Food Bioscience
·
2026
·
IF 6.2
Yiyi Lin,Xiansi Gao,Zheling Zeng,Di Kuang,Kai Fang,Tianyi Song,Ping Yu,Deming Gong,Cheng Zeng,Xianghui Yan
Medium- and long-chain triglycerides (MLCT) are a novel type of functional lipids that exhibit higher bioavailability when long-chain polyunsaturated fatty acids are esterified at the sn-2 position of the glycerol backbone. Enzyme-catalyzed synthesis of MLCT offers significant advantages, including environmental benignity, exceptional catalytic efficiency, and negligible by-product formation. Nevertheless, the inherent limitations of free enzymes in terms of recyclability and industrial implementation, remain a challenge. In this study, the hydrophobicity of the amino resin support LX-1000HAA (HAA) was modified via grafting with dodecenyl succinic anhydride (DDSA). The lipase RM was then immobilized onto the HAA-DDSA carrier via physical adsorption. The activity of the resulting immobilized lipase HAA-DDSA-RM was 1.74 times that of Lipozyme RM C and 2.13 times that of HAA-RM. Analysis of the adsorption kinetics and isotherms for lipase adsorption onto HAA-DDSA revealed that the adsorption behavior conformed to both the pseudo-second-order kinetic model and the Freundlich isotherm model. HAA-DDSA-RM was then employed in the preparation of MLCT in the reaction system comprising algal oil and capric acid. The DHA content at the sn-2 position reached 73.40% in the final product. Moreover, HAA-DDSA-RM demonstrated outstanding thermal stability, good storage stability, and superior recyclability, with 96% of its initial activity after 10 successive operational cycles. This study may provide a new approach for environmentally sustainable production of functional lipids by developing a robust immobilized lipase system.
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JOURNAL OF BIOTECHNOLOGY
·
2026
·
IF 4
Renmin Liu,Tiantian Jia,Hanbing Song,Zhenhui Yu,Chaoqi Lin,Qingchun Yang,Ziyuan Ye,Yaqi Wang,Yanwen Wang,Hongbo Suo
L -histidine ionic liquid modified magnetic COF was successfully fabricated. • Covalent modification of supports with IL optimized the enzyme microenvironment. • Introduction of IL enhanced the activity and stability of immobilized lipase. • IL boosted lipase-substrate affinity and catalytic efficiency. • Magnetic responsiveness improved the separation efficiency of immobilized lipase. This study proposes an innovative immobilized lipase construction strategy to address the low activity and poor stability limitations of current biocatalysts for flavor ester synthesis. L -histidine-based ionic liquid (IL) is covalently grafted onto the surface of magnetic covalent organic framework (COF) via Schiff base reaction, and porcine pancreatic lipase (PPL) is further covalently immobilized on the composite carrier through amide bond coupling. The resulting Fe₃O₄@COF-IL-PPL shows 1.6-fold higher catalytic activity and 2.3-fold better thermal stability than free PPL, and 32% higher activity retention after cycles than PPL immobilized on IL-free COF carrier. Its optimal reaction pH and temperature are 7.5 and 50 °C respectively, maintaining 86% of initial activity at 60 °C and 76% activity after 6 h incubation at 50 °C. Under n-hexane reaction system, the isoamyl acetate yield reaches 87.4% under optimal conditions, and the biocatalyst retains 71.4% activity after 10 consecutive isoamyl acetate synthesis cycles. Although the additional preparation steps and higher cost of the support need to be considered for industrial applications, the improved catalytic performance of Fe 3 O 4 @COF-IL-PPL verified the effectiveness of IL surface modification strategy, and the system can be further extended to solvent-free systems to verify its broader applicability.
