Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase

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A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different...

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Autores principales:	Quintana, P.G., Canet, A., Marciello, M., Valero, F., Palomo, J.M., Baldessari, A.
Formato:	JOUR
Materias:	Chenodeoxycholic acid Esterification Heterologous Rhizopus oryzae Lipase Immobilization Body fluids Catalysis Enzyme immobilization Enzymes Esters Radioactive waste vitrification Substrates Candida antarctica lipase Central composite rotatable design Efficient catalysts Esterification reactions Reaction parameters Response surface methodology Rhizopus oryzae lipase alcohol bile acid chenodeoxycholic acid chenodeoxycholic ester ester fungal enzyme triacylglycerol lipase unclassified drug Article controlled study enzyme immobilization esterification nonhuman pH response surface method solvent effect temperature Candida antarctica Rhizopus oryzae
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_13811177_v118_n_p36_Quintana
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_13811177_v118_n_p36_Quintana2023-10-03T16:11:42Z Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase Quintana, P.G. Canet, A. Marciello, M. Valero, F. Palomo, J.M. Baldessari, A. Chenodeoxycholic acid Esterification Heterologous Rhizopus oryzae Lipase Immobilization Body fluids Catalysis Enzyme immobilization Enzymes Esters Radioactive waste vitrification Substrates Candida antarctica lipase Central composite rotatable design Chenodeoxycholic acid Efficient catalysts Esterification reactions Reaction parameters Response surface methodology Rhizopus oryzae lipase Esterification alcohol bile acid Candida antarctica lipase chenodeoxycholic acid chenodeoxycholic ester ester fungal enzyme Rhizopus oryzae lipase triacylglycerol lipase unclassified drug Article controlled study enzyme immobilization esterification nonhuman pH response surface method solvent effect temperature Candida antarctica Rhizopus oryzae A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different supports proved to be an efficient catalyst, even more active than Candida antarctica lipase, in the esterification reaction using a complex substrate such as a bile acid. The immobilization of the enzyme on Octadecyl Sepabeads at pH 7 and 25°C was the best choice to catalyze the esterification reaction. The influence of various reaction parameters, such as nature of the alcohol, alcohol:substrate ratio, enzyme:substrate ratio, solvent and temperature, was evaluated. Using the response surface methodology and a central composite rotatable design, the conversion of stearyl chenodeoxycholate was optimized by means of the study of the effect of enzyme:substrate ratio and alcohol:substrate ratio. The value 20 for ratios (E/S) and (A/S) was predicted as the optimal value to reach the maximum conversion. However, including economic aspects these ratios can be reduced up to 15. The well-known advantages of biocatalysis and the activity shown by the immobilized heterologous lipase make the reported procedure a convenient way to prepare chenodeoxycholic esters. © 2015 Elsevier B.V. All rights reserved. Fil:Quintana, P.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Baldessari, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13811177_v118_n_p36_Quintana
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Chenodeoxycholic acid Esterification Heterologous Rhizopus oryzae Lipase Immobilization Body fluids Catalysis Enzyme immobilization Enzymes Esters Radioactive waste vitrification Substrates Candida antarctica lipase Central composite rotatable design Chenodeoxycholic acid Efficient catalysts Esterification reactions Reaction parameters Response surface methodology Rhizopus oryzae lipase Esterification alcohol bile acid Candida antarctica lipase chenodeoxycholic acid chenodeoxycholic ester ester fungal enzyme Rhizopus oryzae lipase triacylglycerol lipase unclassified drug Article controlled study enzyme immobilization esterification nonhuman pH response surface method solvent effect temperature Candida antarctica Rhizopus oryzae
spellingShingle	Chenodeoxycholic acid Esterification Heterologous Rhizopus oryzae Lipase Immobilization Body fluids Catalysis Enzyme immobilization Enzymes Esters Radioactive waste vitrification Substrates Candida antarctica lipase Central composite rotatable design Chenodeoxycholic acid Efficient catalysts Esterification reactions Reaction parameters Response surface methodology Rhizopus oryzae lipase Esterification alcohol bile acid Candida antarctica lipase chenodeoxycholic acid chenodeoxycholic ester ester fungal enzyme Rhizopus oryzae lipase triacylglycerol lipase unclassified drug Article controlled study enzyme immobilization esterification nonhuman pH response surface method solvent effect temperature Candida antarctica Rhizopus oryzae Quintana, P.G. Canet, A. Marciello, M. Valero, F. Palomo, J.M. Baldessari, A. Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
topic_facet	Chenodeoxycholic acid Esterification Heterologous Rhizopus oryzae Lipase Immobilization Body fluids Catalysis Enzyme immobilization Enzymes Esters Radioactive waste vitrification Substrates Candida antarctica lipase Central composite rotatable design Chenodeoxycholic acid Efficient catalysts Esterification reactions Reaction parameters Response surface methodology Rhizopus oryzae lipase Esterification alcohol bile acid Candida antarctica lipase chenodeoxycholic acid chenodeoxycholic ester ester fungal enzyme Rhizopus oryzae lipase triacylglycerol lipase unclassified drug Article controlled study enzyme immobilization esterification nonhuman pH response surface method solvent effect temperature Candida antarctica Rhizopus oryzae
description	A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different supports proved to be an efficient catalyst, even more active than Candida antarctica lipase, in the esterification reaction using a complex substrate such as a bile acid. The immobilization of the enzyme on Octadecyl Sepabeads at pH 7 and 25°C was the best choice to catalyze the esterification reaction. The influence of various reaction parameters, such as nature of the alcohol, alcohol:substrate ratio, enzyme:substrate ratio, solvent and temperature, was evaluated. Using the response surface methodology and a central composite rotatable design, the conversion of stearyl chenodeoxycholate was optimized by means of the study of the effect of enzyme:substrate ratio and alcohol:substrate ratio. The value 20 for ratios (E/S) and (A/S) was predicted as the optimal value to reach the maximum conversion. However, including economic aspects these ratios can be reduced up to 15. The well-known advantages of biocatalysis and the activity shown by the immobilized heterologous lipase make the reported procedure a convenient way to prepare chenodeoxycholic esters. © 2015 Elsevier B.V. All rights reserved.
format	JOUR
author	Quintana, P.G. Canet, A. Marciello, M. Valero, F. Palomo, J.M. Baldessari, A.
author_facet	Quintana, P.G. Canet, A. Marciello, M. Valero, F. Palomo, J.M. Baldessari, A.
author_sort	Quintana, P.G.
title	Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_short	Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_full	Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_fullStr	Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_full_unstemmed	Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_sort	enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous rhizopus oryzae lipase
url	http://hdl.handle.net/20.500.12110/paper_13811177_v118_n_p36_Quintana
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_version_	1807319251141263360

Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase

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