Lipase-Catalyzed Synthesis of 6-<i>O</i>-D-Glucosyldecanoate in<i>Tert</i>-Butanol: Reaction Optimization and Effect of Mixing Power Input

Han, Jin; Annuar, Mohamad Suffian Mohamad; Ariffin, Maryam Farhana Kamel; Gumel, Ahmad Mohammed; Ibrahim, Shaliza; Heidelberg, Thorsten; Bakar, Baki Bin; Hossain, Alamgir; Sharifuddin, Yusrizam

doi:10.5504/bbeq.2011.0092

Cited by 5 publications

(1 citation statement)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lipases (EC 3.1.1.3) from different organisms were reported to catalyze the synthesis of different industrially important chemicals and their intermediates (Han et al 2011 ; Gumel et al 2013a , b , c , 2015 ; Gumel and Annuar 2014 ) including flavor esters such as ethyl caproate (Alvarez-Macarie and Baratti 2000 ), cis -3-hexenyl acetate (Jin et al 2012 ), hexyl octanoate (Lopresto et al 2014 ), geraniol and citronellol (Claon and Akoh 1993 ), butyl-hexanoate (Talon et al 1996 ), butyl-acetate, and propyl-acetate esters (Mahapatra et al 2009 ). Similarly, Cvjetko et al ( 2012 ) reported the use of Candida antarctica lipase B to catalyze the synthesis of isoamyl acetate in packed bed microreactor (Mason et al 2007 ).…”

Section: Introductionmentioning

confidence: 99%

Thermomyces lanuginosus lipase-catalyzed synthesis of natural flavor esters in a continuous flow microreactor

Gumel

Annuar

2016

3 Biotech

View full text Add to dashboard Cite

Enzymatic catalysis is considered to be among the most environmental friendly processes for the synthesis of fine chemicals. In this study, lipase from Thermomyces lanuginosus (Lecitase Ultra™) was used to catalyze the synthesis of flavor esters, i.e., methyl butanoate and methyl benzoate by esterification of the acids with methanol in a microfluidic system. Maximum reaction rates of 195 and 115 mM min−1 corresponding to catalytic efficiencies (k cat/K M) of 0.30 and 0.24 min−1 mM−1 as well as yield conversion of 54 and 41 % were observed in methyl butanoate and methyl benzoate synthesis, respectively. Catalytic turnover (k cat) was higher for methyl butanoate synthesis. Rate of synthesis and yield decreased with increasing flow rates. For both esters, increase in microfluidic flow rate resulted in increased advective transport over molecular diffusion and reaction rate, thus lower conversion. In microfluidic synthesis using T. lanuginosus lipase, the following reaction conditions were 40 °C, flow rate 0.1 mL min−1, and 123 U g−1 enzyme loading found to be the optimum operating limits. The work demonstrated the application of enzyme(s) in a microreactor system for the synthesis of industrially important esters.

show abstract