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Journal of Materials Chemistry B
·
2023
·Vol. 11
·期 6
·1302-1311
·
IF 7
Hongbo Suo,Huining Geng,Lu Zhang,Guoyun liu,Hui Yan,Rui Cao,Jiahao Zhu,Yi Hu,Lili Xu
Enzymatic esterification plays an important role in the fields of chemistry and biotechnology. In this study, lipase was immobilized on an ionic liquid (IL)-modified magnetic metal–organic framework (MOF) and used to synthesize isoamyl acetate. The immobilized lipase (PPL-ILs/Fe3O4@MOF) showed 2.1-fold and 1.8-fold higher activity compared to the free and immobilized lipase without ILs (PPL-Fe3O4@MOF), respectively. In addition, the anti-denaturant ability and reusability of the PPL-ILs/Fe3O4@MOF were also higher than those of other samples. The ester yield reached 75.1% when the biocatalyst was used to synthesize isoamyl acetate in hexane. The synthesized supports supplied a good microenvironment for the immobilized lipase through multiple interactions. Results of the structural analysis showed that the conformation state of lipase molecules changed after immobilization. The magnetism of the prepared biocatalyst makes it easy to recycle so that PPL-ILs/Fe3O4@MOF maintained 70.2% of the initial activity after eight cycles. The prepared composite materials exhibited good potential in lipase immobilization with enhanced catalytic ability and stability.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2023
·
IF 8.2
Peiyi Jin,Linzhou Chen,Jinjian Zhong,Tiefeng Yuan,Lin Gan,Jilong Huang,Liping Wang,Huajun Fan,Chen Lin
Dioscoreae nipponica Makino ( D. nipponica ) as the rhizome of dioscoreaceae rich in steroidal saponins, has been reported to have the hypolipidemic effects etc. However, it is still unclear which exact active components are primary responsible for the beneficial effects. This study was conducted to fish out the lipase inhibitors from D. nipponica , and evaluate the inhibitory activity on porcine pancreatic lipase (PPL) through in vitro kinetic assay using p -nitrophenyl palmitate as substrate. Accordingly, the ethanolic extract was subjected to D101 macroporous resin purification for spectrophotometric screening, high performance liquid chromatography (HPLC) separation and structural characterization by ultra-performance liquid chromatography-quadrupole time-of-flight mass spectrometry. Through orlistat validation, the PPL inhibitory activity and IC 50 value of the extract were respectively 68.34 ± 1.47 % and 107.05 μg/mL under the optimized inhibition conditions. From 6 steroidal saponins identified, the inhibitory components named the protodioscin, protogracillin, dioscin and gracillin were fished out by grouping separation and HPLC analysis. Furthermore, dioscin and gracillin with the parent structure of diogenin were confirmed as the major inhibitors by virtue of stability tests based on transformation of protodioscin and protogracillin. Finally, the inhibitory mechanism of the major inhibitors toward PPL was further clarified by kinetic analysis and molecular docking analysis. The proposed method not only revealed the PPL inhibitory components in D. nipponica , but also provided an effective approach to hierarchical screening of PPL inhibitors from natural plants.
