Molecular Catalysis
·
2022
·
IF 5.089
Yuting Sun,Ming Guo,Shengnan Hu,Xiaobo Fang,Zhicheng Jin,Ronghui Wu
Phthalic acid esters (PAEs) are hard-to-degrade organic pollutants of current concern, and enzyme degradation is a green method for effective degradation of PAEs. To improve the recognition of PAEs, the combination of molecular blotting and immobilized enzyme technology is a novel and efficient method for the degradation of PAEs. In this study, molecularly imprinted carrier (MIP-HNTs) was prepared from halloysite nanotubes (HNTs), using di(2-ethylhexyl) phthalate (DEHP) as the template molecule, methyl methacrylate (MMA) as the functional monomer and (ethylene methacrylate) EDGMA as the cross-linking agent. A novel immobilized enzyme (MIP-HNTs@lipase) was prepared successfully via glutaraldehyde cross-linking, subsequently. The lipase loading efficiency was 76%. The optimal enzymatic activity conditions for MIP-HNTs@lipase were determined to be pH=9 and 50 °C. The MIP-HNTs@lipase exhibited good stability and efficient degradation of DEHP with a degradation rate of 94.758% when the DEHP concentration was at 5 mg·L –1 . This research provided a new strategy for industrial application of enzymes and degradation of persistent pollutants.
研究领域:
环境科学
·
生物技术
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DOI
高影响因子
Current Research in Food Science
·
2022
·
IF 6.269
Mang-Mang Li,Yi-Ting Chen,Jin-Cang Ruan,Wen-Jun Wang,Ji-Guang Chen,Qing-Feng Zhang
Lipase is a very important digestive enzyme for triglyceride absorption in vivo. The inhibitory activities of 26 dietary flavonoids, including flavone, flavanone, isoflavone and flavanol, on lipase were determined. Flavone exhibited stronger inhibitory activity than other types of flavonoids. Among them, luteolin exhibited the strongest inhibitory activity with IC50 value of 99 ± 11 μM, followed by quercetin and baicalein. The binding affinity of these flavonoids with lipase was investigated by fluorescence titration method. The binding affinity of flavones was stronger than flavanones, and was linearly positively correlated with their inhibitory activity. The binding of flavones on lipase caused the blue-shift of fluorescence, while flavanones caused red-shift. The analysis of structure-activity relationship of flavonoids on lipase revealed that the structure of C ring is very crucial. The hydrogenation of C2=C3 bond and the absence of C=O group in C ring both caused significant decrease of inhibitory activity. Besides, the hydroxylation on ring A and B of flavones increased the activity, while glycosylation weakened the activity. Molecular docking analysis confirmed that C2=C3 bond in C ring of flavones increases the π-conjugation and contributes to maintaining the planarity of flavonoid structure, which favour its Pi-Pi interaction with lipase.
研究领域:
药理学
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生物化学
·
营养学
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DOI
PubMed
高影响因子
FEBS Journal
·
2015
·Vol. 282
·期 23
·4538-4547
·
IF 4.001
Shaohua Guo,Jinxin Xu,Ioannis V. Pavlidis,Dongming Lan,Uwe T. Bornscheuer,Jinsong Liu,Yonghua Wang
Monoacylglycerol and diacylglycerol lipases are industrially interesting enzymes, due to the health benefits that arise from the consumption of diglycerides compared to the traditional triglyceride oils. Most lipases possess an α-helix (lid) directly over the catalytic pocket which regulates the activity of the enzyme. Generally, lipases exist in active and inactive conformations, depending on the positioning of this lid subdomain. However, lipase SMG1, a monoacylglycerol and diacylglycerol specific lipase, has an atypical activation mechanism. In the present study we were able to prove by crystallography, in silico analysis and activity tests that only two positions, residues 102 and 278, are responsible for a gating mechanism that regulates the active and inactive states of the lipase, and that no significant structural changes take place during activation except for oxyanion hole formation. The elucidation of the gating effect provided data enabling the rational design of improved lipases with 6-fold increase in the hydrolytic activity toward diacylglycerols, just by providing additional substrate stabilization with a single mutation (F278N or F278T). Due to the conservation of F278 among the monoacylglycerol and diacylglycerol lipases in the Rhizomucor miehei lipase-like family, the gating mechanism described herein might represent a general mechanism applicable to other monoacylglycerol and diacylglycerol lipases as well. Database Structural data are available in the Protein Data Bank under the accession numbers 4ZRE (F278D mutant) and 4ZRD (F278N mutant).
