EUROPEAN JOURNAL OF INORGANIC CHEMISTRY
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2018
·Vol. 2018
·期 41
·4579-4585
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IF 2.507
Xiao Liu,Wei Qi,Yuefei Wang,Rongxin Su,Zhimin He
Graphical We demonstrated that UiO-66 and its derivatives possess efficiently intrinsic lipase-like activity, catalyzing ester hydrolysis, transesterification and even the esterification reaction. It's –NH 2 functionalized analogue UiO-66(NH 2 ) exhibited the highest catalytic activity due to the synergistic catalytic effect. To overcome the disadvantages of natural enzymes, artificial enzyme mimics attracted increasing attention of researchers. Metal-organic frameworks (MOFs) are expected as one of the most appropriate candidates for artificial enzyme mimics. In this work, we demonstrate that the zirconium-based MOF material UiO-66 and its analogues possess intrinsic lipase-like activity and can efficiently catalyze ester hydrolysis, transesterification and esterification reactions. Furthermore, the UiO-66(NH 2 ) exhibits much higher catalytic activity than that of UiO-66, which can be attributed to the synergy effect between the zirconium cluster centres and the amino moieties during the catalytic cycle.
研究领域:
生物化学
·
材料科学
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JOURNAL OF MATERIALS SCIENCE
·
2023
·
IF 4.5
Gao Nengwen,Liu Jing,Wang Xiaoli,Zhang Yu
Lipases are widely used in industry. Free lipases are difficult to recover and have poor stability under operational conditions. Herein, lipases are immobilized onto the methyltrimethoxysilane (MTMS)-modified ceramic membranes (~ 5 nm) with reverse filtration method, and further cross-linking by glutaraldehyde (GA) is used to improve the lipase stability. FTIR and XPS analyses demonstrate the successful immobilization of lipase. The immobilized lipases are used to hydrolyze glycerol triacetate (GT) to fatty acids and glycerol. Under the optimal immobilization conditions (MTMS concentration 0.1 M, lipase immobilization time 80 min, lipase concentration 3 mg/mL, and GA concentration 2%), the loading of lipases reaches 0.24 mg/g. Under the optimal operational conditions (temperature 45 °C, pH 7, pressure 0.2 MPa, GT concentration 0.05 M), the immobilized lipases have the highest catalytic activity of 25 U/mg. Moreover, the thermal and pH stabilities of immobilized lipases are found to be higher than those of the free lipases. In the long-term runs, the immobilized lipases still have 64% of the initial activity after 7 cycles, indicating good reusability. This paper provides a simple process for immobilizing lipase on ceramic membranes. The immobilized lipases have better stability at high temperature and basic environments (pH 7–9), which would have broad applications in lipase-catalyzed reactions. Graphical Abstract
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Micro & Nano Letters
·
2018
·Vol. 13
·期 4
·572-575
·
IF 0.841
Yan Zhou,Shanshan Sun,Shuhui Jiang,Hao Liang
The inactivation of lipases caused by organic solvents, high temperature, extremely acidic and alkaline requires a high stability. In this work, a novel one-pot synthesis for the lipase immobilisation on silica nanoparticles was reported. The optimal amounts of (3-ammonia propyl) triethoxysilane (APTES) and ammonia were studied. The apparent K m value of the immobilised Candida rugosa lipase (CRL) was lower than that of free enzyme, showing affinity of the immobilised CRL to its substrate had increased. The results of stability test showed that the immobilised lipase was more stable than free enzyme at different temperatures and pH values. In particular, the immobilised CRL kept 96% activity at 90°C, while the free enzyme only remained 75% activity. Immobilised lipase had high catalytic efficiency, enhanced stability and recyclable usability compared to free enzymes, because of the cross-linking between the protein and the rigid carrier. Therefore, the immobilised method would be beneficial to improving the activity and stability of enzyme universally.
