Bonazza_2018_Appl.Biochem.Biotechnol_184_182

Reference

Title : Operational and Thermal Stability Analysis of Thermomyces lanuginosus Lipase Covalently Immobilized onto Modified Chitosan Supports - Bonazza_2018_Appl.Biochem.Biotechnol_184_182
Author(s) : Bonazza HL , Manzo RM , Dos Santos JCS , Mammarella EJ
Ref : Appl Biochem Biotechnol , 184 :182 , 2018
Abstract :

The aim of this paper was to evaluate different strategies of chitosan activation using cross-linking reagent like glycidol, epichlorohydrin, and glutaraldehyde for Thermomyces lanuginosus lipase (TLL) immobilization. Operational activity and stability by esterification of oleic acid with ethanol and thermal inactivation using these derivatives were investigated. Derivative obtained by sequentially activation with glycidol, ethylenediamine, and glutaraldehyde and subsequent TLL immobilization showed the best performance, with high hydrolytic activity value. Its stability was 15-fold higher than solubilized TLL in the evaluated inactivation conditions (60 degrees C, 25 mM sodium phosphate buffer pH 7). After 5 cycles of oleic acid esterification, only a few percentage of its conversion has reduced. On the other hand, glycidol-activated chitosan derivative showed very low hydrolytic activity value. Epichlorohydrin-activated chitosan derivative showed regular hydrolytic activity value. Both derivatives showed low immobilization yields. Operational stability of this last derivative was very low, where after the first cycle of oleic acid esterification, only 56% of its initial conversion was obtained. Graphical Abstract .

PubMedSearch : Bonazza_2018_Appl.Biochem.Biotechnol_184_182
PubMedID: 28664524

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Citations formats

Bonazza HL, Manzo RM, Dos Santos JCS, Mammarella EJ (2018)
Operational and Thermal Stability Analysis of Thermomyces lanuginosus Lipase Covalently Immobilized onto Modified Chitosan Supports
Appl Biochem Biotechnol 184 :182

Bonazza HL, Manzo RM, Dos Santos JCS, Mammarella EJ (2018)
Appl Biochem Biotechnol 184 :182