研究领域:
生物化学
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分子生物学
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酶工程
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DOI
PubMed
高影响因子
NEW JOURNAL OF CHEMISTRY
·
2023
·Vol. 47
·期 20
·9708-9713
·
IF 3.3
Yuelin Xu,Fengxi Li,Yong Tang,Junhao Wu,Chunyu Wang,Chuang Du,Zhi Wang,Lei Wang
As a base structural unit, 1,4-dihydropyridines (DHPs) containing benzosultams widely exist in bioactive molecules and drugs. These compounds are generally synthesized by organic-base catalyzed methods that require specifically functionalized substrates or harsh conditions. Herein, a [3+3] annulation reaction of cyclic N-sulfonyl ketimine with various substituted isatylidene malononitrile or benzylidene malononitriles was documented. This biocatalytic strategy provides a green route for synthesis of 1,4-DHPs containing benzosultams, with good functional groups compatibility and yields. Under optimal conditions, lipase leads to the formation of 1,4-DHPs containing benzosultams in up to 87% yield.
研究领域:
有机化学
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药物化学
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生物催化
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DOI
高影响因子
JOURNAL OF CHROMATOGRAPHY A
·
2019
·
IF 3.858
Jia Liu,Run-Tian Ma,Yan-Ping Shi
With the increasing demand for lipase inhibitors and new drugs used in the clinical treatment of obesity, it is of great significance to screen lipase inhibitors from traditional Chinese medicines (TCMs) via capillary electrophoresis. In this work, Fe 3 O 4 @TiO 2 nanoparticles was fabricated by solvothermal method and employed as an improved magnetic support to immobilize lipase through electrostatic interaction. By the method of transmission electron microscopy, fourier transform infrared spectroscopy and X-ray diffraction, the magnetic nanoparticles were characterized. The immobilized enzyme possessed advantages of a wider range for pH and temperature endurance, better storage stability and reusability. The kinetics performances of the immobilized lipase were studied. When p-Nitrophenyl palmitate (pNPP) was used as enzyme substrate, the Michaelis-Menten constant was calculated to be 2.51 mM and its inhibition constant for Orlistat was ascertained to be 13.41 μM. Ultimately, the established method was applied to lipase inhibitors screening from 6 Tibetan medicines with lipase inhibitory activity and Oxytropis falcate Bunge was screened out for its supreme lipase inhibitory activity. 11 compounds in the Oxytropis falcate Bunge were further screened, five compounds exhibited similar inhibitory activity to Orlistat, and one compound (kaempferol) presented better inhibitory activity than Orlistat, which is the most commonly used drugs to treat obesity in clinic. This work not only developed a method for new anti-obesity drugs discovery, but also provided inspiration for exploring new medicinal value of the TCMs.
研究领域:
药学
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生物技术
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中药学
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药物发现
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DOI
PubMed
高影响因子
Journal of Future Foods
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2026
·
IF 10.6
Jinchao Hou,Haohua Hu,Shuaiqi Yan,Le Zhong,Geling Kuang,Yuxiao Feng,Hongwu Wang,Jiandong Cui
A green DES/TX-100/water multicomponent interfacial system was constructed for lipase immobilization. • Hydrophobic hollow bowl-shaped mesoporous carbon (H-HBMC) served as an interfacial activation support. • AOL@H-HBMC-L/DTW achieved 108.43% activity recovery and 1.75-fold higher k cat / K m. • The interface induced lid opening, hydrophobic surface exposure, catalytic triad rearrangement, and enhanced organic solvent/thermal stability. Lipase has a wide range of applications in the food industry, such as baked food, dairy products, and oil modification. However, natural free lipase exhibits the poor stability and low activityin in dustrial applications. Inspired by the interfacial catalysis of lipase, herein, lauric anhydride-modified hydrophobic SiO 2 -derived hollow bowl-shaped mesoporous carbon particles (HBMC) were prepared and utilized to immobilize lipase from Aspergillus oryzae (AOL) in a multicomponent interfacial system composed of Deep eutectic solvents/Triton X-100/water (DTW). The resultant immobilized lipase (AOL@H-HBMC-L/DTW) exhibited higher