Molecular Catalysis
·
2021
·
IF 5.062
Yu Han,Xinying Zhang,Liangyu Zheng
In our previous study, the soluble expression of recombinant Candida antarctica lipase B ( r CalB) in E. coli is achieved through fusion with polyamino acid tails. The present study showed that even in the form of inclusion bodies ( r CalB-IBs), r CalB-IBs were still active towards enzyme-catalyzed reactions. r CalB-IBs could be directly crosslinked by the oxidized dextran in the presence of Fe 3 O 4 nanoparticles to obtain magnetic aggregates ( r CalB-mclIBs), and an activity recovery of 113.9 % ± 2.2 % could be achieved under optimized conditions. The obtained r CalB-mclIBs exhibited excellent thermal and storage stabilities, and a good tolerance in changing pH environmental. r CalB-mclIBs could be effectively recycled and could retain 85.4 % ± 2.5 % of its initial activity, and an e.e. p of 84.4 % ± 2.2 % in ( R , S )-NEMPA-ME hydrolysis was observed after the 10th cycle. After the application of r CalB-mclIBs into a promiscuous carbon–carbon bond-forming reaction, the MBH and the Aldol products could be obtained simultaneously. This study provides a simple and inexpensive strategy to highlight the application potential of r CalB-IBs as a biocatalyst.
研究领域:
生物化学
·
酶工程
·
合成生物学
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DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2018
·
IF 3.909
Yue Li,Nanjing Zhong,Ling-Zhi Cheong,Jianrong Huang,Hongxiao Chen,Shaoyan Lin
In this study, SBA-15 was modified by a series of silane coupling reagents and later used to immobilize Candida antartica lipase B (CALB). The enzymatic properties of the immobilized CALB samples were studied. In addition, the catalytic performance in glycerolysis of soybean oil for diacylglycerols (DAG) production was also investigated. The highest enzymatic activity up to 6100.00 ± 246.41 U/g was observed from the propyl methacrylate group modified SBA-15 supported CALB. No loss of activity was observed from the propyl methacrylate group modified SBA-15 supported CALB, but a higher-than-initial activity was notably found from 3-aminopropyl group and n -octyl group modified SBA-15 supported CALB after a 4-h incubation in air at 70 °C. 1-isocyanatopropane group modified SBA-15 supported CALB exhibited selectivity for DAG production. DAG content up to 61.90 ± 2.38 wt% and a DAG/MAG ratio at 3.11 ± 0.08 was obtained after a 24-h reaction at 60 °C in a solvent-free system.
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产品关联
DOI
PubMed
高影响因子
ENZYME AND MICROBIAL TECHNOLOGY
·
2014
·
IF 2.966
Chuan-Yang Shang,Wei-Xun Li,Rui-Feng Zhang
ZnO nanowires were successfully introduced into a macroporous SiO 2 by in situ hydrothermal growth in 3D pores. The obtained composites were characterized by SEM and XRD, and used as supports to immobilize Candida antarctica lipase B (CALB) through adsorption. The high specific surface area (233 m 2 /g) and strong electrostatic interaction resulted that the average loading amount of the composite supports (196.8 mg/g) was 3–4 times of that of macroporous SiO 2 and approximate to that of a silica-based mesoporous material. Both adsorption capacity and the activity of the CALB immobilized on the composite supports almost kept unchanged as the samples were soaked in buffer solution for 48 h. The chiral resolution of 2-octanol was catalyzed by immobilized CALB. A maximum molar conversion of 49.1% was achieved with 99% enantiomeric excess of ( R )-2-octanol acetate under the optimal condition: a reaction using 1.0 mol/L ( R , S )-2-octanol, 2.0 mol/L vinyl acetate and 4.0 wt.% water content at 60 °C for 8 h. After fifteen recycles the immobilized lipase could retain 96.9% of relative activity and 93.8% of relative enantioselectivity .