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CHEMICAL ENGINEERING JOURNAL
·
2023
·
IF 15.1
Xiaohai Yan,Xinru Dong,Qiannan Zhao,Gengan Du,Qi Guo,Yahong Yuan,Tianli Yue
Patulin (PAT) is a mycotoxin synthesized by fungi such as Penicillium expansum . It has become a key risk indicator in fruit juices and therefore needs to be removed. Here, we used an ex-situ method and a self-assembly strategy to prepare a green carboxymethyl cellulose@hierarchical mesoporous zirconium metal–organic framework-cysteine/porcine pancreatic lipase (CMC@HMMOF-Cys/PPL) aerogel for the safe and efficient removal of PAT from apple juice. The optimal CMC@HMMOF-Cys/PPL aerogel exhibited high adsorption capacity (38.41 μg/mg), excellent degradation capacity (28.68 μg/mg at 10 μg/mL PAT), good reusability and storage stability, and improved selectivity. Notably, it could be customized as a filler for flow reactors to achieve the safe and efficient removal of PAT from apple juice. More importantly, the CMC@HMMOF-Cys/PPL aerogel designed did not have a significant effect on the quality of apple juice. The present study provided a new method for removing PAT from apple juice and further expanded the real-world applications of MOFs.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2021
·
IF 6.953
Junxin Zhao,Shichang Liu,Yifang Gao,Maomao Ma,Xianghui Yan,Ding Cheng,Dongman Wan,Zheling Zeng,Ping Yu,Deming Gong
Enzymatic degradation has become the most promising approach to degrading organic ester compounds. In this study, Bacillus licheniformis NCU CS-5 was isolated from the spoilage of Cinnamomum camphora seed kernel, and its extracellular lipase was purified, with a specific activity of 192.98 U/mg. The lipase was found to be a trimeric protein as it showed a single band of 27 kDa in SDS-PAGE and 81 kDa in Native-PAGE. It was active in a wide range of temperatures (5–55 °C) and pH values (6.0–9.0), and the optimal temperature and pH value were 40 °C and 8.0, respectively. The enzyme was active in the presence of various organic solvents, metal ions, inhibitors and surfactants. Both crude and purified lipase retained more than 80% activity after 5 h in the presence of commercial detergents, suggesting its great application potential in detergent industry. The highest activity was found to be towards medium- and long-chain fatty acids (C 6 -C 18 ). Peptide mass spectrometric analysis of the purified lipase showed similarity to the lipase family of B. licheniformis . Furthermore, it degraded more than 90% 2,4-D butyl ester to its hydrolysate 2,4-D within 24 h, indicating that the novel lipase may be applied to degrade organic ester pesticides.
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3 Biotech
·
2020
·Vol. 10
·期 12
·1-9
·
IF 1.798
Zhang Jun,Tian Miao,Lv Pengmei,Luo Wen,Wang Zhiyuan,Xu Jingliang,Wang Zhongming
Long-chain fatty acids are widely used in food and chemical industries, and the enzymatic preparation of fatty acids is considered an environmentally friendly process. In the present study, long-chain fatty acids were prepared by the enzymatic hydrolysis of rapeseed oil with a genetically engineered lipase. Because thermophilic lipase has strong stability at higher temperatures, it was more suitable for the industrial production of long-chain fatty acids. Therefore, the thermophilic lipase BTL2 from Geobacillus thermocatenulatus was efficiently expressed in E. coli BL21(DE3) cells with an enzyme activity of 39.50 U/mg followed by gene codon optimisation. Experimental results showed that the recombinant lipase BTL2 exhibited excellent resistance to certain organic solvents ( n -hexane, benzene, ethanol, and butanol). The metal cation Ca 2+ and the non-ionic surfactant Triton-100X enhanced enzyme activity by 7.36% and 56.21% respectively. Moreover, the acid value of the liberated long-chain fatty acids by hydrolysing rapeseed oil was approximately 161.64 mg KOH/g at 50 °C in 24 h, the hydrolytic conversion rate was 91.45%, and the productivity was approximately 6.735 mg KOH/g h. These results suggested that the recombinant lipase BTL2 has excellent hydrolytic performance for rapeseed oil and showed great potential for the enzymatic preparation of long-chain fatty acids.