研究领域:
生物化学
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纳米生物学
·
酶工程
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高影响因子
ANALYTICAL BIOCHEMISTRY
·
2018
·
IF 2.275
Jianyong Zheng,Wei Wei,Xing Lan,Yinjun Zhang,Zhao Wang
This study describes a sensitive and fluorescent microplate assay method to detect lipase transesterification activity. Lipase-catalyzed transesterification between butyryl 4-methyl umbelliferone (Bu-4-Mu) and methanol in tert -butanol was selected as the model reaction. The release of 4-methylumbelliferone (4-Mu) in the reaction was determined by detecting the fluorescence intensity at λ ex 330 nm and λ em 390 nm. Several lipases were used to investigate the accuracy and efficiency of the proposed method. Apparent Michaelis constant ( K m) was calculated for transesterification between Bu-4-Mu and methanol by the lipases. The main advantages of the assay method include high sensitivity, inexpensive reagents, and simple detection process.
研究领域:
生物化学
·
酶学
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PubMed
高影响因子
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
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2013
·Vol. 171
·期 7
·1559-1567
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IF 1.893
Wang Na,Zhang Wei,Zhou Long-Hua,Deng Qing-Feng,Xie Zong-Bo,Yu Xiao-Qi
A facile tandem route to α,β-unsaturated aldehydes was developed by combining the two catalytic activities of the same enzyme in a one-pot strategy for the aldol reaction and in situ generation of acetaldehyde. Lipase from Mucor miehei was found to have conventional and promiscuous catalytic activities for the hydrolysis of vinyl acetate and aldol condensation with in situ formed acetaldehyde. The first reaction continuously provided material for the second reaction, which effectively reduced the volatilization loss, oxidation, and polymerization of acetaldehyde, as well as avoided a negative effect on the enzyme of excessive amounts of acetaldehyde. After optimizing the process, several substrates participated in the reaction and provided the target products in moderate to high yields using this single lipase-catalyzed one-pot biotransformation.
研究领域:
生物化学
·
酶工程
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SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
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2016
·
IF 2.653
Yunchang Fan,Xing Dong,Xiaojing Li,Yingying Zhong,Jichuan Kong,Shaofeng Hua,Juan Miao,Yan Li
The effects of ionic liquids (ILs) on the lipase activity were studied by UV–Vis spectroscopy and the IL-lipase interaction mechanism at the molecular level was investigated by fluorescence technique. Experimental results indicated that the lipase activity was inhibited by ILs and the degree of inhibition highly depended on the chemical structures of ILs. The inhibitory ability of the Cl − - and Br − -based ILs increased with increasing the alkyl chain length in the IL cation. Thermodynamic parameters, enthalpy change (Δ H ) and entropy change (Δ S ) were obtained by analyzing the fluorescence behavior of lipase with the addition of ILs. Both Δ H and Δ S were positive suggesting hydrophobicity was the major driven force for the Cl − - and Br − -based ILs. For the BF 4 − -, CF 3 SO 3 − -, ClO 4 − - and N(CN) 2 − -based ILs, hydrogen bonding was the main driven force. For a more comprehensive understanding of the effects of ILs on lipase activity, the roles of hydrophobicity and hydrogen bonding must be considered simultaneously. A regression-based equation was developed to describe the relationship of the inhibitory ability of ILs and their hydrophobicity and hydrogen bonding ability.
研究领域:
生物化学
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分子生物学
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高影响因子
ChemistrySelect
·
2023
·Vol. 8
·期 29
·e202300512
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IF 2.1
Kangjing Wang,Xinyi Dong,Ting Li,Qian Wang,Zhongyang Ding,Weifu Dong
Graphical The contact angle of modified starch was changed from 12.2° to 71.5°, and the particle size was changed from ∼10 μm to ∼300 nm. In the subsequent enzyme catalyzed reaction, the immobilized enzyme is adsorbed at the water oil interface, thereby improving the lipase activity. As a natural macromolecular material, starch is an ideal carrier for enzyme immobilization because of its widely available source, easy regeneration and excellent biodegradability. However, the natural starch cannot be directly used for immobilization due to the large particle size and excessive hydrophilicity. In this paper, the epoxy groups were grafted onto esterified starch by bifunctional reagents. The grafting efficiency of epoxy groups was increased by starvation drop addition. The changes of contact angle and particle size are conducive to the adsorption of immobilized enzyme at the water oil interface in the subsequent enzyme catalytic reaction, hence improve of the lipase activity. The maximum amount of lipase mobilized on such modified starch was ∼143.7 mg/g, which was near 40 mg/g higher than that of those from direct crosslinking. The immobilized enzymes showed excellent resistance to organic solvents and good reusability. Immobilization of lipases on epoxy-functionalized starch nanoparticles can potentially improves the possibility of enzymes industrial application.
