The primary means of immobilizing enzymes are to boost the enzyme productivity and operational stability, alongside facilitating the reuse of enzymes. Notwithstanding the …
MK Nezhad, H Aghaei - Renewable Energy, 2021 - Elsevier
In this paper, cloisite 30B (CL) was converted to tosylated cloisite (TCL) as new heterofunctional support. Lipase from Candida rugosa was covalently immobilized on the …
Enzyme immobilization is a well-known method for the improvement of enzyme reusability and stability. To achieve very high effectiveness of the enzyme immobilization, not only does …
In recent years, biolubricants have been gaining further prominence than conventional petroleum-based lubricants. This trend is observed in almost all sectors relying on these …
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 …
E Gkantzou, AV Chatzikonstantinou, R Fotiadou… - Biotechnology …, 2021 - Elsevier
The ever-growing demand for cost-effective and innocuous biocatalytic transformations has prompted the rational design and development of robust biocatalytic tools. Enzyme …
The lipase from Pseudomonas fluorescens (PFL) has been immobilized on octyl-agarose beads under 16 different conditions (varying pH, ionic strength, buffer, adding some …
Enzyme immobilization is a well-known technique that allows the reuse of the biocatalyst and generally improves its stability. These improved characteristics are of fundamental …
Lipases belong to α/β hydrolases that cause hydrolytic catalysis of triacylglycerols to release monoacylglycerols, diacylglycerols, and glycerol with free fatty acids. Lipases have a …