeutic proteins or antigens to mucosal sites using vesicles derived from the outer membrane of commensal bacteria, recombinant bacteria capable of producing such vesicles, and methods for the production of such vesicles. The invention further relates to an inducible expression system for use in recombinant bacteria.
Pichia pastoris strains for producing predominantly homogeneous glycan structure
Disclosed herein are novel Pichia pastoris strains for expression of exogenous proteins with substantially homogeneous N-glycans. The strains are genetically engineered to include a mutant OCH1 allele which is transcribed into an mRNA coding for a mutant OCH1 gene product (i.e., -1,6-mannosyltransferase, or OCH1 protein). The mutant OCH1 protein contains a catalytic domain substantially identical to that of the wild type OCH1 protein, but lacks an N-terminal sequence necessary to target the OCH1 protein to the Golgi apparatus. The strains disclosed herein are robust, stable, and transformable, and the mutant OCH1 allele and the ability to produce substantially homogeneous N-glycans are maintained for generations after rounds of freezing and thawing and after subsequent transformations.
Polypeptides Having Beta-Glucanase Activity, Polynucleotides Encoding Same and Uses Thereof In Cleaning and Detergent Compositions
The invention relates to cleaning or detergent compositions comprising polypeptides exhibiting beta-glucanase activity, optionally comprising one or more amylases and/or one or more proteases and uses thereof in cleaning or detergent applications and processes such as cleaning hard-surfaces, dish wash and laundering. The present invention relates to polypeptides having beta-glucanase activity, catalytic domains, beta-glucan binding domains and polynucleotides encoding the polypeptides, catalytic domains or beta-glucan binding domains. 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, catalytic domains or beta-glucan binding domains.
PICHIA PASTORIS STRAINS FOR PRODUCING PREDOMINANTLY HOMOGENEOUS GLYCAN STRUCTURE
Disclosed herein are novel Pichia pastoris strains for expression of exogenous proteins with substantially homogeneous N-glycans. The strains are genetically engineered to include a mutant OCH1 allele which is transcribed into an mRNA coding for a mutant OCH1 gene product (i.e., -1,6-mannosyltransferase, or OCH1 protein). The mutant OCH1protein contains a catalytic domain substantially identical to that of the wild type OCH1 protein, but lacks an N-terminal sequence necessary to target the OCH1 protein to the Golgi apparatus. The strains disclosed herein are robust, stable, and transformable, and the mutant OCH1 allele and the ability to produce substantially homogeneous N-glycans are maintained for generations after rounds of freezing and thawing and after subsequent transformations.