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MICROPOROUS AND MESOPOROUS MATERIALS
·
2023
·
IF 5.2
Lili Xu,Xinyue Geng,Rui Cao,Jiahao Zhu,Fei Chen,Cuihong Li,Lexuan Wang,Xuekun Wang,Hongbo Suo
Metal-organic frameworks (MOFs) have shown great potential as supports for enzyme immobilization, but their application is limited by separation difficulties due to their nanoscale size. Herein, magnetic MOFs (Fe 3 O 4 @MIL-53-NH 2 (Al)) were prepared under mild conditions, and an ionic liquid (IL) was used as linker to covalently immobilize lipase in Fe 3 O 4 @MIL-53-NH 2 -IL/PPL. The IL was composed of imidazolium cations and bis(trifluoromethylsulfonyl)imide anions, which enhanced the hydrophobicity of the support. The synthesized biocatalyst Fe 3 O 4 @MIL-53-NH 2 -IL/PPL showed excellent activity, 2.4 times higher than free lipase, and its denaturation, thermal, and storage stability were all satisfactory. The activity of the biocatalyst remained at up to 88.4% after ten recycles. The excellent magnetic responsiveness facilitated the collection of the biocatalyst, which may be beneficial to its reusability, and the multiple interactions between lipase and support may enhance the structural stability of lipase, which was investigated by circular dichroism spectroscopy. Compared to free lipase, both the substrate affinity and catalytic efficiency of Fe 3 O 4 @MIL-53-NH 2 -IL/PPL were improved. The magnetic MOF composite materials prepared through the post-synthesis method exhibited good potential in the field of lipase immobilization. The preparation method of immobilized lipase in this work provides a meaningful reference for the application of other MOF composites in the field of enzyme immobilization.
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BIOCONJUGATE CHEMISTRY
·
2023
·
IF 4.7
Yun-Yan Xiao,Jiang-Tao Zhang,Yong-Hua Dong,Shu-Li Li,Gao-Ying Zhi,Ya-Fang Zhang,Dong-Hao Zhang
Here, lipase encapsulation is constructed by locking enzyme molecules in nanomolecular cages on the surface of SH-PEI@PVAC magnetic microspheres. To improve the encapsulation efficiency in enzyme loading, the thiol group is efficiently modified on the grafted polyethyleneimine (PEI) using 3-mercaptopropionic acid. N2 adsorption–desorption isotherms reveal the existence of mesoporous molecular cages on the microsphere surface. The robust immobilizing strength of carriers to lipase demonstrates the successful encapsulation of enzymes in nanomolecular cages. The encapsulated lipase shows high enzyme loading (52.9 mg/g) and high activity (51.4 U/mg). Different sizes of molecular cages are established, and the cage size showed important effects on lipase encapsulation. It shows that enzyme loading is low at a small size of molecular cages, which is attributed to that the nanomolecular cage is too small to house lipase. The investigation in lipase conformation suggests that the encapsulated lipase retains its active conformation. Compared with the adsorbed lipase, the encapsulated lipase shows higher thermal stability (4.9 times) and higher resistance to denaturants (5.0 times). Encouragingly, the encapsulated lipase shows high activity and reusability in lipase-catalyzed synthesis of propyl laurate, suggesting the potential application value of encapsulated lipase.
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COLLOIDS AND SURFACES B-BIOINTERFACES
·
2023
·
IF 5.8
Mianxing Luo,Liang Wang,Guo Chen,Jun Zhao
The orientation of the enzyme molecular on the interface of the carrier affects its activity. Therefore, it is very important to controllably induce the orientation of the enzyme on the surface to improve the performance of the immobilized enzyme . Magnetic nanoparticles were used to construct microenvironments with the different surface hydrophobicity and charge characteristics by controlled modification, and those particles with various microenvironments were further used to study their interaction with the lipase . The amount and activity of immobilized enzyme on different magnetic nanoparticles surfaces were studied by physical adsorption and covalent binding. Through the enzyme surface and particle surface characteristics analysis, the possible preferred orientation of enzyme and enzyme conformation on different surfaces were inferred, which well explained the effect of surface induction on enzyme loading and activity. The methods of surface microenvironment regulation and the strategy of controllable induction of enzyme orientation adopted in this study are enlightening for the rational design of immobilized enzyme methods.
