Improving reuse cycles of <i>Thermomyces lanuginosus</i> lipase (NS-40116) by immobilization in flexible polyurethane

Facin, Bruno R.; Valério, Alexsandra; Bresolin, Daniela; Centenaro, Giselle; Oliveira, Débora de; Oliveira, J. Vladimir

doi:10.1080/10242422.2018.1458842

Cited by 27 publications

(16 citation statements)

References 36 publications

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“…In terms of "enzymatic biodiesel," most of researches consider the application of lipases immobilized at different supports as catalysts of the reaction justified by a higher operational stability of the enzyme and possibility of the biocatalyst to be recovered and reutilized in the process [25][26][27]. However, recently published researches has demonstrated the great potential that lipases in liquid (or soluble or also free) formulation have in catalyzing the biodiesel synthesis [28][29][30][31][32].…”

Section: Introductionmentioning

confidence: 99%

Lipases in liquid formulation for biodiesel production: Current status and challenges

Wancura

Tres

Jahn

et al. 2019

Biotech and App Biochem

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Enzymatic synthesis of biodiesel showed advantageous characteristics in relation to other technologies once it works under bland conditions, no generation of wastewater, no occurrence of saponifications reactions and production of a biodiesel with high quality. Although many researches still apply immobilized lipases, the high costs associated with this biocatalyst hamper the economic viability of the process. Lipases in free/soluble/liquid formulation employed to biodiesel production via hydroesterification reaction have attracted interest from researchers because they are more cost effective than the immobilized form, making the enzymatic route more competitive. In addition, soluble lipases present higher reaction rates, reducing the time required to obtain a satisfactory biodiesel yield. Despite the fact that already exist industrial plants producing biodiesel with the assistance of lipases in liquid formulation, results of researches show that the process still needs to overcome some drawbacks. This paper is a comprehensive and critical discussion on the publications where soluble lipases were applied on biodiesel synthesis, as well as the challenges that the technology faces and its current status in pilot and industrial applications.

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Section: Introductionmentioning

confidence: 99%

Lipases in liquid formulation for biodiesel production: Current status and challenges

Wancura

Tres

Jahn

et al. 2019

Biotech and App Biochem

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“…An interesting lipase was isolated from T. lanuginosus that is both heat and organic solvent resistant (lipase NS-40116). The optimal temperature for this lipase is 60 °C; enzyme maintained at 60 °C for under 24 h retains 90% of its activity ( Facin et al, 2018 ). A thermophilic lipase from Burkholderia ubonensis SL-4, has an optimal temperature at 65 °C, and maintains good stability when held at 50–55 °C ( Yang et al, 2016 ).…”

Section: Identification Of Lipase Activity In Microorganisms and Analysis Of Its Enzymatic Propertiesmentioning

confidence: 99%

“…The optimum pH of a solvent-resistant lipase from Micrococcus luteus EMP48-D was 5.0; enzyme activity significantly decreased up to pH 6.0 and reducing continuously from pH 6.0 to pH 10.0, although was more than 85% of the initial activity of LipEMP48-D after incubation for 120 min at 40 °C ( Adina et al, 2021 ). The heat and organic solvent-resistant lipase NS-40116 from T. lanuginosus displays highest activity at pH = 7.0 and maintains stability between pH 5.0–9.0 ( Facin et al, 2018 ). Another lipase from T. lanuginosus exhibits an optimum pH of 8.5, although high activity is maintained within the pH range of 8.0–10.0 ( Kumar et al, 2019 ).…”

Section: Identification Of Lipase Activity In Microorganisms and Analysis Of Its Enzymatic Propertiesmentioning

confidence: 99%

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Yao

Liu

et al. 2021

Front. Microbiol.

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As a powerful factory, microbial cells produce a variety of enzymes, such as lipase. Lipase has a wide range of actions and participates in multiple reactions, and they can catalyze the hydrolysis of triacylglycerol into its component free fatty acids and glycerol backbone. Lipase exists widely in nature, most prominently in plants, animals and microorganisms, among which microorganisms are the most important source of lipase. Microbial lipases have been adapted for numerous industrial applications due to their substrate specificity, heterogeneous patterns of expression and versatility (i.e., capacity to catalyze reactions at the extremes of pH and temperature as well as in the presence of metal ions and organic solvents). Now they have been introduced into applications involving the production and processing of food, pharmaceutics, paper making, detergents, biodiesel fuels, and so on. In this mini-review, we will focus on the most up-to-date research on microbial lipases and their commercial and industrial applications. We will also discuss and predict future applications of these important technologies.

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“…posits of reaction product accumulated on the matrix surfaces, which in turn causing mass transfer restrictions to the protein molecules 36 . Interestingly, catalytic activity above 50 after five cylces of reuse was retained, when TLL was immobilized onto the polyurethane foam PU by entrapment 37 . The present immobilized TLL samples could be used for preparation of monoacylglycerols and diacylglycerols through glycerolysis.…”

Section: Reusability Of the Immobilized Tllmentioning

confidence: 99%

Organic Modifications of SBA-15 Improves the Enzymatic Properties of its Supported TLL

Zhao

Zhong

2020

J. Oleo Sci.

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In this study, lipase from Thermomyces lanuginosus (TLL) was immobilized onto the parent and organic groups modified SBA-15, and the enzymatic properties of the obtained immobilized TLL samples were investigated. 1) Activity of SBA-15-TLL at 2862.78 ± 293.24 U/g was obtained. 2) Most of the organic groups modification favored a great improvement in activity, and higher activity over 12000 U/g was observed for N-phenylaminomethyl and phenyl group modification. 3) Most of the supported TLL showed better thermostability in air while poor in phosphate buffer, with over 80% vers less than 20% of their initial activity retained after 4 h incubation at 70℃. 4) The n-dodecyl, phenyl and N-phenylaminomethyl group functionalization decreased the sensitivity of immobilized TLL in extreme pH values. 5) The n-octyl and 2-(propoxymethyl)oxirane group modification confered the supported TLL good reusability, and over 60% of their initial activity was retained after five successive cycles of reuse.

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Improving reuse cycles of Thermomyces lanuginosus lipase (NS-40116) by immobilization in flexible polyurethane

Cited by 27 publications

References 36 publications

Lipases in liquid formulation for biodiesel production: Current status and challenges

Lipases in liquid formulation for biodiesel production: Current status and challenges

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Organic Modifications of SBA-15 Improves the Enzymatic Properties of its Supported TLL

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