Immobilization of trypsin on polysaccharide film from Anacardium occidentale L. and its application as cutaneous dressing

Improvement of the stability and activity of immobilized trypsin on modified Fe3O4 magnetic nanoparticles for hydrolysis of bovine serum albumin and its application in the bovine milk

“…Furthermore at 55°C, the immobilized trypsin retained 38.7% of its initial activity after 120 min of heat treatment, whereas the free trypsin retained 16% of its initial activity after 120 min. In several studies of bovine pancreatic trypsin, the enzyme preserves a large proportion of its activity until 50°C, after which it rapidly loses its catalytic activity (Montero, Silva, & Silva, 2007). As can be seen from the results, at higher temperature value (55°C), there is a relatively higher decrease in the activity of immobilized trypsin by approaching that of free trypsin with time, indicating that at high temperature values, enzyme denaturation can be observed with time.…”

Carrier free immobilization and characterization of trypsin

“…Production of peptides in a range ideal for mass mapping through mass spectroscopy makes the enzyme suitable for protein fragmentation in order for identifi cation and characterization of proteins (Massolini and Calleri 2005). Furthermore trypsin is used in many processes such as preparation of bioactive peptides, treatment of milk (Bryjak and Kolarz 1998), cutaneous dressing (Monteiro et al 2007), and as an additive in detergent industry (Ktari et al 2012).…”

Effect of enzyme location on activity and stability of trypsin and urease immobilized on porous membranes by using layer-by-layer self-assembly of polyelectrolyte

“…As above mentioned, the activity test was carried out using the same samples of TRY immobilized membranes indicating that TRY retains its activity after repeated exposure to the substrate. A TRY stability increase has been reported to also occur by covalent bonding to polysaccharide [39] and to silica beads [40]. However, the effect takes place at a much lesser extent probably due to the active site modification.…”