Improving catalytic performance of Burkholderia cepacia lipase immobilized on macroporous resin NKA

Liu, Tao; Liu, Yun; Li, Qin; Wang, Junkai; Yan, Yunjun

doi:10.1016/j.molcatb.2011.03.007

Cited by 87 publications

(63 citation statements)

References 25 publications

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“…In this way, the immobilized's operational stability was evaluated in multiple operating cycles on hydrolytic reactions. The immobilized lipase showed a residual activity of 32%, relative to 93.33 U g The results obtained from the current study are similar to those from previous reports in the literature by Jegannathan et al (2009) and Liu et al (2011). The immobilization efficiency can be determined by the possibility of recovery, use, and reuse in continuous biocatalytic processes.…”

Section: Operational Stabilitysupporting

confidence: 88%

“…for the free and immobilized forms, respectively. This trend suggests the presence of two reaction mechanisms (hydrolyses and esterification), both linked to lipases (Liu & Chang, 2008, Liu et al, 2011. Initially, there is a predominance of hydrolyses reaction on the first reaction minutes, which generates alcohol and carboxylic acid as products.…”

Section: Study Of the Reaction Timementioning

confidence: 98%

“…In this context, we highlight the enzymatic treatments that correspond to the most recent technology for the biological treatment of effluents (Buss & Henkes, 2014, Silva, Silva, Gois, Almeida, & Abud, 2015 by hydrolytic method reduce the concentration and degrade a large number of toxic and persistent substances (Liu et al, 2011, Baldo et al, 2013, Chen, Zhang, Xu, & Yan, 2013, Zadinelo et al, 2013. The use of immobilized lipase on a suitable support increases the process financial viability, mainly due to its reuse (reaction medium separation), it improves the thermal and mechanical properties (stability at different temperatures), operational stability, storage and the enzymatic activity (Cadena et al 2010, Hu et al, 2012, Palomino-Romero et al, 2012, Colla et al, 2014, Manoel et al, 2015, Nyari, Zeni, Steffens, Dallago, & Rigo, 2015, Shao, Jing, Tian, Zheng, & Shang, 2015, Nyari et al, 2016.…”

Section: Introductionmentioning

confidence: 99%

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Optimization of olive oil hydrolysis process using immobilized Lipase from Burkholderia cepacia sp. in Polyurethane

et al. 2017

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ABSTRACT. The aim of this study was to achieve the best conditions for the olive oil hydrolysis process at optimal pH and temperature using Burkholderia cepacia lipase immobilized in situ in rigid polyurethane support. The influences of the temperature (13.85 to 56.5ºC) and pH (4.18 to 9.82) were evaluated by a central composite rotational experimental design 2 2 . The operational stability and storage conditions were also studied. The olive oil hydrolysis process was optimized in pH 7.0, at 40°C and 15 min of reaction, with 66 and 93 U g -1 of hydrolysis activity in free and immobilized lipase, respectively, with > 700% yield. The immobilized remained stable for up to 40 days of storage at temperatures of 60 o C, and for 100 days from 4 to 25°C. The operational stability of the immobilized was 6 continuous cycles. In this way, immobilization showed to be a promising alternative for its application in olive oil hydrolysis, having storage stability and reuse capability. Otimização do processo de hidrólise do azeite de oliva utilizando lipase Burkholderia cepacia sp. imobilizada em poliuretano RESUMO. As lipases são enzimas que, naturalmente, atuam na hidrólise de óleos e gorduras, porém, em meios com quantidade baixa de água, são capazes de atuar em reações como a esterificação, alcoólise, acidólise, aminólise, entre outras. Sendo utilizadas na redução da concentração dos lipídios contidos nos efluentes, promovendo a hidrólise dos óleos e gorduras presentes. Sendo assim, o objetivo do presente estudo foi obter as melhores condições do processo de hidrólise do óleo de oliva em termos de pH e temperatura, utilizando lipase de Burkholderia cepacia imobilizada in situ em suporte rígido de poliuretano. O processo de hidrólise do óleo de oliva foi obtido utilizando as condições de pH de 7,0, temperatura de 40°C e 15 min de reação com atividade hidrolítica para a enzima livre e imobilizada de 66 e 93 U g -1 respectivamente, com rendimento de > 700%. O imobilizado apresentou estabilidade de 40 dias de estocagem nas temperaturas de 60ºC e 100 dias de armazenamento nas temperaturas entre -4 a 25ºC e a estabilidade operacional de 6 ciclos contínuos. O imobilizado se mostrou uma alternativa promissora para aplicação no processo de hidrólise frente à enzima livre, tendo estabilidade de estocagem e possibilidade de reutilização operacional.Palavras-chaves: biocatálise, lipase, imobilização in situ, poliuretano, hidrólise.

