Biodiesel production catalyzed by Rhizomucor miehei lipase-displaying Pichia pastoris whole cells in an isooctane system

Huang, Di; Han, Sang‐Ik; Han, Zhenlin; Lin, Ying

doi:10.1016/j.bej.2010.08.009

Cited by 87 publications

(32 citation statements)

References 23 publications

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“…Lipases has been successfully applied in various applications, such as in the food industry, organic synthesis, pharmaceutical (Houde et al 2004;Diego et al 2009) and in the field of biodiesel (Huang et al 2012;Huang et al 2014). The success is challenging us to keep looking for a better lipase expression with the aid of genetic engineering.…”

Section: Discussionmentioning

confidence: 99%

“…R. miehei is a mold that has lipase with high activity and good stability under diverse conditions (Rodrigues and Lafuente 2010). Lipase of R. miehei has been used in in ester hydrolysis, ester synthesis, and transesterification reaction (Huang et al 2012). These lipase was able to successfully catalyze the synthesis of ethyl caproate in organic solvent displayed on the surface Pichia pastoris (Han et al 2009), and also effective for the Lipase (EC 3.1.1.3) is classified as hydrolase that hydrolyzes lipids.…”

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confidence: 99%

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Cloning of Synthetic Lipase Gene from Rhizomucor miehei with Original Signal Peptide in Pichia pastoris

Cahyani¹,

Helianti²,

Nurhayati³

et al. 2017

Microbiol Indones

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Lipases (EC 3.1.1.3) are classified as hydrolases that hydrolyze lipids. These enzymes have potential application in biotechnology and industrial process. In previous study we have cloned the synthetic Rhizomucor miehei lipase gene using the vector pUC57 in Escherichia coli DH5α, but only found the very low enzymes activity. This study aimed to clone synthetic Rhizomucor miehei lipase gene into Pichia pastoris expression plasmid for lipase expression with the original signal peptide. A DNA fragment with the original signal peptide had been obtained by PCR, cut by Xho I and Xba I and then ligated into pPICZα A linearized with the same enzymes. The mixture of ligation reaction, then was transformed into Escherichia coli DH5α. Zeocin-resistant transformants were selected and contained plasmid was analyzed by restriction enzymes analyses and DNA sequencing. As the result, a synthetic Rhizomucor miehei lipase gene (RMlip) with the size of 1132 bp was successfully cloned to pPICZα A vector plasmid. The recombinant plasmid with the correct DNA sequence was transformed into Pichia pastoris X33. Cultivation of recombinant P. pastoris was carried out with the addition of 1.5% methanol every day with appropriate aeration. The recombinant lipase produced by Pichia pastoris X33 o containing RMlip in its chromosomal DNA had optimal temperature and pH, 30 C and 9.0, respectively.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Cloning of Synthetic Lipase Gene from Rhizomucor miehei with Original Signal Peptide in Pichia pastoris

Cahyani¹,

Helianti²,

Nurhayati³

et al. 2017

Microbiol Indones

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“…Yeasts are another attractive host strains for cellsurface display systems due to their safety, ease of highcell density cultivation and the capability of eukaryotic proteins folding and glycosylation (Gai, 2007).These properties make enzyme displayed yeast be of great value in biocatalytic process, especially in the industrial production using displaying yeast as whole-cell biocatalysts (Huang et al, 2012;Tanino, 2009). Yeasts are abundant in habitats in which carbohydrates are present, such as fruits, flowers and tree bark (Kurtzman and Fell, 1998).…”

Section: Troductionmentioning

confidence: 99%

Effect of pH and temperature on the production and activity of Schwanniomyces polymorphus extracellular proteases in fermentation medium

Alexander¹,

Cleiton²,

Dangely³

et al. 2015

Afr. J. Microbiol. Res.

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“…The transesterification of triglycerides provides an environmentally more attractive option compared to the conventional process. The advantages related to this technique are less energy-intensive, ease of recovery of glycerol and production of high concentrations of free fatty acids [6,7].…”

Section: Introductionmentioning

confidence: 99%

Selection of Strains Producing Lipase with Transesterification Activity and Its Characterization

Castiglioni¹,

Costa²,

Padilha³

et al. 2016

JCCE

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Abstract:The interest for lipase production is due to the ability of this enzyme to catalyze some reactions, such as the transesterification. Although industrial biodiesel is produced chemically, there are several problems associated with this technology that can be prevented through the use of lipases. The present work aimed to select microorganisms with potential for production of lipase with transesterification activity. The lipase from Burkholderia cepacia was the one with the most promising results for this type of reaction, showing results of hydrolytic activity at 37 °C and pH 8.0. The pH and volume of crude enzyme extract that showed favorable for synthesis of biodiesel is at about pH 6.0 and 3.75 mL, respectively, which represents approximately 42% of water in the system, ensuring the conversion of nearly 60% to biodiesel.

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Biodiesel production catalyzed by Rhizomucor miehei lipase-displaying Pichia pastoris whole cells in an isooctane system

Cited by 87 publications

References 23 publications

Cloning of Synthetic Lipase Gene from Rhizomucor miehei with Original Signal Peptide in Pichia pastoris

Cloning of Synthetic Lipase Gene from Rhizomucor miehei with Original Signal Peptide in Pichia pastoris

Effect of pH and temperature on the production and activity of Schwanniomyces polymorphus extracellular proteases in fermentation medium

Selection of Strains Producing Lipase with Transesterification Activity and Its Characterization

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