activity recovery (108.43%) than free lipase. Meanwhile, the catalytic efficiency ( k cat / K m ) of immobilized lipase was 1.75-fold that of free lipase. In addition, thermal stability and organic solvent tolerance were also enhanced. After heating at 55 °C for 25 min, the immobilized lipase could retain 41.87% of its initial activity, whereas free lipase only maintained 29.63% of its initial activity. After dimethylformamide (DMF) treatment for 1 h, the free lipase retained only 50.12% of its activity, whereas the immobilized lipase retained 90.14%. Furthermore, it was demonstrated that hydrophobic H-HBMC-L and the multicomponent interfacial system could facilitate lipase activation and improve its activity. Therefore, we believe that the strategy proposed here has potential in preparing lipase biocatalysts with high activity and stability. Download: Download high-res image (203KB) Download: Download full-size image
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DOI
高影响因子
Surfaces and Interfaces
·
2025
·
IF 6.3
Buqing Huo,Xuanhong Zhou,Xiaohui Huang,Tianci LIU,Haozhou Yu,Ziyin Huang,Qingyue Sun,Shihong Chen,Xiaojun Zhang,Ruimin Long,Changbiao Chi,Guo Chen
While lipases offer an environmentally friendly and highly efficient means of degrading lipids and mitigating waterborne lipid pollution, the practical application of free lipases in industrial settings is often limited by inherent instability and dependence on oil-water interfaces for activation. To address these limitations, this study presents an innovative strategy based on the synthesis of phenylalanine-modified magnetic nanoparticles (Fe₃O₄@Phe), which leverages hydrophobic-electrostatic synergistic interactions to achieve high lipase loading and stable immobilization. The hydrophobic phenylalanine moiety of Fe₃O₄@Phe is specifically designed to mimic the oil-water interfacial microenvironment, thereby enhancing catalytic efficiency. Furthermore, we ingeniously employed hollow microsphere-integrated 3D printing to fabricate Fe₃O₄@Phe@Lipase Floating Microspheres, enabling precise positioning of the immobilized lipase at the oil-water interface and resulting in a 1.86-fold increase in reaction efficiency compared to non-floating Fe₃O₄@Phe@Lipase. Importantly, the Fe₃O₄@Phe@Lipase Floating Microspheres demonstrated exceptional stability to a wide range of extreme conditions, including varying pH levels, elevated temperatures, and denaturants. These characteristics render them well-suited for scalable applications in lipid contamination remediation in aquatic environments and industrial lipid hydrolysis, without requiring mechanical agitation or emulsification. This research not only demonstrates a promising strategy for enzyme immobilization on amino acid-functionalized magnetic nanoparticles through microenvironment mimicry, but also introduces a flexible assembly platform for tuning catalyst density and enhancing catalytic efficiency. The described method holds significant potential for broader application across a spectrum of interfacial reactions and with diverse catalysts in lipid pollution control.
研究领域:
环境科学
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酶工程
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纳米技术
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催化化学
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海洋污染控制
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化学工程
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产品关联
DOI
高影响因子
BioDesign Research
·
2025
·
IF 4.7
Qian Li,Mingpeng Li,Ling Wang,Xiaojuan Yu,Yuling Zhou,Chenghua Gao,Aitao Li
Clascoterone (cortexolone 17α-propionate), a novel therapeutic agent for acne, provides enhanced safety and efficacy over conventional therapies. However, the traditional synthesis of clascoterone, especially the final step, suffers from the use of hazardous and excessive organic solvents, along with suboptimal yields due to side reactions and incomplete conversion, which poses environmental and economic challenges. In this study, we developed a regioselective solvent-free alcoholysis method with the commercially available immobilized lipase Novozyme 435 as a catalyst and isopropanol (IPA) as an alcohol donor, achieving a conversion rate of over 98.0% with 20 g/L substrate. Furthermore, we implemented a continuous flow microreactor process that increased the conversion rate to 100% with 4 g/L substrate, demonstrating scalability for industrial manufacturing.
