Abstract: The enantioselectivity of fungal lipolytic enzymes can be altered by substituting a suitably selected amino acid residue. The residue to be substituted is selected from its location in the 3D structure of the enzyme and an ester substrate (or a substrate analogue). A residue in the lid may be selected if it is located close to the acid part or close to the alcohol part of an ester substrate. A residue outside the lid region may be selected if it is located close to the active site or close to the substrate.

Abstract: Variants of Glycoside Hydrolase family 53 galactanases, e.g. variants of the galactanases from strains of Yersinia, Aspergillus, Humicola, Meripilus, Myceliophthora, Thermomyces, Bacillus, Bifidobacterium, Cellvibrio, Clostridium, Pseudomonas, Thermotoga, or Xanthomonas.

Abstract: The invention relates to a novel class of serine proteases of peptidase family S2A or S1E that are stable in the presence of copper (Cu2+) and/or inhibited by copper only to a limited extent. Structural features of potential relevance for this effect are also disclosed. This class of proteases includes proteases derived from Brachysporiella gayana, Nocardiopsis dassonvillei subsp. dassonvillei, Nocardiopsis prasina, and Nocardiopsis alba, but excludes the known proteases derived from Metarhizium anisopliae and Nocardiopsis sp. NRRL 18262. The invention also relates to DNA encoding such proteases, the expression thereof in a host cell, includiThe invention relates to a novel class of serine proteases of peptidase family S2A or S1E that are stable in the presence of copper (Cu2+) and/or inhibited by copper only to a limited extent. Structural features of potential relevance for this effect are also disclosed.