JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2025
·Vol. 105
·期 7
·3931-3941
·
IF 3.5
Jiawei Zheng,Qiangyue Zhang,Nanjing Zhong
BACKGROUND Immobilized enzyme possessing both high activity and good selectivity is important in practice. In this study, Candida antarctica lipase B (CALB) was immobilized onto the macroporous resin ADS-17 for triacylglycerol (TAG) synthesis through esterification of oleic acid and glycerol. The reaction conditions were optimized by single-factor study and orthogonal test, and the reusability of the immobilized CALB (CALB@ADS-17) was evaluated. In addition, the mechanism of lipase immobilization was studied and the catalytic mechanism of CALB@ADS-17 was investigated. RESULTS Oleic acid conversion up to 99.20% and TAG content at 91.58 wt% could be obtained under optimal conditions. In addition, the CALB@ADS-17 retained 84.28% of its initial activity after 11 cycles of reuse. The mechanism of lipase immobilization was through hydrophobic adsorption. The relationship between temperature and oleic acid conversion was ln V 0 = 6.3316 − 4.3321/ T , and the activation energy ( E a ) was 36.02 kJ mol −1 . CALB@ADS-17 did not exhibit an obvious interfacial activation phenomenon. Its kinetic behavior can be described by the Michaelis–Menten model, whose kinetic parameters of v max , k cat , K m , K i , and k ca t /K m were 0.01265 μmol L −1 s −1 , 9310.72 s −1 , 0.4907 mmol L −1 , 3.997 mmol L −1 , and 1.90 × 10 4 L mmol −1 s −1 , respectively. CONCLUSION CALB@ADS-17 showed good esterification performance and exhibited good selectivity towards TAG generation. In addition, CALB@ADS-17 exhibited good reusability in esterification reactions and has potential in practical applications. © 2025 Society of Chemical Industry.
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PubMed
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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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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高影响因子
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
·
2023
·
IF 2
Miao Qiao,Xin Hua,Yongjun Yuan,Xi Cao
This work attempts to achieve the enrichment of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in acylglycerols as well as biodiesel production by investigating the performance of various lipases in ethanolysis. The ethanolysis activities of five immobilized lipases in decreasing order were as follows: Lipozyme TL IM, Novozym 40086/Lipozyme RM IM, Novozym 435 and Rhizopus oryzae lipase immobilized on polypropylene (RO PP). EPA could be enriched to a certain content by Lipozyme TL IM, Novozym 40086, Lipozyme RM IM, and RO PP. The enrichment of DHA was achieved well by those four sn -1,3 regioselective lipases, and DHA contents in acylglycerols were the highest when Lipozyme TL IM and Novozym 40086 were used, reaching 2.87-fold and 2.81-fold of the initial content. However, Novozym 435 could not enrich EPA and DHA effectively. Fatty acid ethyl esters produced in this work contained abundant palmitic acid and palmitoleic acid, which could be ideal biodiesel considering their chain length. The competitive factors of five lipases towards DHA were all significantly higher than those towards EPA. When Lipozyme TL IM and Novozym 40086 achieved the maximum DHA contents, their DHA recoveries in acylglycerols reached 91.87% and 89.00%, respectively. The DHA recoveries were all significantly higher than the corresponding EPA recoveries in the reactions catalyzed by five lipases. Moreover, Lipozyme TL IM could be a potential lipase for the separation of EPA and DHA. This study may promote the full use of fish oil and broaden the application of lipases.
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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.
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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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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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