It is a mammoth task to develop a modular protein toolbox enabling the production of
posttranslational organized multifunctional enzymes that catalyze reactions in complex …

Literature from the past two decades has outlined the existence of a trade-off between
protein stability and function. This trade-off creates a unique challenge for protein engineers …

Enzymes catalyze reactions with exceptional selectivity and rate acceleration but are often
limited by instability. Towards a generic route to thermo-resilience, we established the …

The wide range of moieties installed in ribosomally synthesized and post‐translationally
modified peptides (RiPPs) suggests largely untapped potential for protein engineering …

Cyclization of proteins using SpyTag/SpyCatcher is a novel approach to increase their
thermal stability. In this paper, we test this approach on two β-galactosidases from Bacillus …

Integral membrane proteins isolated from cellular environment often lose activity and native
conformation required for functional analyses and structural studies. Even in their native …

The reduction of fossil fuels, coupled with its increase in price, has made the search for
alternative energy resources more plausible. One of the topics gaining fast interest is the …

A bifunctional enzyme has been created by fusing two Bacillus subtilis enzymes: the β-1, 3–
1, 4-glucanase (BglS, EC 3.2. 1.73) that hydrolyzes plant cell wall β-glucans and the copper …

Enzymes often have marginal stability, with unfolding typically leading to irreversible
denaturation. This sensitivity is a major barrier, both for de novo enzyme development and …

High xylanase activity and stability toward alkaline pH is strongly desired for pulping and
bleaching processes. We previously enhanced thermal stability of Bacillus circulans …