2009
DOI: 10.1016/j.jbiotec.2009.09.002
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Improved reactivation of immobilized-stabilized lipase from Thermomyces lanuginosus by its coating with highly hydrophilic polymers

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Cited by 30 publications
(20 citation statements)
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“…For the amino-dextran (AMD) preparation, 18 aldehydedextran was first obtained by oxidation of 1.67 g of dextran (average mol wt 15 000-30 000, Aldrich) dissolved in water (50 cm 3 ) with 0.8 g of sodium periodate (NaIO 4 , ≥99.0%, Aldrich). The oxidation was performed overnight at room temperature under magnetic stirring.…”
Section: Methodsmentioning
confidence: 99%
“…For the amino-dextran (AMD) preparation, 18 aldehydedextran was first obtained by oxidation of 1.67 g of dextran (average mol wt 15 000-30 000, Aldrich) dissolved in water (50 cm 3 ) with 0.8 g of sodium periodate (NaIO 4 , ≥99.0%, Aldrich). The oxidation was performed overnight at room temperature under magnetic stirring.…”
Section: Methodsmentioning
confidence: 99%
“…In fact, if several enzyme-support linkages are established, the refolding may be facilitated because the relative positions of these groups cannot be altered, and those may act as reference points during refolding [29]. Even heavily chemically modified enzymes could be unfolded and refolded after immobilization via multipoint covalent attachment [29,30]. The main requirements to use this strategy are that the enzyme should remain attached to the support during all the reactivation steps, and that the support is inert enough to avoid undesired enzyme-support interactions.…”
Section: Introductionmentioning
confidence: 99%
“…Furthermore, the support surface will never be "inert", and this can produce undesired enzyme supports/interactions during storage or use. This kind of immobilization may not be compatible with folding/unfolding reactivation strategies of enzymes: unfolding may produce enzyme release, whereas refolding will be affected by interactions with the support [4,[49][50][51][52] (Fig. 6).…”
Section: Immobilization Via Physical Adsorptionmentioning
confidence: 99%