JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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2016
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IF 2.189
Yicheng Bi,Min Yu,Haiyan Zhou,Hua Zhou,Ping Wei
In our study, oleyl oleate was synthesized through enzymatic esterification of oleic acid with oleyl alcohol using Candida rugosa lipase (CRL) immobilized on macroporous resin in a solvent-free system. CRL was immobilized flexibly on the support via aldehyde-dextran, and the effectiveness of aldehyde-dextrans, as cross-linking agents with different molecular weights, was compared and discussed. The impact of various factors, such as different molecular weights of dextran , molar ratio between oleic acid and oleyl alcohol, and the temperature and stability of enzymes, on esterification was investigated as well. Our study indicated that lipase immobilized by 20000 Da dextran yielded the best result. The optimal condition to produce oleyl oleate using immobilized CRL was found in our study and turned out to be molar ratio of 1, reaction temperature of 40 °C, and a 12-h reaction time to reach reaction equilibrium. Under the optimal reaction conditions, a high percentage yield of ester was achieved (92.6%). The immobilized CRL also reached a conversion rate of 86.7% with excellent stability even after 8 cycles.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Ruirui Li,Wei Zhuang,Yan Gao,Yahan Bai,Keke Zhang,Zhenfu Wang
Herein, UiO-66 was selected as the immobilization carrier of Rhizomucor miehei lipase (RML). After etching and hydrophobic modification, the functionalized UIO-66 (H-UIO-66-OPA) was utilized for RML immobilization and the obtained RML@H-UIO-66-OPA showed about 70 % relative activity after incubation at 60 °C, which was much better than RML (20 %). RML@H-UIO-66-OPA was used in the synthesis of 1,3-dioleic acid glycerol (1,3-DAG) and the effects of reaction conditions (temperature, enzyme addition, substrate molar ratio, and time) on 1,3-DAG yield were investigated. Under the optimal conditions (temperature of 65 °C, enzyme addition of 2 wt%, substrate molar ratio of 2:1, and reaction time of 4 h), 1,3-DAG yield reached 77 %. Finally, Box-Behnken experimental design method was utilized to optimize the process parameters for the preparation of 1,3-DAG, and the final 1,3-DAG content was 79.80 %, which demonstrated that the model could predict the relationship between the factors and be suitable for the process optimization in 1,3-DAG preparation.
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Biotechnology Journal
·
2024
·Vol. 19
·期 3
·2300615
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IF 3.2
Yifei Zhang,Wei Zhang,Guangzheng Ma,Binbin Nian,Yi Hu
Phytosterols usually have to be esterified to various phytosterol esters to avoid their disadvantages of unsatisfactory solubility and low bioavailability. The enzymatic synthesis of phytosterol esters in a solvent-free system has advantages in terms of environmental friendliness, sustainability, and selectivity. However, the limitation of the low stability and recyclability of the lipase in the solvent-free system, which often requires a relatively high temperature to induce the viscosity, also increased the industrial production cost. In this context, a low-cost material, namely diatomite, was employed as the support in the immobilization of Candida rugosa lipase (CRL) due to its multiple modification sites. The Fe 3 O 4 was also then introduced to this system for quick and simple separation via the magnetic field. Moreover, to further enhance the immobilization efficiency of diatomite, a modification strategy which involved the octadecyl and sulfonyl group for regulating the hydrophobicity and interaction between the support and lipase was successfully developed. The optimization of the ratio of the modifiers suggested that the -SO 3 H/C 18 (1:1.5) performed best with an enzyme loading and enzyme activity of 84.8 mg·g −1 and 54 U·g −1 , respectively. Compared with free CRL, the thermal and storage stability of CRL@OSMD was significantly improved, which lays the foundation for the catalytic synthesis of phytosterol esters in solvent-free systems. Fortunately, a yield of 95.0% was achieved after optimizing the reaction conditions, and a yield of 70.0% can still be maintained after six cycles.
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FOOD CHEMISTRY
·
2024
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IF 8.5
Tiefeng Yuan,Liping Wang,Linzhou Chen,Jinjian Zhong,Yuyang Lin,Yihan Wang,Chen Lin,Huajun Fan
In this study, an efficient approach to preparation of different anthocyanins from Purple-heart Radish was developed by combining microwave-assisted extraction (MAE), macroporous resin purification (MRP) and ultrasound-assisted acid hydrolysis (UAAH) for evaluation of physicochemical stability and pancreatic lipase (PL) inhibitory activity. By optimization of MAE, MRP and UAAH processes, the anthocyanins reached the yield of 6.081 ± 0.106 mg/g, the purity of 78.54 ± 0.62 % (w/w) and the content of 76.29 ± 1.31 % (w/w), respectively. With high-resolution UHPLC-Q-Orbitrap/MS, 15 anthocyanins were identified as pelargonins with diverse glucosides and confirmed by pelargonidin standard. By glycosylation, pelargonins exhibited higher stability in different pH, temperature, light, metal ions environments than that of pelargonidin. However, PL inhibitory assay, kinetic analysis and molecular docking demonstrated that pelargonidin had higher PL inhibitory activity than pelargonins even though with similar binding sites and a dose–effect relationship. The above results revealed that the effect of glycosylation and deglycosylation on PL inhibitory activity and physicochemical stability.
