Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI)

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Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI).

Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on its surface. The enzyme activity was fully maintained during the coating and the thermal stability was marginally improved. The enzyme release fro...

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Intermediate Production of Mono- and Diolein by an Immobilized Lipase from Candida antarctica

Lipase from Candida antarctica, fixed on macroporous acrylic resin, has been used for the intermediate production of mono- and diolein by hydrolysis of triolein. The effect of altering concentrations of triolein and glycerol and the function of the molecular sieve on the hydrolysis reaction of triolein were investigated. The highest hydrolysis yield was observed for the utmost concentration of ...

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[Expression of Candida antarctica lipase B on yeast surface and synthesis of ethyl hexanoate catalyzed by CALB].

Short-chain esters play a significant role in the food industry as flavor and aroma constituents. Candida antarctica lipase B (CALB) is one of the most effective catalysts for organic synthesis. We constructed a CALB-displaying yeast whole-cell biocatalyst and applied it to esterification from caproic acid and ethanol. CALB was fused with the alpha-agglutinin C-terminal and the signal peptide o...

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Rational redesign of Candida antarctica lipase B

This thesis describes the use of rational redesign to modify the properties of the enzyme Candida antarctica lipase B. Through carefully selected single-point mutations, we were able to introduce substrate-assisted catalysis and to alter the reaction specificity. Other single-point mutations afforded variants with greatly changed substrate selectivity and enantioselectivity. Mutation of the cat...

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ژورنال

عنوان ژورنال: Molecules

سال: 2016

ISSN: 1420-3049

DOI: 10.3390/molecules21060751