Patent application number | Description | Published |
20090186381 | CELLULASE VARIANTS WITH REDUCED INHIBITION BY GLUCOSE - A Family 6 cellulase variant enzyme comprising one or more than one amino acid substitution selected from a basic, polar or non-polar amino acid at position 103, a valine or isoleucine at position 136, a tyrosine at position 186, a glutamic acid or glutamine at position 365 and a glutamine at position 410 is provided (said position determined form alignment of the parental Family 6 with SEQ ID NO: 1). Genetic constructs and genetically modified microbes comprising DNA sequences encoding the Family 6 cellulase variant are also provided. Family 6 cellulases of the invention display reduced inhibition by glucose relative to the parent Family 6 cellulases. Such cellulases find use in a variety of applications in industry, e.g., in the hydrolysis of pretreated lignocellulosic feedstock, that require cellulose activity in the presence glucose concentrations that would otherwise inhibit the activity of the parental enzyme. | 07-23-2009 |
20100041100 | FAMILY 6 CELLULASE WITH DECREASED INACTIVATION BY LIGNIN - A modified | 02-18-2010 |
20100093040 | MODIFIED BETA-GLUCOSIDASES WITH IMPROVED STABILITY - Provided are modified beta-glucosidase enzymes, derived from the | 04-15-2010 |
20100304438 | NOVEL BETA-GLUCOSIDASE ENZYMES - Provided are modified beta-glucosidase enzymes, derived from the | 12-02-2010 |
20120295308 | CARBOHYDATE BINDING MODULES WITH REDUCED BINDING TO LIGNIN - Provided is a modified Family 1 carbohydrate binding module (CBM) comprising amino acid substitutions at one or more of positions 10, 11, 12, 14, 17, 21, 24, 29, 31, 33, and 37, said position determined from alignment of a Family 1 CBM amino acid sequence with SEQ ID NO: 30, and exhibiting from about 50% to about 99.9% amino acid sequence identity to SEQ ID NO: 30. Also provided are modified glycosidase enzymes comprising the modified Family 1 CBM, genetic constructs and genetically modified microbes for expressing the modified Family 1 CBM or modified glycosidase enzyme. The modified Family 1 CBM confers reduced lignin binding and/or increased hydrolysing activity in the presence of lignin to the modified glycosidase enzyme, which may be used in a process for hydrolysing cellulose or hemicellulose in the presence of lignin. | 11-22-2012 |
20130337542 | Cellulase Enzyme Mixtures For Depilling and Uses Thereof - The present invention relates to a depilling composition comprising an enzyme mixture that comprises a Family 45 cellulase enzyme component and one or more additional cellulase enzyme components selected from a Family 5 cellulase, a Family 6 cellulase or a combination thereof. The enzyme mixture may be characterized in that the Family 45 and the Family 5 cellulase enzyme components or the Family 45 and the Family 6 cellulase enzyme components are present at a weight ratio that exhibits synergy in an assay that measures specific depilling activity. The enzyme mixture may be secreted by a genetically modified microbe overexpressing theforegoing cellulase enzyme components. Also provided is a process for depilling that comprises a step of contacting cellulose-containing goods with the depilling composition. | 12-19-2013 |
20140295504 | FUNGAL CELLS AND FERMENTATION PROCESSES - The present invention provides an isolated fungal cell that is capable of producing one or more biomass-degrading enzymes and that exhibits increased or decreased expression or copy number of a polynucleotide encoding a PtaB-like protein. Also provided is a fermentation processes for producing one or more biomass-degrading enzymes comprising a fungal cells exhibiting increased or decreased expression or copy number of a polynucleotide encoding a PtaB-like protein. The biomass-degrading enzymes produced by the isolate fungal cell and fermentation processes of the present invention may be used in a process to produce soluble sugars from biomass. | 10-02-2014 |
20140356914 | ENDOGLUCANASE 1B - The present invention provides endoglucanase 1b (EG1b) suitable for use in saccharification reactions. | 12-04-2014 |