Improving Catalytic Performance of Burkholderiacepacia Lipase by Chemical Modification with Functional Ionic Liquids

Xu, Chao; Xuhan, Yin; Zhang, Chuan; Chen, Hongyue; Huang, He; Hu, Yi

doi:10.1007/s40242-018-7246-7

Cited by 10 publications

(8 citation statements)

References 44 publications

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“…In contrast, all the modified enzymes exhibited good DMSO tolerance, with a DMSO volume fraction of 10% resulting in a maximum increase in enzyme activity. [BetaineC 16 ][H 2 PO 4 ]-CALB retained 55% of its initial enzyme activity in 50% DMSO, which differs from the response previously reported for Burkholderia cepacia lipase (BCL) modified using imidazolium choline ionic liquid, in which rapid deactivation of the modified enzyme was observed in 30% DMSO, further demonstrated the superiority of long chain alkylated betaine ionic liquids as lipase modifiers (Xu et al, 2018). As shown in Figure 5B, the tolerance of native and modified enzymes to organic solvents were also assessed using different concentrations of mercaptoethanol (0-30% v/v).…”

Section: Organic Solvent and Denaturing Agents Tolerance Of Native An...contrasting

confidence: 73%

Enhancing the Catalytic Performance of Candida antarctica Lipase B by Chemical Modification With Alkylated Betaine Ionic Liquids

Xue

Zhang

et al. 2022

Front. Bioeng. Biotechnol.

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Various betaine ionic liquids composed of different chain lengths and different anions were designed and synthesized to modify Candida antarctica lipase B (CALB). The results showed that the catalytic activity of all modified lipases improved under different temperature and pH conditions, while also exhibiting enhanced thermostability and tolerance to organic solvents. With an increase in ionic liquid chain length, the modification effect was greater. Overall, CALB modified by [BetaineC16][H2PO4] performed best, with the modified CALB enzyme activity increased 3-fold, thermal stability increased 1.5-fold when stored at 70°C for 30 min, with tolerance increased 2.9-fold in 50% DMSO and 2.3-fold in 30% mercaptoethanol. Fluorescence and circular dichroism (CD) spectroscopic analysis showed that the introduction of an ionic liquid caused changes in the microenvironment surrounding some fluorescent groups and the secondary structure of the CALB enzyme protein. In order to establish the enzyme activity and stability change mechanisms of the modified CALB, the structures of CALB modified with [BetaineC4][Cl] and [BetaineC16][Cl] were constructed, while the reaction mechanisms were studied by molecular dynamics simulations. Results showed that the root mean square deviation (RMSD) and total energy of modified CALB were less than those of native CALB, indicating that modified CALB has a more stable structure. Root mean square fluctuation (RMSF) calculations showed that the rigidity of modified CALB was enhanced. Solvent accessibility area (SASA) calculations exhibited that both the hydrophilicity and hydrophobicity of the modified enzyme-proteins were improved. The increase in radial distribution function (RDF) of water molecules confirmed that the number of water molecules around the active sites also increased. Therefore, modified CALB has enhanced structural stability and higher hydrolytic activity.

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Section: Organic Solvent and Denaturing Agents Tolerance Of Native An...contrasting

confidence: 73%

Enhancing the Catalytic Performance of Candida antarctica Lipase B by Chemical Modification With Alkylated Betaine Ionic Liquids

Xue

Zhang

et al. 2022

Front. Bioeng. Biotechnol.

