Abstract:
Provided is a novel β-glucosidase which can exhibit a high activity in the presence of a biomass and has high thermal stability to conventional enzymes. A β-glucosidase characterized by being produced by substituting and/or deleting at least three amino acid residues selected from the group consisting of Glu39, Asp169, Arg170, Arg220, Tyr227 and Glu330 in the amino acid sequence for a parent β-glucosidase by another amino acid residue, and exhibiting a cellobiose decomposition activity.
Abstract:
Provided is an endoglucanase of which the activity can be inhibited by a lignin-derived aromatic compound at a reduced level. An endoglucanase produced by substituting a tryptophan residue located at position-273 in the amino acid sequence for an endoglucanase originated from a wild-type thermophilic bacterium by an amino acid residue other than an aromatic amino acid residue.
Abstract:
Provided is a novel ß-glucosidase which can exhibit a high activity in the presence of a biomass and has high thermal stability to conventional enzymes. A ß-glucosidase characterized by being produced by substituting and/or deleting at least three amino acid residues selected from the group consisting of Glu39, Asp169, Arg170, Arg220, Tyr227 and Glu330 in the amino acid sequence for a parent ß-glucosidase by another amino acid residue, and exhibiting a cellobiose decomposition activity.
Abstract:
Provided is an endoglucanase of which the activity can be inhibited by a lignin derived aromatic compound at a reduced level. An endoglucanase produced by substituting a tryptophan residue located at position 273 in the amino acid sequence for an endoglucanase originated from a wild type thermophilic bacterium by an amino acid residue other than an aromatic amino acid residue.
Abstract:
Provided is an endoglucanase of which the activity can be inhibited by a lignin-derived aromatic compound at a reduced level. An endoglucanase produced by substituting a tryptophan residue located at position-273 in the amino acid sequence for an endoglucanase originated from a wild-type thermophilic bacterium by an amino acid residue other than an aromatic amino acid residue.
Abstract:
Provided is a novel β-glucosidase exhibiting high activity in the presence of biomass and having high thermal stability compared to conventional enzymes. The β-glucosidase includes substitutions and/or deletions of amino acids, i.e., at least three amino acids selected from the group consisting of Glu39, Asp169, Arg170, Arg220, Tyr227, and Glu330, of the parent β-glucosidase with other amino acids and shows a cellobiose decomposition activity.
Abstract:
Provided is a novel &bgr;-glucosidase which can exhibit a high activity in the presence of a biomass and has high thermal stability to conventional enzymes. A &bgr;-glucosidase characterized by being produced by substituting and/or deleting at least three amino acid residues selected from the group consisting of Glu39, Asp169, Arg170, Arg220, Tyr227 and Glu330 in the amino acid sequence for a parent &bgr;-glucosidase by another amino acid residue, and exhibiting a cellobiose decomposition activity.