Improved esterification activity of Candida rugosa lipase in organic solvent by immobilization as Cross-linked enzyme aggregates (CLEAs)

Kartal, Funda; Janssen, Michiel H. A.; Hollmann, Frank; Sheldon, Roger A.; Kilinc, Ali

doi:10.1016/j.molcatb.2011.04.002

Cited by 120 publications

(84 citation statements)

References 25 publications

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“…Final The phenomenon of interfacial activation of lipases by additives such as surfactants, crown ethers or amines is well documented [27,35] and generally ascribed to the lipase adopting a more active conformation under these conditions. On preparing Lipex CLEAs, most of the tested compounds produced a negative effect with the exception of Tween 80, which had 129.7% retained activity as compared to the free (native) enzyme, and 150.3% retained activity as compared to the Lipex CLEAs prepared without surfactant.…”

Section: Compoundmentioning

confidence: 99%

Stabilization of a Lipolytic Enzyme for Commercial Application

Rose¹,

Novak²,

Dowd³

et al. 2017

Catalysts

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Thermomyces lanouginosa lipase has been used to develop improved methods for carrier-free immobilization, the Cross-Linked Enzyme Aggregates (CLEAs), for its application in detergent products. An activator step has been introduced to the CLEAs preparation process with the addition of Tween 80 as activator molecule, in order to obtain a higher number of the individual lipase molecules in the "open lid" conformation prior to the cross-linking step. A terminator step has been introduced to quench the cross-linking reaction at an optimal time by treatment with an amine buffer in order to obtain smaller and more homogenous cross-linked particles. This improved immobilization method has been compared to a commercially available enzyme and has been shown to be made up of smaller and more homogenous particles with an average diameter of 1.85 ± 0.28 µm which are 129.7% more active than the free enzyme. The CLEAs produced show improved features for commercial applications such as an improved wash performance comparable with the free enzyme, improved stability to proteolysis and a higher activity after long-term storage.

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Section: Compoundmentioning

confidence: 99%

Stabilization of a Lipolytic Enzyme for Commercial Application

Rose¹,

Novak²,

Dowd³

et al. 2017

Catalysts

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“…Therefore, the conversion rate of the ester declined soon after 8 h of reaction time for the free CRL. It has also been reported that aggregation of the free enzyme with the substrate and product may cause inappropriate distribution of the enzyme and reactants that may alter the reaction equilibrium in favor of hydrolysis [45]. …”

Section: Effect Of Timementioning

confidence: 99%

Candida rugosa Lipase Immobilized onto Acid-Functionalized Multi-walled Carbon Nanotubes for Sustainable Production of Methyl Oleate

Marzuki

Mahat

Huyop

et al. 2015

Appl Biochem Biotechnol

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The chemical production of methyl oleate using chemically synthesized fatty acid alcohols and other toxic chemicals may lead to significant environmental hazards to mankind. Being a highly valuable fatty acid replacement raw material in oleochemical industry, the mass production of methyl oleate via environmentally favorable processes is of concern. In this context, an alternative technique utilizing Candida rugosa lipase (CRL) physically adsorbed on multi-walled carbon nanotubes (MWCNTs) has been suggested. In this study, the acid-functionalized MWCNTs prepared using a mixture of HNO3 and H2SO4 (1:3 v/v) was used as support for immobilizing CRL onto MWCNTs (CRL-MWCNTs) as biocatalysts. Enzymatic esterification was performed and the efficiency of CRL-MWCNTs was evaluated against the free CRL under varying conditions, viz. temperature, molar ratio of acid/alcohol, solvent log P, and enzyme loading. The CRL-MWCNTs resulted in 30-110 % improvement in the production of methyl oleate over the free CRL. The CRL-MWCNTs attained its highest yield (84.17 %) at 50 °C, molar ratio of acid/alcohol of 1:3, 3 mg/mL of enzyme loading, and iso-octane (log P 4.5) as solvent. Consequently, physical adsorption of CRL onto acid-functionalized MWCNTs has improved the activity and stability of CRL and hence provides an environmentally friendly means for the production of methyl oleate.

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“…1,7,13 Cross-linking is a reaction; therefore, the time required to obtain the maximum λ is very important. 32 The MCLLAs of YLL were prepared using varying cross-linking times (4,8,12,20, and 24 h). The results (presented in Fig.…”

Section: Nature and Amount Of The Cross-linking Agent Andmentioning

confidence: 99%

Novel Magnetic Cross‐Linked Lipase Aggregates for Improving the Resolution of (R, S)‐2‐octanol

2014

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Novel magnetic cross-linked lipase aggregates were fabricated by immobilizing the cross-linked lipase aggregates onto magnetic particles with a high number of -NH2 terminal groups using p-benzoquinone as the cross-linking agent. At the optimal fabrication conditions, 100% of immobilization efficiency and 139% of activity recovery of the magnetic cross-linked lipase aggregates were achieved. The magnetic cross-linked lipase aggregates were able to efficiently resolve (R, S)-2-octanol, and retained 100% activity and 100% enantioselectivity after 10 cycles of reuse, whereas the cross-linked lipase aggregates only retained about 50% activity and 70% enantioselectivity due to insufficient cross-linking. These results provide a great potential for industrial applications of the magnetic cross-linked lipase aggregates.

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Improved esterification activity of Candida rugosa lipase in organic solvent by immobilization as Cross-linked enzyme aggregates (CLEAs)

Cited by 120 publications

References 25 publications

Stabilization of a Lipolytic Enzyme for Commercial Application

Stabilization of a Lipolytic Enzyme for Commercial Application

Candida rugosa Lipase Immobilized onto Acid-Functionalized Multi-walled Carbon Nanotubes for Sustainable Production of Methyl Oleate

Novel Magnetic Cross‐Linked Lipase Aggregates for Improving the Resolution of (R, S)‐2‐octanol

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