研究领域:
有机合成
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生物催化
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药物化学
·
化学工程
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DOI
PubMed
高影响因子
Catalysts
·
2023
·Vol. 13
·期 12
·1493
·
IF 3.9
Feiyang Wen,Yuelin Xu,Fengxi Li,Jinglin Ma,Zhi Wang,Hong Zhang,Lei Wang
Disulfides, as fundamental scaffolds, are widely present in peptides, natural products, and pharmaceutical molecules. However, traditional synthesis of disulfides often involves the utilization of toxic reagents or environmentally unfriendly reaction conditions. In this work, a green and efficient method was developed for synthesizing pyrrole disulfides using β-ketothioamides and ethyl cyanoacetate as substrates, with lipase serving as a catalyst. Under the optimal conditions (β-Ketothioamides (1 mmol), ethyl cyanoacetate (1 mmol), PPL (200 U), and EtOH (5 mL)), lipase leads to the formation of pyrrole disulfides in yields of up to 88% at 40 °C. The related mechanism is also speculated in this paper. This approach not only presents a new application of lipase in enzyme catalytic promiscuity, but also offers a significant advancement in the synthetic pathway for pyrrole disulfides and aligns with the current mainstream research direction of green chemistry, contributing to the further development of environmentally friendly biocatalytic processes.Keywords:lipase;catalytic promiscuity;pyrrole disulfide;β-ketothioamides;cyanoacetate
研究领域:
生物化学
·
绿色化学
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DOI
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2012
·
IF 2.823
Xuanxuan Lu,Zhigang Luo,Shujuan Yu,Xiong Fu
Lipase-catalyzed synthesis of starch palmitate was investigated in ionic liquid mixtures consisting of 1-butyl-3-methyl-imidazolium acetic ([BMIm]Ac) and 1-butyl-3-methyl-imidazolium tetraflouroborate ([BMIm][BF4]). The effect of reaction parameters such as the amount of enzyme used, the reaction temperature, the mass ratio of [BMIm][BF4]/[BMIm]Ac, the molar ratio of methyl palmitate/anhydroglucose unit in starch, and the reaction time on the degree of substitution was studied. The formation of starch esters was confirmed by the presence of the carbonyl signal in the FT-IR and NMR spectra. Scanning electron microscopy and X-ray diffraction data showed that the morphology and crystallinity of starch esters were largely disrupted. Thermogravimetric analysis suggested thermal stability of starch palmitate decreased compared to native starch. Water contact angle measurements revealed that the hydrophobicity of starch esters was improved after modification. The successful lipase-catalyzed synthesis of starch palmitate in ionic liquids suggested that ionic liquids could be used as a potentially attractive green alternative to harmful organic solvents for synthesis of high fatty acid starch ester.
研究领域:
生物化学
·
材料科学
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产品关联
DOI
PubMed
高影响因子
MOLECULES
·
2018
·Vol. 23
·期 9
·2154
·
IF 3.098
Yunchang Fan,Dongxu Cai,Xin Wang,Lei Yang
Recently, ionic liquids (ILs) have been regarded as ideal media for non-aqueous bio-catalysis. In this work, the synthesis of warfarin by the lipase-catalyzed Michael addition in IL media and the parameters that affected the warfarin yield were investigated. Experimental results demonstrated that the chemical structures of the ILs were a major factor for influencing the warfarin yield. The ILs containing the NTf2–anion were suitable reaction media due to the high chemical stability of this anion. The incorporation of the hydroxyl group on the IL cation significantly improved the lipase activity due to the H2O-mimicking property of this group. The lipase activity decreased by increasing the alkyl chain length on the IL cation due to the non-polar domain formation of the IL cation at the active site entrance of lipase. The ILs and lipase could be reused no less than five times without reduction in the warfarin yield.Keywords:ionic liquids (ILs);lipase;Michael addition;warfarin;bio-catalysis
研究领域:
生物化学
·
制药工程
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产品关联
DOI
PubMed
高影响因子
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
·
2014
·Vol. 172
·期 6
·3128-3140
·
IF 1.687
Zhang Wei-Wei,Wang Na,Zhang Ling,Wu Wan-Xia,Hu Cheng-Li,Yu Xiao-Qi
An inexpensive, facile, and environmentally benign method was developed to improve the activity and stability of Candida rugosa lipase (triacylglycerol acylhydrolase) immobilized on microemulsion-based organogels (CRL MBGs) via the addition of additives during immobilization. The additives used were polyethylene glycol (PEG) or polysaccharides. This study is the first report on the effect of additives in CRL MBGs. Among the tested additives, PEG produced the most improvement in the immobilized CRL, enhancing its stability in organic solvents (specifically polar solvents). The results of circular dichroism and fluorescence spectra experiments indicated that exposure of the acidic CRL to electronegative additives in the buffer, such as polyethylenimine and the electropositive surfactant cetyltrimethylammonium bromide, may change the lipase secondary structure, ultimately causing enzyme inactivation. However, sodium bis(2-ethylhexyl)sulfosuccinate and PEG 2000 had minimal effects on the secondary structure of CRL. The CRL MBGs containing PEG 2000 demonstrated remarkable retention of their catalytic activity during the recycling test. No significant changes in enzymatic activity were observed, even after nine runs, and 90 % of the original yield was maintained after 15 cycles.
研究领域:
生物技术
·
酶学
·
化学工程
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）