Design of an immobilized preparation of catalase from Thermus thermophilus to be used in a wide range of conditions.

Use of immobilized lipases for lipase purification via specific lipase–lipase interactions

“…Moreover, this support has been used to yield a very intense enzyme-support multipoint attachment between the enzyme and the support, and a fully inert surface after immobilization. Thus, many enzymes have been stabilized using this technique, e.g., Penicillin G acylase from Escherichia coli [26] and K. citrophila [27], trypsin [28], chymotrypsin [29], alcalase [30], carboxypeptidase A [31], FNR NADP-reductase [32], esterase [33], thermolysin [34], DAAO [35], catalases [36,37], and lipases from different sources [18,38], urokinase [39], l-aminoacylase [40], chitosinase [41]. The final reduction of the immobilized preparations with sodium borohydride permits to have very stable secondary amino bonds and very inert hydroxy groups in the support surface (Fig.…”

Improved pharmacokinetics and stability properties of catalase by chemical glycosidation with end‐group activated dextran

“…20 Through this approach, the intra and intersubunit crosslinking could provide a more compact and stable protein structure. However, the approach here described for preparing a dextran-catalase conjugate is better from a pharmacological point of view.…”

Influence of stabilizers cosolutes on catalase conformation

“…The fluorescence quenching of a fluorophore by a quencher is a technique that gives information not only about the quencher accessibility to the fluorophore, but also of any modification at the TRP microenvironment [7] induced by the cosolute presence. According to Eq.…”

“…Costa et al [6] studied the effect of different cosolutes on the kinetic stability of catalase and found that glycerol and glutaraldehyde significantly increase the half life of the enzyme; however, studies about the effects that solutes have on the conformational structure of the enzyme have not been done yet. Hidalgo et al [7] studied the kinetic stability of the fungus catalase immobilized on different supports, but they did not give any information about how the conformation of the enzyme is modified and the factors that may influence the enzyme conformation.…”