The present invention relates to glucoamylase variants having improved thermostability. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

Provided herein are compositions and methods for stabilizing enzymes. Also provided are systems, compositions and methods for using the stabilized enzymes to produce a desired compound.

Provided herein are compositions and methods for stabilizing enzymes. Also provided are systems, compositions and methods for using the stabilized enzymes to produce a desired compound.

The present invention relates to a method to improve the production of a secondary metabolite catalyzed by a non-ribosomal peptide synthetase comprising contacting in a eukaryotic host a eukaryotic non-ribosomal peptide synthetase with an MbtH-like protein. The present invention further relates to a composition comprising a eukaryotic non-ribosomal peptide synthetase that is not a hybrid and a prokaryotic MbtH and to a eukaryotic host cell comprising a non-ribosomal peptide synthetase and a polynucleotide allowing the expression of an MbtH-like protein.

The present invention relates to a method to improve the production of a secondary metabolite catalyzed by a non-ribosomal peptide synthetase comprising contacting in a eukaryotic host a eukaryotic non-ribosomal peptide synthetase with an MbtH-like protein. The present invention further relates to a composition comprising a eukaryotic non-ribosomal peptide synthetase that is not a hybrid and a prokaryotic MbtH and to a eukaryotic host cell comprising a non-ribosomal peptide synthetase and a polynucleotide allowing the expression of an MbtH-like protein.

Provided herein are penicillin expandase mutants, DNA coding the mutants, reagent kit containing the mutants and the application. The penicillin expandase mutants using SEQ ID NO.: 2 in the Sequence Listing as a reference sequence, have at least one amino acid mutation at residue positions corresponding to threonine at position 42 and glutamine at position 126, wherein, amino acid at position 42 is substituted by any other natural amino acid except threonine, amino acid at position 126 is substituted by any other natural amino acid except glutamine. The penicillin expandase mutants of present invention have increased its thermostability and catalytic activity; it is more suitable for commercial and industrial applications.

The present invention relates to glucoamylase variants having improved thermostability. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention relates to glucoamylase variants having improved thermostability. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention discloses methods and systems for producing fungal secondary metabolites. The invention also discloses genetically modified organisms and kits including such organisms for producing fungal secondary metabolites.

The present invention relates to the hemi sulfuric acid salt of methyl (R)-2-amino-2-(cyclohexa-1,4-dien-1-yl)acetate, also trivially referred to as the hemi sulfuric acid salt of D-dihydrophenylglycine methyl ester, to a method for the preparation of said salt and to the use of said salt in the enzymatic synthesis of antibiotics.