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“…Xu and coworkers grafted imidazolium and choline-based ionic liquid (IL) onto lipase from Burkholderia cepacia. [65] The authors observed a 1.2-fold increase in the lipases' relative activity and 1.4-fold in its thermostability, compared to the native enzyme. [65] Jayawardena et al [66] used benzoic anhydride for the modification of lipase from C. antarctica A and greasex from Humicola lanuginosa.…”

Section: Modification Of Lipases With Small Moleculesmentioning

confidence: 96%

“…Xu and coworkers grafted imidazolium and choline‐based ionic liquid (IL) onto lipase from Burkholderia cepacia . [ 65 ] The authors observed a 1.2‐fold increase in the lipases’ relative activity and 1.4‐fold in its thermostability, compared to the native enzyme. [ 65 ]…”

Section: Improvement Of Lipases’ Propertiesmentioning

confidence: 99%

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Chemical modification of lipases: A powerful tool for activity improvement

Noro

Cavaco‐Paulo

Silva

2022

Biotechnology Journal

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The demand for adequate and ecologically acceptable procedures to produce the most differentiated products has been growing in recent decades, with enzymes being excellent examples of the advances achieved so far. Lipases are astonishing catalysts with a vast range of applications including the synthesis of esters, flavors, biodiesel, and polymers. The broad specificity of the substrates, as well as the regio-, stereo-, and enantioselectivity, are the differentiating factors of these enzymes. Structural modification is a current approach to enhance the activity of lipases. Chemical modification of lipases to improve catalytic performance is of great interest considering the increasingly broad fields of application. Together with the physical immobilization onto solid supports, different strategies have been developed to produce catalysts with higher activity and stability. In this review, practical insights into the different strategies developed in recent years regarding the modification of lipases are described. For the first time, the impact of the modifications on the activity and stability of lipases, as well as on the biotechnological applications, is fully compiled.

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“…Then, 1.5 mmol EDC and 1.5 mmol NHS were added into the system, mixed by ultrasound for 15 s, then reacted at 37°C for 30 min to obtain the activated modification agent for CRL. 12 Additionally, 400 mg of CRL was dissolved in 8 mL of phosphate buffer (pH 7.0). Then the earlier solution was centrifuged at 3354 × g for 10 min at 4°C, the supernatant was collected, and then dialyzed for 24 h. The purified lipase concentration was adjusted to 4 mg protein mL −1 .…”

Section: Preparation Of Immobilized Crlmentioning

confidence: 99%

Lipase nanogel catalyzed synthesis of vitamin E succinate in non‐aqueous phase

et al. 2020

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BACKGROUND: In order to improve the stability of vitamin E and broaden its scope of application, an effective solution is to convert vitamin E into its derivatives. This work developed a new Candida rugosa lipase (CRL) nanogel based on modification of ionic liquid with vinyl functional groups. This novel CRL nanogel was used in the preparation process of vitamin E succinate based on the principle of non-aqueous enzymology. At the same time, various factors including enzyme concentration, substrate molar ratio, reaction temperature and reaction time, that affect the yield of vitamin E succinate were optimized and analyzed.RESULTS: Different solvents with various hydrophobicity parameters (LogP values) from −1.3 to 3.5 were studied, it was found that dimethyl sulfoxide (DMSO) had the lowest LogP value among organic solvents but vitamin E succinate had the highest yield in DMSO. Furthermore, the effect of different operating conditions, such as molar ratios of substrate, enzyme concentration, reaction temperature and reaction time was studied. Under the optimal process conditions (enzyme concentration 6 mg mL −1 , substrate molar ratio 4:1, reaction temperature 55°C and reaction time 15 h), the product yield was 62.58 ± 1.16%. CRL and CRL nanogel were characterized using Fourier-transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM). It was shown that CRL nanogel influenced the catalytic behavior of lipase significantly by changing the structure and surface properties of CRL. CONCLUSION: Novel lipase nanogel was an excellent biocatalyst for enzymatic synthesis of vitamin E succinate.

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Improving Catalytic Performance of Burkholderiacepacia Lipase by Chemical Modification with Functional Ionic Liquids

Cited by 10 publications

References 44 publications

Enhancing the Catalytic Performance of Candida antarctica Lipase B by Chemical Modification With Alkylated Betaine Ionic Liquids

Enhancing the Catalytic Performance of Candida antarctica Lipase B by Chemical Modification With Alkylated Betaine Ionic Liquids

Chemical modification of lipases: A powerful tool for activity improvement

Lipase nanogel catalyzed synthesis of vitamin E succinate in non‐aqueous phase

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