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ChemCatChem
·
2017
·Vol. 10
·期 5
·1166-1172
·
IF 4.803
Lan-Lan Lou,Huaxin Qu,Wenjun Yu,Bei Wang,Lezi Ouyang,Shuangxi Liu,Wuzong Zhou
Graphical Thermoresponsive lipase catalyst : A UCST-type thermoresponsive polymer–lipase conjugate was exploited and applied as an asymmetric biocatalyst in the kinetic resolution of racemic α-methylbenzyl butyrate, exhibiting high catalytic performance, easy recovery, and good durability. A thermoresponsive lipase catalyst with an upper critical solution temperature (UCST) of about 26 °C was exploited by covalent immobilization of an enzyme, Pseudomonas cepacia lipase (PSL), onto poly(acrylamide- co -acrylonitrile) by glutaraldehyde coupling. The experimental conditions for the PSL immobilization were optimized. The immobilized PSL was much more stable for wide ranges of temperature and pH than free PSL. The material was also evaluated as an asymmetric catalyst in the kinetic resolution of racemic α-methylbenzyl butyrate at 55 °C in an aqueous medium and exhibited high catalytic performance and stability. Up to 50 % conversion and 99.5 % product enantiomeric excess were achieved, thus providing highly pure enantiomers. This biocatalyst could be easily recovered by simple decantation for reuse based on temperature-induced precipitation. It showed good reusability and retained 80.5 % of its original activity with a well reserved enantioselectivity in the 6th cycle. This work would shed light on the future development of new UCST-type enzyme catalysts.
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BIOCHEMICAL ENGINEERING JOURNAL
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2022
·
IF 4.446
Jun Cao,Rong Wu,Feng Zhu,Qihui Dong,Erzheng Su
Non-aqueous biocatalysis has been expanding the application fields of biocatalysis and is playing an increasingly important role in industrial biocatalysis. Deep eutectic solvents (DESs) have been recognized as green reaction media of non-aqueous biocatalysis. To provide guidance for improving the catalytic performance of enzymes in pure DESs, Candida antarctica lipase B (CALB) catalyzed transesterification reaction was chosen as the model reaction to assess the catalytic efficiency in different series of pure DESs. The catalytic efficiency of CALB was strongly influenced by the properties of DESs. Hydrophobic DESs caused less inactivation of CALB than hydrophilic DESs. The highest yield in hydrophobic DESs reached 56.75% after 12 h. The amount of carboxyl group in hydrophobic DESs, the amount of hydroxyl group in hydrophilic DESs, and the length of carbon chain had positive impacts on the catalytic efficiency of CALB in DESs. Learning from the CALB behaviors in DESs, a preliminary attempt in rational design DESs for higher transesterification efficiency was provided. Except for reaction media, the catalytic activity of CALB in DESs was improved by medium engineering means and enzyme engineering measures, such as adding a trace amount of water, imprinting CALB with pH buffer or inorganic salt, and protecting CALB by lyoprotectants. Synergistic effect of multiple activation methods could also be observed in improving the catalytic efficiency. This study can provide insights into expanding the application of DESs in non-aqueous biocatalysis.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2026
·
IF 8.7
Yueling Shang,Jinhui Yi,Ying Fan,Shihaoran Xu,Xin Zhao,Xujia Dai,Xia Zhao,Yanli Liu,Jinbin Liu,Xiaohong Yu
In this study, sea buckthorn juice phenolics, free, bound, and conjugated fractions, were investigated for pancreatic lipase (PL) inhibition, and conjugated phenolics (CPs) were found to exhibit the highest inhibitory activity (IC50: 253.9 μg/mL pre-fermentation, 185.2 μg/mL post-fermentation). Fermentation modified the conjugated phenolic composition, upregulating 31 compounds and downregulating 18 compounds, notably protocatechuic acid and isorhamnetin derivatives. Importantly, kinetic analysis demonstrated a fermentation-induced shift in the inhibition mode from mixed-type (unfermented CPs [CCP]) to uncompetitive (fermented CPs [FCP]), suggesting its potential application as an adjunctive therapy. Spectroscopic studies indicated that CP-PL interactions occurred through static quenching and hydrophobic forces, with FCP inducing secondary structural perturbations in PL. Notably, FCP demonstrated synergistic effects with orlistat, suggesting its potential for combined therapeutic applications. These results highlight the value of sea buckthorn as a source of anti-obesity polyphenols and provide a mechanistic basis for the development of functional ingredients that target PL activity regulation. These findings suggest that fermented sea buckthorn phenolics are promising candidates for metabolic disorder interventions owing to their dual inhibition mechanism and structural modulation of PL.