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Section: Operational Stabilitysupporting

confidence: 88%

Section: Study Of the Reaction Timementioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Optimization of olive oil hydrolysis process using immobilized Lipase from Burkholderia cepacia sp. in Polyurethane

et al. 2017

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“…Among them, Burkholderia cepacia lipase (BCL) is a versatile one and has been widely used in organic synthesis, biodiesel preparation, biodegradation and many other reactions in aqueous and non-aqueous phases [3][4][5]. Recently, enzymatic chiral resolution by lipases has generated huge interest due to the merits of it having fewer byproducts, a simple operation and environmental friendliness [6,7].…”

Section: Introductionmentioning

confidence: 99%

“…Recently, enzymatic chiral resolution by lipases has generated huge interest due to the merits of it having fewer byproducts, a simple operation and environmental friendliness [6,7]. However, the freeform lipases generally exhibit low stability, poor recyclability and non-reusability [3,8], especially low enzyme activity in non-aqueous phase reaction. These demerits were also reflected in the freeform BCL in our previous studies [3,9].…”

Section: Introductionmentioning

confidence: 99%

Immobilized Burkholderia cepacia Lipase on pH-Responsive Pullulan Derivatives with Improved Enantioselectivity in Chiral Resolution

Cui

et al. 2018

Catalysts

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Abstract:A kind of pH-responsive particle was synthesized using modified pullulan polysaccharide. The synthesized particle possessed a series of merits, such as good dispersity, chemical stability and variability of particle size, making it a suitable carrier for enzyme immobilization. Then, Burkholderia cepacia lipase (BCL), a promising biocatalyst in transesterification reaction, was immobilized on the synthesized particle. The highest catalytic activity and immobilization efficiency were achieved at pH 6.5 because the particle size was obviously enlarged and correspondingly the adsorption surface for BCL was significantly increased. The immobilization enzyme loading was further optimized, and the derivative lipase was applied in chiral resolution. Under the optimal reaction conditions, the immobilized BCL showed a very good performance and significantly shortened the reaction equilibrium time from 30 h of the free lipase to 2 h with a conversion rate of 50.0% and ee s at 99.2%. The immobilized lipase also exhibited good operational stability; after being used for 10 cycles, it still retained over 80% of its original activity. Moreover, it could keep more than 80% activity after storage for 20 days at room temperature in a dry environment. In addition, to learn the potential mechanism, the morphology of the particles and the immobilized lipase were both characterized with a scanning electron microscope and confocal laser scanning microscopy. It was found that the enlarged spherical surface of the particle in low pH values probably led to high immobilized efficiency, resulting in the improvement of enantioselectivity activity in chiral resolution.

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Application of Ionic Liquids in Biocatalysis and Biotechnology

Elimian,

Ajibade,

Ajibade

et al. 2023

Handbook of Ionic Liquids

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Improving catalytic performance of Burkholderia cepacia lipase immobilized on macroporous resin NKA

Cited by 87 publications

References 25 publications

<b>Optimization of olive oil hydrolysis process using immobilized Lipase from <i>Burkholderia cepacia</i> sp. in Polyurethane

<b>Optimization of olive oil hydrolysis process using immobilized Lipase from <i>Burkholderia cepacia</i> sp. in Polyurethane

Immobilized Burkholderia cepacia Lipase on pH-Responsive Pullulan Derivatives with Improved Enantioselectivity in Chiral Resolution

Application of Ionic Liquids in Biocatalysis and Biotechnology

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