Iogen Energy Corporation

Novozymes A/s

Nabil Masri

Patrick St-Pierre

Theresa C White

John J Tomashek

James A Lavigne

Brian R Scott

Marie-Christine Fournier

Loreta Gudynaite-Savitch

Christopher Hill

Christopher D Hindle

Christopher M D Hill

Fuad Tahna

Sandra Mortimer

Jacqueline Montalibet

Chris Hill

Provided are modified cellulase enzymes exhibiting increase cellulose-hydrolyzing activity in the presence of lignin and/or reduced binding to lignin comprising modified linker peptides comprising one or more amino acid substitutions, insertions, or deletions that result in (a) a decrease in the calculated isoelectric point of the linker peptide and/or (b) an increase in the ratio of threonine:serine in the linker peptide relative to a parental linker peptide from which said modified linker peptide is derived. Also provided are genetic constructs comprising nucleic acid sequences encoding for modified cellulase enzymes, methods for the production of the modified cellulase enzymes from host strains and a process for hydrolysing cellulose with the modified cellulases in the presence of lignin.

Cellulase enzymes having a modified linker and reduced lignin binding

Provided are isolated cellobiohydrolases comprising a modified Glycoside Hydrolase (GH) Family 7 catalytic domain, a GH Family 7 catalytic domain and a modified Family 1 carbohydrate binding module (CBM), or both a modified Family 7 catalytic domain and a modified Family 1 CBM. Such isolated cellobiohydrolases exhibit from 45% to about 99.9% amino acid sequence identity to amino acids 1-436 of SEQ ID NO: 1 or to amino acids 1-438 of SEQ ID NO: 2 and improved activity on process substrates. Also provided are genetic constructs and genetically modified microbes for expressing the isolated cellobiohydrolases, a process for producing the isolated cellobiohydrolases, cellulase enzyme mixtures comprising the isolated cellobiohydrolase and a process for hydrolyzing a cellulosic substrate with such cellulase enzyme mixtures.

Cellobiohydrolase enzymes

Provided are modified cellulase enzymes exhibiting increase cellulose-hydrolyzing activity in the presence of lignin and/or reduced binding to lignin comprising modified linker peptides comprising one or more amino acid substitutions, insertions, or deletions that result in (a) a decrease in the calculated isoelectric point of the linker peptide and/or (b) an increase in the ratio of threonine:serine in the linker peptide relative to a parental linker peptide from which said modified linker peptide is derived. Also provided are genetic constructs comprising nucleic acid sequences encoding for modified cellulase enzymes, methods for the production of the modified cellulase enzymes from host strains and a process for hydrolyzing cellulose with the modified cellulases in the presence of lignin.

The present invention relates to a modified Family 5 cellulase comprising a substitution of an amino acid at position 363 with a non-native alanine, serine or threonine, the position determined from alignment of the modified Family 5 cellulase with amino acids 71-397 of aCel5A amino acid sequence as set forth in SEQ ID NO:1 and enzyme mixtures comprising same. Additionally provided is a genetic construct comprising a nucleic acid sequence encoding the modified Family 5 cellulase and a genetically modified microbe comprising the genetic construct. The invention also provides a process for producing the modified Family 5 cellulase.

Modified family 5 cellulases and uses thereof

A modified Family 6 cellulase enzyme comprising a proline residue at position 413 is provided. Genetic constructs and genetically modified microbes comprising DNA sequences encoding the modified Family 6 cellulase are also provided. Family 6 cellulases of the invention display improved thermostability, thermophilicity, alkalophilicity, or a combination thereof, relative to the parent Family 6 cellulases. Such cellulases find use in a variety of applications in industry that require cellulase stability and activities at temperatures, pH values, or both, above that of the native enzyme.

Modified cellulases with increased thermostability, thermophilicity, and alkalophilicity

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Gatineau, Canada

Nabil Masri