Proteases have gained significant scientific and industrial interest due to their unique
biocatalytic characteristics and broad-spectrum applications in different industries. The …

The identification or design of biocatalysts to mitigate the accumulation of plastics, including
sub-micro-and nano-sized polyethylene terephthalate (nPET), is becoming a global …

Biocatalysis is currently a workhorse used to produce a wide array of compounds, from bulk
to fine chemicals, in a green and sustainable manner. The success of biocatalysis is largely …

The objective of this paper was to analyze whether an interaction between the effects of the
buffer nature and chemical modification on enzyme stability exists. For this, the lipase B from …

Lipases have valuable potential for industrial use, particularly those mostly active against
water-insoluble substrates, such as triglycerides composed of long-carbon chain fatty acids …

Lipase B from Candida antarctica was immobilized on heterofunctional support octyl
agarose activated with vinyl sulfone to prevent enzyme release under drastic conditions …

With advances in protein structure predictions, the number of available high-quality
structures has increased dramatically. In light of these advances, structure-based enzyme …

Penicillin G acylase (PGA) from Escherichia coli was immobilized on vinyl sulfone (VS)
agarose. The immobilization of the enzyme failed at all pH values using 50 mM of buffer …

Proteases are abundant in prokaryotic genomes (~ 10 per genome), but their recovery
encounters expression problems, as only 1% can be produced at high levels; this value …

In this article, we have analyzed the interactions between enzyme crowding on a given
support and its chemical modification (ethylenediamine modification via the carbodiimide …