Lipase‐catalyzed ethanolysis of soybean oil in a solvent‐free system using central composite design and response surface methodology

Rodrigues, Rafael C.; Volpato, Giandra; Ayub, Marco Antônio Záchia; Wada, Keiko

doi:10.1002/jctb.1879

Cited by 43 publications

(16 citation statements)

References 12 publications

(19 reference statements)

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“…In addition, we evaluated the methanolysis of soybean oil and waste chicken oil by wild-type lipase T6, variant H86Y/A269T/R374W and two commercial lipases, T. lanuginosus lipase (Novozymes®, Lipolase 100 L, TLL) and Candida antarctica lipase B (Novozymes® CALB), which were often used in biodiesel production studies (Maceiras et al 2011;Raita et al 2011;Rodrigues et al 2008;Tan et al 2010). The protein concentration of the lipase solutions was determined by the method of Bradford (Bradford 1976), and samples were analyzed on SDS-PAGE (Sambrook and Russel 2001) to ensure their protein purity.…”

Section: Methodsmentioning

confidence: 99%

Structural insights into methanol-stable variants of lipase T6 from Geobacillus stearothermophilus

Dror

Kanteev

Kagan

et al. 2015

Appl Microbiol Biotechnol

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Enzymatic production of biodiesel by transesterification of triglycerides and alcohol, catalyzed by lipases, offers an environmentally friendly and efficient alternative to the chemically catalyzed process while using low-grade feedstocks. Methanol is utilized frequently as the alcohol in the reaction due to its reactivity and low cost. However, one of the major drawbacks of the enzymatic system is the presence of high methanol concentrations which leads to methanol-induced unfolding and inactivation of the biocatalyst. Therefore, a methanol-stable lipase is of great interest for the biodiesel industry. In this study, protein engineering was applied to substitute charged surface residues with hydrophobic ones to enhance the stability in methanol of a lipase from Geobacillus stearothermophilus T6. We identified a methanol-stable variant, R374W, and combined it with a variant found previously, H86Y/A269T. The triple mutant, H86Y/A269T/R374W, had a half-life value at 70 % methanol of 324 min which reflects an 87-fold enhanced stability compared to the wild type together with elevated thermostability in buffer and in 50 % methanol. This variant also exhibited an improved biodiesel yield from waste chicken oil compared to commercial Lipolase 100L® and Novozyme® CALB. Crystal structures of the wild type and the methanol-stable variants provided insights regarding structure-stability correlations. The most prominent features were the extensive formation of new hydrogen bonds between surface residues directly or mediated by structural water molecules and the stabilization of Zn and Ca binding sites. Mutation sites were also characterized by lower B-factor values calculated from the X-ray structures indicating improved rigidity.

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Section: Methodsmentioning

confidence: 99%

Structural insights into methanol-stable variants of lipase T6 from Geobacillus stearothermophilus

Dror

Kanteev

Kagan

et al. 2015

Appl Microbiol Biotechnol

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“…Recently, several researchers have reported enzymatic synthesis of esters in organic solvent-free systems in an attempt to make the processes commercially feasible [3,16,22]. These systems offer several advantages including minimizing environmental impact by avoiding the use of toxic and flammable organic solvents, significant cost-savings due to the absence of down-stream processing, and easier and fewer purification steps.…”

Section: Introductionmentioning

confidence: 99%

Optimized lipase-catalyzed synthesis of adipate ester in a solvent-free system

Chaibakhsh

Rahman

Abd‐Aziz³

et al. 2009

J Ind Microbiol Biotechnol

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Immobilized Candida antarctica lipase-catalyzed esterification of adipic acid and oleyl alcohol was investigated in a solvent-free system (SFS). Optimum conditions for adipate ester synthesis in a stirred-tank reactor were determined by the response surface methodology (RSM) approach with respect to important reaction parameters including time, temperature, agitation speed, and amount of enzyme. A high conversion yield was achieved using low enzyme amounts of 2.5% w/w at 60 degrees C, reaction time of 438 min, and agitation speed of 500 rpm. The good correlation between predicted value (96.0%) and actual value (95.5%) implies that the model derived from RSM allows better understanding of the effect of important reaction parameters on the lipase-catalyzed synthesis of adipate ester in an organic solvent-free system. Higher volumetric productivity compared to a solvent-based system was also offered by SFS. The results demonstrate that the solvent-free system is efficient for enzymatic synthesis of adipate ester.

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“…To do this, it is very important to use a rational experimental design to effectively detect the possible interaction in all concentration range of two components, pesticide and IL. Central composite design (CCD) is one of the most useful response surface exploration method, and widely used in the optimization of many procedures [15][16][17][18][19]. CCD derived from the (n × n) design can almost cover any possible combinations.…”

Section: Introductionmentioning

confidence: 99%

Effect of ionic liquid on the toxicity of pesticide to Vibrio-qinghaiensis sp.-Q67

Zhang

Liu

2009

Journal of Hazardous Materials

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Lipase‐catalyzed ethanolysis of soybean oil in a solvent‐free system using central composite design and response surface methodology

Cited by 43 publications

References 12 publications

Structural insights into methanol-stable variants of lipase T6 from Geobacillus stearothermophilus

Structural insights into methanol-stable variants of lipase T6 from Geobacillus stearothermophilus

Optimized lipase-catalyzed synthesis of adipate ester in a solvent-free system

Effect of ionic liquid on the toxicity of pesticide to Vibrio-qinghaiensis sp.-Q67

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