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JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2023
·Vol. 103
·期 7
·3489-3500
·
IF 4.1
Yihang Liu,Qingzhi Wang,Chen Liu,Haonan Yang,Li Jia,Litao Zhao,Fayong Gong,Chen Tan,Hongxun Tao,Wen-Sen He
BACKGROUND Oxidation is a major problem for oils and fats, which can be mitigated by antioxidants. Rutin has excellent antioxidant activity, but its poor lipid solubility greatly limits its practical application. In this study, an efficient enzymatic synthesis route of lipophilic rutin ester was established using oleic acid as an acyl donor, and the antioxidant potential of rutin oleate was evaluated for the first time by proton ( 1 H) nuclear magnetic resonance (NMR) spectroscopy. RESULTS The synthesized product was finally identified as rutin oleate by Fourier transform infrared, high-performance liquid chromatography–mass spectrometry, and 1 H, carbon-13, and DEPT-135 NMR analyses, and the acylation site was the 4‴-OH of the rhamnose group in the rutin molecule. The maximum conversion was over 93% after 48 h of reaction using Novozym 435 as catalyst under the best conditions among these tests. The conversion of rutin ester decreased with the increase of carbon chain length and the number of carbon–carbon double bonds of the fatty acid molecule. Most importantly, rutin oleate exhibited antioxidant capacity comparable to butylated hydroxytoluene and its counterparts (rutin and oleic acid) at low temperatures (60° C), but had a significant advantage at high temperatures (120° C). CONCLUSION The antioxidant activity of rutin was significantly enhanced by lipase-mediated esterification with oleic acid. Therefore, rutin oleate could be further developed as a novel antioxidant for use in oil‑ and fat-based foods. © 2023 Society of Chemical Industry.
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Nanoscale
·
2021
·Vol. 13
·期 42
·17871-17880
·
IF 7.79
Wenjing Qi,Huimin Yu
Surface immobilization of enzymes on magnetic-recoverable carriers is of great interest and importance for the biocatalysis of relatively large molecules. In this work, the nanosized amino-rich filamentous M13 virus, a versatile biological scaffold, was applied as the unique soft backbone for lipase immobilization. Based on the structure and capsid proteins of M13 phages, the magnetic-recoverable mimic-free-lipases (MFLs) composed of the M13 hydrogels and magnetic particles were developed in two designs. In the first design, nanosized wild M13 phages were crosslinked into a phage hydrogel through the N-terminals of pVIII peptides while NH2-Fe3O4 magnetic nanoparticles (MNPs) were attached to the M13 virus through glutaraldehyde, forming the M13-(NH2-Fe3O4) magnetic phage hydrogel. In the second design, special M13 with Fe3O4 affinity pIII-peptide (FAP-M13) was biopanned for strongly binding towards bare Fe3O4 with the “hook”-like pIII-peptide (N-LPLSTQH-C). TEM observation confirmed the direct grasp of FAP-M13 on bare Fe3O4, forming the magnetic (FAP-M13)-Fe3O4 virus hydrogel. Lipases were uniformly anchored on the phage surface of nanoscale by crosslinking with the N-terminals of pVIII peptides, and then lipase@M13-(NH2-Fe3O4) and lipase@(FAP-M13)-Fe3O4 MFLs were constructed. For both MFLs, high activity recovery yield (>95%) and efficient magnetic separation were characterized. Significantly reduced MNP-usage-amount and enhanced lipase-loading-amount both by about 40 folds were obtained, compared with the conventional NH2-Fe3O4 carriers. The quantified Km and Vmax/Km values were almost equal to those of the free lipases, verifying free-enzyme-mimicking features of the MFLs. High pH-tolerance, wide temperature adaptability, enhanced thermal stability and stable magnetic separation capability of both MFLs were also observed. In particular, the (FAP-M13)-Fe3O4 magnetic virus hydrogel simply using bare Fe3O4 MNPs would be more convenient and economical in the scaled-up biocatalysis.
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