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产品关联
DOI
PubMed
高影响因子
ACS Applied Nano Materials
·
2023
·
IF 5.9
Jiawei Lu,Ying-Nan Li,Youran Li,Huilin Zhu,Guiyang Shi
The reusability of immobilized lipases, including their hydrolysis activity, is greatly affected by lipase leakage, mass transfer channel blockage, and compound deposition on the outside surface. In this study, Candida antarctica lipase B (CALB) was immobilized on Fe3O4 nanoparticle-polyacrylonitrile (PAN) composite magnetic beads through phase inversion (L/FP). The hydrolysis activity of lipase was investigated using p-nitrophenyl palmitate (p-npp) as a model ester. To overcome the limitations of immobilized lipase in ester hydrolysis, three modification strategies were employed. First, lipase was covalently immobilized on Fe3O4 nanoparticles modified with methallyl (M9) and chloro (M13) silane modifiers, which exhibited faster immobilization with reduced lipase leaching and higher activity expression and stability. Second, poly(ethylene glycol) (PEG6000) and polylactic acid (PLA) were added to the precursors to physically modify the composite structures of L/FP, resulting in modified beads with larger specific surface area (15.26 m2·g–1) and smaller average pore size (19 nm). The modified beads, L/FP-9-M and L/FP-13-M, demonstrated superior reusability in long-term hydrolysis activity over 250 cycles. L/FP-9-M retained 63 and 34% of the initial activity at the 100th cycle and the 250th cycle, respectively. L/FP-13-M retained 55 and 36% of the initial activity at the 100th cycle and the 250th cycle, respectively. Furthermore, even after 250 repeated uses, the unit activities (U·gsupport–1) of both L/FP-9-M and L/FP-13-M remained higher than the initial activity of Novo 435.
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DOI
高影响因子
RSC Advances
·
2020
·Vol. 10
·期 15
·8949-8957
·
IF 3.119
Huijuan Shangguan,Shan Zhang,Xin Li,Qi Zhou,Jie Shi,Qianchun Deng,Fenghong Huang
Lutein scavenges free radicals and inhibits vision damage caused by photo oxidation, while decomposing easily with light and heat. Its stability and bioavailability can be tremendously improved by lutein ester synthesis. However, green and efficient esterification preparation methods are urgently needed. In this study, which used functionalized graphitic carbon nitride nanosheets (g-C3N4-Ns) as the immobilized carrier, a novel biocatalyst was designed and prepared to accommodate Candida antarctica lipase B (CALB), considerably enhancing the performance. It was characterized by TEM, XRD, FTIR, XPS, TGA, and BET to demonstrate successful preparation and then applied to catalyze esterification between lutein and succinate anhydride in dimethyl formamide (DMF) solvent resulting in a conversion rate up to 92% at 50 °C in 60 h, 34% more than free CALB under the same conditions. We believe this is the highest esterification rate in lutein esters synthesis and it has great potential to facilitate eco-friendly and efficient preparation.
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产品关联
DOI
PubMed
高影响因子
EUROPEAN JOURNAL OF ORGANIC CHEMISTRY
·
2014
·Vol. 2014
·期 14
·2917-2923
·
IF 3.154
Bo Xia,Guilin Cheng,Xianfu Lin,Qi Wu
Graphical A dynamic double kinetic resolution (DDKR) strategy under the co-catalysis of Raney nickel and Candida antarctica lipase B (CAL-B) was established for the one-pot simultaneous resolution of primary amines and secondary alcohols. Herein, we have established a dynamic double kinetic resolution (DDKR) strategy under the co-catalysis of Raney nickel and Candida antarctica lipase B (CAL-B) for the one-pot simultaneous resolution of primary amines and secondary alcohols (or esters). The DDKR strategy was successfully applied to the resolution of a series of racemic amines and secondary alcohols (or esters) as well as mexiletine, an important antiarrhythmic agent. The catalysts could be recycled and reused several times with the same high activity. Scale-up experiments were also successful. As a more atom-economical and efficient process than traditional simple kinetic resolutions, the DDKR strategy can be widely used to prepare optically pure amines and alcohols.