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LWT-FOOD SCIENCE AND TECHNOLOGY
·
2025
·
IF 6.6
Guoying Fu,Lei Cai,Peihang He,Yan Wang,Yingqi Zhang,Enxue Xie,Liang Li,Zedong Zhang,Guoqiang Wu
A series of Candida antarctica lipase B (CALB) catalysts immobilized on two-dimensional planar ZSM-5 zeolite (denoted as x CAL/ZSM-5-P) were developed for the efficient and green esterification of capric acid (CA) and glycerol (Gly) to synthesize medium-chain glycerides (MCGs). Comprehensive characterizations, including X-ray diffraction, Fourier-transform infrared, scanning electron microscopy, transmission electron microscopy, N 2 physisorption, and thermogravimetric analysis, confirmed the successful immobilization and uniform dispersion of lipase of CALB on ZSM-5-P via sulfhydryl modification. The framework structure of ZSM-5-P remained structurally intact after immobilization. The CAL/ZSM-5-P catalysts exhibited outstanding catalytic performance in the esterification reaction. Notably, the 9CAL/ZSM-5-P catalyst achieved the highest CA conversion of 66.94 %, with nearly 100 % selectivity toward MCGs—substantially outperforming bare ZSM-5-P (without immobilized lipase), which showed only 0.19 % conversion. Additionally, 9CAL/ZSM-5-P demonstrated excellent catalytic stability and chemical robustness. A possible mechanism for the CALB/ZSM-5-P-catalyzed esterification of CA to MCGs was also proposed. This approach provides both theoretical insight and practical guidance for developing MCGs as food emulsifiers and functional oils via heterogeneous catalytic esterification using immobilized lipase in the food industry.
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FOOD RESEARCH INTERNATIONAL
·
2025
·
IF 8
Hui Zhang,Mengjia Xu,Ming Yang,Jun Ding,Mingquan Guo
The seeds of Cassia obtusifolia L. (Cassia seed) have long been utilized as an edible traditional Chinese medicinal herb and tea with various health benefits, including improving obesity and protecting eyesight. In this work, we developed a rapid screening method based on pancreatic lipase (PL)-functionalized magnetic composite nanoparticles coupled with ultra-performance liquid chromatography-quadrupole-time of flight mass spectrometry (UPLC-QTOF-MS/MS) and molecular networking analysis. This method utilized the advantages of polydopamine (PDA) and metal-organic frameworks (MOFs) functionalized magnetic core-shell structures (Fe 3 O 4 @PDA@MOFs MNPs), significantly enhancing the immobilization efficiency and performance of PL. The enzyme loading capacity was increased by 1.5-fold, and notable improvements in reusability and storage stability were also observed. By using this immobilized enzyme model in combination with UPLC-QTOF-MS/MS, 22 potential PL inhibitors were selectively screened and identified from the seeds of Cassia obtusifolia L. Molecular network analysis was innovatively introduced to improve the efficiency of compound identification by summarizing the similarity of mass spectral fragments. The inhibitory activities of three representative ligands of Cassiaside B, Biochanin A 7-glucoside and Aurantio-obtusin were further investigated. Molecular docking analysis revealed that the amino acid residue ASP249 in lipase contributes a significant role in the binding of active ligands to lipase. Overall, this proposed screening strategy, characterized by its specificity in enzyme binding and the convenience of functionalized magnetic separation, presents promising prospects for rapid and high-throughput screening of active components and drug candidates from natural resources.
