Optimization of isoamyl acetate production by using immobilized lipase from Mucor miehei by response surface methodology

• Published in: Enzyme and microbial technology Vol. 26; no. 2; pp. 131 - 136
• Main Authors: Hari Krishna, S, Manohar, B, Divakar, S, Prapulla, S.G, Karanth, N.G
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 01-02-2000; Elsevier Science
• Subjects: Acidity; Alcohols; Bioconversion; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Enzymatic synthesis; Enzyme immobilization; Enzyme kinetics; Esterification; Flavors; Fundamental and applied biological sciences. Psychology; Isoamyl acetate; Lipase; Lipozyme IM; Methods. Procedures. Technologies; Mucor miehei; Response surface methodology; Surface phenomena; Enzymatic synthesis; Lipozyme IM; Mucor miehei; Isoamyl acetate; Response surface methodology; Lipase; Esterification; Enzyme; Phycomycetes; Triacylglycerol lipase; Esterases; Acetic acid derivative; Optimization; Carboxylic ester hydrolases; Fungi; Statistical method; Production; Hydrolases; Response surface; Immobilized enzyme; Thallophyta
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/S0141-0229(99)00149-0

Immobilized lipase from
Mucor miehei was employed for the esterification of isoamyl alcohol with acetic acid in
n-heptane solvent. The important process variables studied were enzyme/substrate (E/S) ratio, alcohol (acid) concentration, and incubation period. Based on Box–Behnken design of experiments, a second order response function was developed. The percentage esterification increased with both E/S ratio and time and decreased with alcohol (acid) concentration. The model indicated optimum conditions for maximum esterification ranging from 20 to 99.6% in the alcohol (acid) concentration range of 0.031 to 0.3 M for a range of E/S ratios 8.33 to 50 g/mol, which were in good agreement with the experimental yields.