研究领域:
有机化学
·
生物催化
·
制药工程
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DOI
高影响因子
Molecular Catalysis
·
2021
·
IF 5.062
Chao Xu,Hongbo Suo,Yu Xue,Jing Qin,Hongyue Chen,Yi Hu
Four types of amino acid ionic liquids (AAILs) with chiral structure were used to modify Candida antarctica lipase B (CALB). The results showed that the catalytic activity at different temperatures and pH, thermostability, and tolerance to organic solvents of all modified lipases were improved. The composition and configuration of modifiers have great influence on the catalytic performance of the modified lipases. AAILs composed of l -proline exhibited better modification effect than those containing d -proline. The use of [N-AC- l -Pro] [Cl] led to the highest modification degree (47.92 %) of the lipase, which exhibited the highest hydrolytic activity (430.67 U/g), as well as enhanced thermal stability and tolerance to organic solvents. The structure of CALB was characterized by circular dichroism (CD) and fluorescence spectroscopy. It was found that the introduction of a modifier changes the secondary structure of CALB to a certain extent, and the microenvironment around the fluorescent group changed slightly. The structural stability of CALB modified with [N-AC- l -Pro] [Cl] and the mechanism of reaction were studied by molecular dynamics simulations. The molecular dynamics simulations of the native and modified CALB were performed for 20 ns at 300 and 328 K. The simulation results showed that the root mean square deviation (RMSD) and total energy of modified CALB were less than those of native CALB, indicating a more stable structure for the modified CALB. The root mean square fluctuation (RMSF) calculations showed that the rigidity of the modified CALB and the flexibility of the active center region were both enhanced. The solvent accessibility area (SASA) calculations showed that both hydrophilicity and hydrophobicity of the modified enzyme-protein were improved. The increase in radial distribution function (RDF) of water molecules confirmed that the number of water molecules around the active sites was also increased. Thus, the modified CALB has enhanced structural stability and higher hydrolytic activity towards the triglyceride substrates.
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DOI
高影响因子
Journal of Environmental Chemical Engineering
·
2026
·Vol. 14
·期 4
·123412
·
IF 7.5
Jiahao Ouyang,Yulin Chen,Xiaonuo Li,Jiahao Li,Qiu Xia,Kai Huang,Guangyang Wang,Yong Ye
To address enzyme inactivation upon immobilization and the underutilization of surplus glycerol from biodiesel production, a near-infrared (NIR)-responsive bioconjugate was developed which comprised Candida antarctica lipase B (CALB) immobilized on a CuS/Cu-TCPP support. In this design, Cu-TCPP (a porphyrin-based metal-organic framework) provides a high-surface-area scaffold, CuS nanoparticles act as NIR photothermal converters, and hydrophobic surface modification enhances lipase adsorption. XRD, XPS, SEM, and TEM confirmed the formation of covellite-structure CuS on Cu-TCPP and successful enzyme immobilization. The system achieves a photothermal conversion efficiency of 22.70% (defined as the ratio of heat generated to absorbed laser energy), retains 99.52% of its initial activity at 70 °C, and preserves 74.20% activity after five reuse cycles. During glycerol esterification under NIR irradiation (808 nm) at room temperature, oleic acid conversion reaches 69.2%, representing a 2.42-fold increase compared to the non-irradiated control (28.6%). Bandgap analysis (1.66 eV > 1.53 eV) confirms the absence of reactive oxygen species generation, preventing enzyme oxidative inactivation. This work enables remote, real-time, and precise control of lipase catalysis via localized photothermal heating, offering a green strategy for glycerol valorization.
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DOI
高影响因子
危险品化学品经营许可证（带存储）