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Immobilized Heterologous Rhizopus Oryzae Lipase as an Efficient Catalyst in the Acetylation of Cortexolone
Author(s) -
Quintana Paula G.,
Guillén Marina,
Marciello Marzia,
Valero Francisco,
Palomo Jose M.,
Baldessari Alicia
Publication year - 2012
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201200178
Subject(s) - rhizopus oryzae , chemistry , acylation , substrate (aquarium) , lipase , catalysis , yield (engineering) , enzyme catalysis , acetylation , organic chemistry , transesterification , enzyme , biochemistry , oceanography , materials science , fermentation , metallurgy , geology , gene
The enzymatic preparation of a monoacetyl derivative of the corticosteroid cortexolone, through a transesterification reaction, is described. The heterologous Rhizopus oryzae lipase, immobilized on three different supports, proved to be an efficient catalyst in the acylation reaction using a complex substrate such as cortexolone. Immobilization of the enzyme on Lewatit 1600 resin at pH = 7 and 25 °C was the best condition for catalysis of the acetylation reaction. The influence of various reaction parameters, such as the nature of the acetylating agent, the solvent, the temperature, and the ratios of acetylating agent to substrate, and enzyme to substrate, was evaluated. Using the response surface methodology and a central composite rotatable design, the specific yield of acetylated cortexolone was optimized by means of the study of the effect of the enzyme (E)/substrate (S) and the acylating agent (A)/substrate ratios. The ratios of 5 (E/S) and 31.6 (A/S) were predicted as the optimal values to reach the maximum specific yield of the product (P): 1.59 mmol P/mmol A · g E. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the reported derivative of this biologically active steroid.