The invention relates to an endocellulase catalytic domain comprising the sequence of SEQ ID NO: 1 or a functionally equivalent variant of said catalytic domain that substantially maintains or improves its catalytic activity. The invention also relates to a polypeptide, a nucleic acid, an expression cassette, a vector or a host cell. Additionally, the invention relates to the use of an endocellulase catalytic domain or the polypeptide of the invention for hydrolysing cellulose, producing bioethanol or as a detergent. The invention also relates to a method for hydrolysing cellulose and for producing bioethanol.

The present invention relates to an isolated synthetic polynucleotide encoding the mature amylase AX856 from Bacillus akibai, using codon modified polynucleotide constructs for the expression of the amylase.

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.

Chimeric and other variant β-glucuronidase enzymes with enhanced properties as compared to unmodified enzyme are provided. The enzymes of the invention advantageously exhibit enhanced enzymatic activity, enhanced substrate range, enhanced pH range, enhanced temperature range and/or enhanced enzyme stability. Methods of using the variant enzymes for hydrolysis of glucuronide substrates, including opiates and benzodiazepines, are also provided.

The application relates to antimicrobial agents against Gram-negative bacteria, in particular to fusion proteins composed of an enzyme having the activity of degrading the cell wall of Gram-negative bacteria and a peptide stretch fused to the enzyme at the N- or C-terminus, as well as pharmaceutical compositions comprising the same. Moreover, it relates to nucleic acid molecules encoding such a fusion protein, vectors comprising said nucleic acid molecules and host cells comprising either said nucleic acid molecules or said vectors. In addition, it relates to such a fusion protein for use as a medicament, in particular for the treatment or prevention of Gram-negative bacterial infections, as diagnostic means or as cosmetic substance. The application also relates to the treatment or prevention of Gram-negative bacterial contamination of foodstuff, of food processing equipment, of food processing plants, of surfaces coming into contact with foodstuff, of medical devices, of surfaces in hospitals and surgeries.

The present disclosure relates to a novel chitinolytic enzyme, particularly to a chitinolytic enzyme including an exo-β-N-acetylglucosaminidase (Clocel_3193) constituting a cellulosome derived from Clostridium cellulovorans as an active ingredient. The present disclosure allows utilization of chitin biomass which has not been used formerly as a raw material and allows environment-friendly production of N-acetylglucosamine. In addition, since the Clocel_3193 has a cell wall binding ability and degrading ability, the Clocel_3193 may be used in an antifungal composition.

The present invention discloses an L-type amylase variant and use thereof. The -amylase variant is obtained by deleting the first N-terminal amino acid residue V from the -amylase of B. licheniformis and replacing it with three other amino acid residues DGL. The -amylase variant provided by the present invention has high catalytic activity under the acidic conditions of pH 5.0-5.8 and a high temperature of 100 C. or above. The acid resistance and thermal stability of these -amylase variants are suitable for starch liquefaction.

Aspects of the present disclosure include glucoamylase (GA) variants having at least one improved property over a parent GA, compositions containing the GA variants, nucleic acids encoding the GA variants, and methods for producing and using the same. In some aspects, the GA variant is a variant of a parent GA from Humicola grisea.

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.

Methods for regulating protein activity by fusing dimerization domains to target protein are provided. Chimeric proteins that include dimerization domains fused to target proteins for altering the activity of the target proteins are described. Engineered nucleic acids encoding chimeric proteins and hosts engineered to express engineered nucleic acids are also provided.