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Food Bioscience
·
2026
·
IF 5.9
Liuyi Wei,Taoying Wu,Hao Wu,Li Wen,Bo Cui,Yunhui Cheng
Rice-derived peptides are a sustainable protein source with emerging lipid regulation functions. In this study, peptides with novel pancreatic lipase (PL) and cholesterol esterase (CE) inhibition from rice protein hydrolysates (RPHs) were identified by peptidomics. Then their alleviating effects and mechanisms on lipid accumulation in cells were investigated. 55 peptides were identified, showing significant enrichment of Phe, Pro, Arg, and Leu, with hydrophobic/polar amino acids at terminal positions. Among them, five peptides (WQ7, FR6, GF6, GA7, and GY7) exhibited potent inhibitory activity against PL and CE, with IC 50 values of 0.19-0.70 μg/mL and 0.22-0.25 μg/mL, respectively. Molecular docking studies revealed that five peptides bind stably to the active sites of PL (Phe77, Tyr114, Phe215, and His263) and CE (Ser194 and His435) through hydrogen bonding, PI-alkyl, and PI-PI interactions. Dynamic simulations demonstrated that three peptides (WQ7, FR6, and GF6) form stable complexes with both CE and PL, exhibiting strong binding affinity. In vitro study confirmed that these peptides reduced levels of TC, TG, and LDL-c while increasing HDL-c content, with WQ7 showing superior efficacy. Western blot and qPCR results indicated WQ7 regulated lipid metabolism by suppressing the PPARγ pathway and downregulating the protein expression of related factors, such as ACS, FASN, and SREBP-1c. This study showed that the WQ7, a multifunctional bioactive peptide, demonstrates direct enzyme-inhibitory activity and regulates core transcriptional pathways, providing theoretical support for utilizing rice protein in the development of lipid-lowering functional food.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2023
·
IF 8.2
Geling Kuang,Zichen Wang,Xiuyan Luo,Zixin Geng,Jiandong Cui,Muhammad Bilal,Ziyuan Wang,Shiru Jia
The hydrolysis of natural oils (vegetable oils and fats) by lipase has significant applications in food and medicine. However, free lipases are usually sensitive to temperature, pH and chemical reagents in aqueous solutions, which hinders their widespread industrial application. Excitingly, immobilized lipases have been widely reported to overcome these problems. Herein, inspired by lipase interface activation, a hydrophobic Zr-MOF (UiO-66-NH 2 -OA) with oleic acid was synthesized for the first time in an emulsion consisting of oleic acid and water, and the Aspergillus oryzae lipase (AOL) was immobilized onto the UiO-66-NH 2 -OA through hydrophobic interaction and electrostatic interaction to obtain immobilized lipase (AOL/UiO-66-NH 2 -OA). 1 H NMR and FT-IR data indicated that oleic acid was conjugated with the 2-amino-1,4-benzene dicarboxylate (BDC-NH 2 ) by amidation reaction. As a result, the V max and K cat values of AOL/UiO-66-NH 2 -OA were 179.61 μM﹒min −1 and 8.27 s −1 , which were 8.56 and 12.92 times higher than those of the free enzyme, respectively, due to the interfacial activation. After treated at 70 °C for 120 min, the immobilized lipase maintained 52 % of its original activity, but free AOL only retained 15 %. Significantly, the yield of fatty acids by the immobilized lipase reached 98.3 % and still exceeded 82 % after seven times of recycling.
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JOURNAL OF SEPARATION SCIENCE
·
2022
·Vol. 45
·期 23
·4198-4208
·
IF 3.614
Fu-Qin He,Guang-Zhen Wan,Juan Chen
As a traditional Chinese medicine, Schisandra chinensis has a potential weight-loss effect by delaying carbohydrate absorption and improving lipid metabolic disorders. However, its active components are still unclear and require in-depth research. In this study, the active components of Schisandra chinensis responsible for pancreatic lipase and alpha-glucosidase inhibitory activity were screened and identified based on a spectrum-effect relationship study in combination with ultra-performance liquid chromatography-tandem mass spectrometry analysis. The ultra-high-performance liquid chromatography fingerprints of 17 batches of Schisandra chinensis were established, and 14 common peaks were specified by similarity analysis. The half-maximal inhibition concentration values for pancreatic lipase and alpha-glucosidase inhibition were separately measured by enzymatic reactions. Using multivariate statistical methods including principal component analysis, partial least square analysis, and grey relational analysis, the correlation models between the peak areas of 14 common peaks and half-maximal inhibition concentration values were constructed, and the chromatographic peaks making a great contribution to efficacy were screened out. Peak1, Peak2, Peak4, Peak6, Peak9, Peak10, Peak11, and Peak13 were responsible for alpha-glucosidase inhibitory activity, while Peak1, Peak4, Peak6, Peak9, Peak10, and Peak11 for pancreatic lipase inhibitory activity. Finally, the 70% ethanol extracts of Schisandra chinensis were characterized by ultra-high-performance liquid chromatography-tandem mass spectrometry analysis, and 14 lignans were identified to further elucidate the active constituents of Schisandra chinensis . The positive results suggested the proposed strategy is simple and effective to screen active components from complex medicinal plants.
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