One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

Enzymes within a family often catalyze different reactions. In some cases, this variety stems
from different catalytic machinery, but in other cases, the machinery is identical; …

From reviews to the first edtion:" Bornscheuer and Kazlauskas have set out, and succeeded,
in producing a definitive manual on hydrolytic enzymes (especially lipases, esterases, and …

Quaternary stereocenters are a particular challenge for stereoselective synthesis. With a
central view on this specific structural issue, selected examples from the recent literature are …

Esterase plays a major role in the degradation of natural materials and industrial pollutants,
viz., cereal wastes, plastics, and other toxic chemicals. It is useful in the synthesis of optically …

The yeast Candida antarctica produces two different lipases, lipases A and B. While lipase B
(CAL-B) is probably the mostly employed hydrolase in the biocatalysis field, the use of the …

We have developed a statistical method named MAP (mutagenesis assistant program) to
equip protein engineers with a tool to develop promising directed evolution strategies by …

The α/β-hydrolase fold enzyme superfamily is one of the largest groups of structurally related
enzymes.[1] Applications of the members of this versatile enzyme family range from the …

In a previous paper, the combinatorial active‐site saturation test (CAST) was introduced as
an effective strategy for the directed evolution of enzymes toward broader substrate …

Protein engineering has emerged as an important tool to overcome the limitations of natural
enzymes as biocatalysts. Recent advances have mainly focused on applying directed …