The use of enzymes in industrial processes requires the improvement of their features in
many instances. Enzyme immobilization, a requirement to facilitate the recovery and reuse …

Enzymes are efficient catalysts designed by nature to work in physiological environments of
living systems. The best operational conditions to access and convert substrates at the …

The stability of proteins in aqueous solution is routinely enhanced by cosolvents such as
glycerol. Glycerol is known to shift the native protein ensemble to more compact states …

Hyperosmotic stress is an often overlooked process that potentially contributes to a number
of human diseases. Whereas renal hyperosmolarity is a well-studied phenomenon, recent …

Within the context of biomedicine and pharmaceutical sciences, the issue of (therapeutic)
protein stabilization assumes particular relevance. Stabilization of protein and protein-like …

Lipases A and B from Candida antarctica (CALA, CALB), and those from Candida rugosa
(CRL) and Rhizomucor miehei (RML) have been immobilized on octyl agarose beads under …

The lipase from Pseudomonas fluorescens (PFL) has been immobilized on octyl-agarose
beads under 16 different conditions (varying pH, ionic strength, buffer, adding some …

Due to the problems raised by the use of animal or microbial recombinant proteases, the use
of proteases from vegetable origin is becoming increasingly popular.. Among them, sulfidryl …

Lipase from Thermomyces lanuginosus (TLL) was immobilized on octyl agarose (OC). Three
different TLL-OC biocatalysts were prepared: one lowly loaded using a low enzyme …

Organisms use organic molecules called osmolytes to adapt to environmental conditions. In
vitro studies indicate that osmolytes thermally stabilize proteins, but mechanisms are …