Enzymatic Esterification of Ammonium Lactate with Ethanol in Organic Solvent: Kinetic Study

Author

Wang, Yingying ; Jiang, Yanjun ; Zhou, Liya ; Gao, Jing

Author_Institution

Dept. of Bioeng., Hebei Univ. of Technol., Tianjin, China

fYear

2010

fDate

18-20 June 2010

Firstpage

1

Lastpage

4

Abstract

The kinetics of the esterification of ammonium lactate with ethanol catalyzed by Novozym 435 was investigated. The Ping-Pong Bi-Bi enzymatic mechanism with competitive inhibition by both substrates was proposed. The corresponding kinetic parameters were calculated by non-linear regression. r_max = 75.6 μmol/(g·min). The inhibition constants for lactic acid (A) and ethanol (B) were K_iA = 0.016 mol/L and K_iB = 0.38 mol/L, respectively. The model was found to be in good agreement with the experimental data. As we know, it is the first time for the kinetic study of the ethyl lactate synthesis, which used ammonium lactate as raw material and catalyzed by immobilized lipase.

Keywords

biochemistry; chemical technology; enzymes; organic compounds; reaction kinetics theory; reaction rate constants; regression analysis; Novozym 435; Ping-Pong Bi-Bi enzymatic mechanism; ammonium lactate; catalysis; competitive inhibition; esterification kinetics; ethanol; ethyl lactate synthesis; inhibition constants; nonlinear regression; Bismuth; Chemical analysis; Environmentally friendly manufacturing techniques; Ethanol; Industrial pollution; Kinetic theory; Production; Resins; Solvents; Temperature;

fLanguage

English

Publisher

ieee

Conference_Titel

Bioinformatics and Biomedical Engineering (iCBBE), 2010 4th International Conference on

Conference_Location

Chengdu

ISSN

2151-7614

Print_ISBN

978-1-4244-4712-1

Electronic_ISBN

2151-7614

Type

conf

DOI

10.1109/ICBBE.2010.5517244

Filename

5517244