Synthetic resin-bound truncated Candida antarctica lipase B for production of fatty acid alkyl esters by transesterification of corn and soybean oils with ethanol or butanol

Hughes, Stephen R.; Moser, Bryan R.; Robinson, Samantha; Cox, Elby J.; Harmsen, Amanda J.; Friesen, Jon A.; Bischoff, Kenneth M.; Jones, Marjorie A.; Pinkelman, Rebecca; Bang, S.; Tasaki, Ken; Doll, Kenneth M.; Qureshi, Nasib; Liu, Siqing; Saha, Badal C.; Jackson, John S.; Cotta, Michael A.; Rich, Joseph O.; Caimi, Paolo

doi:10.1016/j.jbiotec.2012.01.025

Cited by 8 publications

(4 citation statements)

References 33 publications

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“…lipase (Mander et al 2012), transesterification of corn and soybean oils with ethanol and butanol by synthetic resin-bound truncated C. antarctica lipase (Hughes et al 2012), and transesterification of palm oil by whole cells of Rhodotorulla mucilagenosa (Srimhan et al 2011) have also been recorded. Such lipasemediated transesterification reactions are useful in biodiesel production from vegetable oils.…”

Section: Applications Of Lipasesmentioning

confidence: 93%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

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Lipases are serine hydrolases that catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids, by acting at the oil-water interface. Lipases from microbial sources have received heightened attention for an array of industrial applications, and these enzymes have been well exploited in the environmental sector as well. In this article, we present an overview of microbial lipase, including the microorganisms from which it could be produced; the application of recombinant DNA technology tools to produce lipase with enhanced properties, the effective use of waste materials as substrates for lipase production; the usage of statistical tools to efficiently optimize the production medium; lipase purification strategies; and the immobilization of the enzyme on a variety of support materials. The next section of the article provides a gist of its application in diversified spheres and focusses exclusively on the environmentally relevant ones. Lipasecatalyzed esterification, transesterification, and interesterification reactions, an emerging area of green chemistry; lipase-mediated in vitro biopolymer synthesis and degradation; and the application of lipase for remediating fat and oil constituents in wastewater are dealt with in-depth. When its full potential is harnessed, the enzyme could play a pivotal role in environmental management.

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Section: Applications Of Lipasesmentioning

confidence: 93%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

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“…Both the purified CALB Lyt-1 immobilized on a resin support and the intact yeast cells expressing CALB Lyt-1 had specific activities greater than Novozym 435 (80 and 160 µg FAEEs/mg lipase versus 40 µg FAEEs/mg lipase, respectively). With the same approach, Hughes and coworkers [ 211 ] obtained a truncated variant of CALB that lacked the initial 34 amino-acid residues. This truncated CALB, once expressed and purified from P. pastoris , was immobilized on a resin support and tested for biodiesel production from corn and soybean oils, and it was shown to have a specific activity 36% and 50% higher, respectively, than Novozym 435.…”

Section: Industrial Applications Of Recombinant Lipases and Phosphmentioning

confidence: 99%

Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications

Borrelli

Trono

2015

IJMS

287

182

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Lipases and phospholipases are interfacial enzymes that hydrolyze hydrophobic ester linkages of triacylglycerols and phospholipids, respectively. In addition to their role as esterases, these enzymes catalyze a plethora of other reactions; indeed, lipases also catalyze esterification, transesterification and interesterification reactions, and phospholipases also show acyltransferase, transacylase and transphosphatidylation activities. Thus, lipases and phospholipases represent versatile biocatalysts that are widely used in various industrial applications, such as for biodiesels, food, nutraceuticals, oil degumming and detergents; minor applications also include bioremediation, agriculture, cosmetics, leather and paper industries. These enzymes are ubiquitous in most living organisms, across animals, plants, yeasts, fungi and bacteria. For their greater availability and their ease of production, microbial lipases and phospholipases are preferred to those derived from animals and plants. Nevertheless, traditional purification strategies from microbe cultures have a number of disadvantages, which include non-reproducibility and low yields. Moreover, native microbial enzymes are not always suitable for biocatalytic processes. The development of molecular techniques for the production of recombinant heterologous proteins in a host system has overcome these constraints, as this allows high-level protein expression and production of new redesigned enzymes with improved catalytic properties. These can meet the requirements of specific industrial process better than the native enzymes. The purpose of this review is to give an overview of the structural and functional features of lipases and phospholipases, to describe the recent advances in optimization of the production of recombinant lipases and phospholipases, and to summarize the information available relating to their major applications in industrial processes.

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“…antarctica [131], Y. lipolytica [132] and R. oryzae [133] have been expressed in S. cerevisiae. P. pastoris has been used for expression of lipases from R. miehei [134], R. oryzae [135 , 136, 137], a chimera from R. oryzae and R. chinesis [120] and P. cyclopium [138].…”

Section: Heterologous Expression Of Lipasesmentioning

confidence: 99%

Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

Sandoval

Casas-Godoy

Bonet-Ragel

et al. 2017

CBE

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Biodiesel represents an interesting alternative to fossil fuels. Traditionally the standard method for biodiesel production from oils is alkaline-catalyzed transesterification. Chemical catalysis can be replaced by enzymatic catalysis using lipases (EC 3.1.1.3, triacylglycerol acyl hydrolases), obtained from plants, animals or microorganisms. These biocatalysts act at milder temperature and normal pressure conditions, resulting in lower energy consumption. Also, undesirable side-reactions do not occur, originating pure products. Refined vegetable oils are the most common feedstocks for biodiesel production, accounting for 70-80% of the overall biodiesel production costs. The search for low-cost feedstocks, i.e. non-edible oils and high acidic waste oils/greases, is an alternative to make biodiesel competitive. Non-regioselective and sn-1,3regioselective lipases can catalyze esterification of free fatty acids and transesterification of triacylglycerols with good yields. The lipases used as catalysts for biodiesel production must present alcohol resistance, thermo-tolerance, high stability and activity. Recently, enzymatic processes for biodiesel production have been implemented at industrial scale. Despite this trend, the conventional chemical process still remains the most popular, mainly due to the high cost of commercial lipases. This review consists of an update of the state of the art of enzymatic biodiesel production, including legislation, feedstocks, lipases used for biodiesel synthesis, the role of acyl acceptors and strategies to avoid lipase inactivation, the mechanisms proposed for biocatalysis and the enzymatic bioreactors used. In addition, the economics of the bioprocess is also presented.

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Synthetic resin-bound truncated Candida antarctica lipase B for production of fatty acid alkyl esters by transesterification of corn and soybean oils with ethanol or butanol

Cited by 8 publications

References 33 publications

An insight into microbial lipases and their environmental facet

An insight into microbial lipases and their environmental facet

Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications

Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

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