Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study
The present study reports on Candida rugosa lipase (CRL) supported on magnetized nanosilica from oil palm leaves (CRL/Gl-A-SiO2-MNPs) and its utilization in the catalytic synthesis of butyl butyrate. Statistical optimization of process parameters, viz: enzyme loading, incubation time, temperature an...
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Taiwan Institute of Chemical Engineers, Elsevier B.V.
2018
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my.utm.855162020-06-30T08:49:55Z http://eprints.utm.my/id/eprint/85516/ Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study Onoja, Emmanuel Chandren, Sheela Abdul Razak, Fazira Ilyana Abdul Wahab, Roswanira QD Chemistry The present study reports on Candida rugosa lipase (CRL) supported on magnetized nanosilica from oil palm leaves (CRL/Gl-A-SiO2-MNPs) and its utilization in the catalytic synthesis of butyl butyrate. Statistical optimization of process parameters, viz: enzyme loading, incubation time, temperature and substrate molar ratio (1-butanol:n-butyric acid), was executed using the Box–Behnken Design. Under optimized conditions, using 3.5 mg/mL of CRL/Gl-A-SiO2-MNPs, molar ratio of 2:1, incubated at 45 °C a 93.9% yield of ester was achieved in 3 h. CRL/Gl-A-SiO2-MNPs-catalyzed the esterification reaction according to Bi-Bi Ping Pong mechanism. The obtained kinetic values corresponded to Vmax of 0.298 mM/min, as well as Michaelis-Menten constants for substrates, n-butyric acid (KM a) and 1-butanol (KM b) of 17.274 and 13.780 mM, respectively. The values for Kcat, Keff and inhibition constant for 1-butanol (Ki b) for the CRL/Gl-A-SiO2-MNPs-catalyzed esterification are 5.109/min, 0.371/min mM−1 and 288.184 mM, respectively. CRL/Gl-A-SiO2-MNPs exhibited higher thermal-stability than the aggregated CRL, as seen in the attained higher values of half-life (45.894 min), D-value (152.45 min), Ed (125 KJ/mol), ΔHd∘ (122.64 KJ/mol) and ΔGd∘ (11.957 KJ/mol) at 70 °C. Storage stability of CRL/Gl-A-SiO2 MNPs was improved by ∼ 9 fold over the aggregated CRL when incubated at room temperature. Taiwan Institute of Chemical Engineers, Elsevier B.V. 2018-10 Article PeerReviewed Onoja, Emmanuel and Chandren, Sheela and Abdul Razak, Fazira Ilyana and Abdul Wahab, Roswanira (2018) Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study. Journal of the Taiwan Institute of Chemical Engineers, 91 . pp. 105-118. ISSN 1876-1070 http://dx.doi.org/10.1016/j.jtice.2018.05.049 DOI:10.1016/j.jtice.2018.05.049 |
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QD Chemistry Onoja, Emmanuel Chandren, Sheela Abdul Razak, Fazira Ilyana Abdul Wahab, Roswanira Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study |
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The present study reports on Candida rugosa lipase (CRL) supported on magnetized nanosilica from oil palm leaves (CRL/Gl-A-SiO2-MNPs) and its utilization in the catalytic synthesis of butyl butyrate. Statistical optimization of process parameters, viz: enzyme loading, incubation time, temperature and substrate molar ratio (1-butanol:n-butyric acid), was executed using the Box–Behnken Design. Under optimized conditions, using 3.5 mg/mL of CRL/Gl-A-SiO2-MNPs, molar ratio of 2:1, incubated at 45 °C a 93.9% yield of ester was achieved in 3 h. CRL/Gl-A-SiO2-MNPs-catalyzed the esterification reaction according to Bi-Bi Ping Pong mechanism. The obtained kinetic values corresponded to Vmax of 0.298 mM/min, as well as Michaelis-Menten constants for substrates, n-butyric acid (KM a) and 1-butanol (KM b) of 17.274 and 13.780 mM, respectively. The values for Kcat, Keff and inhibition constant for 1-butanol (Ki b) for the CRL/Gl-A-SiO2-MNPs-catalyzed esterification are 5.109/min, 0.371/min mM−1 and 288.184 mM, respectively. CRL/Gl-A-SiO2-MNPs exhibited higher thermal-stability than the aggregated CRL, as seen in the attained higher values of half-life (45.894 min), D-value (152.45 min), Ed (125 KJ/mol), ΔHd∘ (122.64 KJ/mol) and ΔGd∘ (11.957 KJ/mol) at 70 °C. Storage stability of CRL/Gl-A-SiO2 MNPs was improved by ∼ 9 fold over the aggregated CRL when incubated at room temperature. |
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Article |
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Onoja, Emmanuel Chandren, Sheela Abdul Razak, Fazira Ilyana Abdul Wahab, Roswanira |
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Onoja, Emmanuel Chandren, Sheela Abdul Razak, Fazira Ilyana Abdul Wahab, Roswanira |
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Onoja, Emmanuel |
title |
Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study |
title_short |
Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study |
title_full |
Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study |
title_fullStr |
Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study |
title_full_unstemmed |
Enzymatic synthesis of butyl butyrate by Candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: Process optimization, kinetic and thermodynamic study |
title_sort |
enzymatic synthesis of butyl butyrate by candida rugosa lipase supported on magnetized-nanosilica from oil palm leaves: process optimization, kinetic and thermodynamic study |
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Taiwan Institute of Chemical Engineers, Elsevier B.V. |
publishDate |
2018 |
url |
http://eprints.utm.my/id/eprint/85516/ http://dx.doi.org/10.1016/j.jtice.2018.05.049 |
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