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JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2020
·Vol. 100
·期 12
·4565-4574
·
IF 2.614
Zhaoxian Huang,Zhenyu Cao,Zengwang Guo,Liang Chen,Zhongjiang Wang,Xiaonan Sui,Lianzhou Jiang
BACKGROUND Medium- and long- chain triacylglycerols (MLCTs) are functional structural lipids that can provide the human body with essential fatty acids and a faster energy supply. This study aimed to prepare MLCTs rich in α -linolenic by enzymatic interesterification of perilla oil and medium-chain triacylglycerols (MCTs), catalyzed by Lipozyme RM IM, Lipozyme TL IM, Lipozyme 435, and Novozyme 435 respectively. RESULTS The effects of lipase loading, concentration of MCTs, reaction temperature, and reaction time on the yield of MLCTs were investigated. It was found that the reaction achieved more than a 70% yield of MLCTs in triacylglycerols under the conditions of 400 g kg −1 MCTs and 60 g kg −1 lipase loading after equilibrium. A novel two-stage deodorization was also applied to purify the interesterification products. The triacylglycerols reach over 97% purity in the products with significant removal ( P < 0.05) of the free fatty acids, and the trans fatty acids were strictly controlled at below 1%. There was more than 40% α -linolenic in the purified products, with long-chain fatty acids mostly occupying the desired sn -2 position in acylglycerols, which are more active in hydrolysis. CONCLUSION A series of novel α -linolenic acid-rich medium- and long-chain triacylglycerols was prepared. Under appropriate reaction conditions, the yield of MLCTs in triacylglycerols was above 70%. A novel two-stage deodorization can be used to promote the elimination of free fatty acids and limit the generation of trans fatty acids. © 2020 Society of Chemical Industry
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FOOD CHEMISTRY
·
2021
·
IF 7.514
Ruiguo Cui,Long Xu,Dongming Lan,Bo Yang,Yonghua Wang
Our study offers a novel sn -1,3 specific lipase MAJ1 from marine member Janibacter sp. strain HTCC2649 for preparing long-medium-long (LML) type structured triacylglycerols (TAGs). Firstly, the resin ECR1030 was selected as a suitable support for the immobilization of lipase MAJ1. An efficient synthesis of LML-type structured TAGs by the immobilized lipase MAJ1-catalyzed interesterification of methyl palmitate and tricaprylin was studied in a solvent-free system. The reaction conditions, including substrate molar ratio, temperature and enzyme loading, were optimized. Under the optimum conditions (immobilized lipase MAJ1 of 45 U/g, substrate molar ratio of 4:1, temperature of 35 °C, reaction time of 24 h), the structured TAGs with double long chains (DLCST) were obtained in a yield of 44.3 mol%. Secondly, multi-dimensional mass spectrometry-based shotgun lipidomics (MDMS-SL) was employed to quantify each TAG positional isomer in DLCST. The content of 1,3-dipalmitoyl-2-capryloyl- sn -glycerol in DLCST was 97.6% determined by the MDMS-SL technology.
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AMB Express
·
2018
·Vol. 8
·期 1
·1-12
·
IF 1.719
Hu Xingcui,Cheng Tao,Liu Jianhua
Biosurfactants emulsify lipids, facilitating their exposure to microorganisms in water. Secretion of biosurfactant together with lipase can enhance oil assimilation by microorganisms. In this study, we show the analysis of the biosurfactant and lipase producing microbe originating from oil-sludge. The enrichment of the biosurfactant-producing ZS6 strain from the mixed culture of sludge-derived microbes in medium with olive oil as sole carbon source was monitored using the modified T-RFLP (or mT-RFLP) methodology. Phylogenetic tree analysis based on 16S rDNA sequences suggested that ZS6 belonged to a member of Serratia sp. Serratia sp. ZS6 secreted both a serrawettin-type biosurfactant and lipase in medium with olive oil as sole carbon source. By using an in-gel lipase assay followed by LC–MS/MS analysis, we identified the amino acid sequences of the ZS6 lipase, which belonged to the lipase subfamily III of the family I. Its lipolytic activity was found to be enhanced by salinity, calcium, and methanol. Together, we show that the novel isolate Serratia sp. ZS6 secretes both biosurfactant and lipase which makes it useful for applications such as in food industry wastewater treatment and biodiesel production.
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RSC Advances
·
2014
·Vol. 4
·期 49
·25983-25992
·
IF 3.708
Jun Liu,Wenjing Wang,Huiwen Liu,Yaoliang Zhou,Haibo Zhang,Xiaohai Zhou
Herein, amino-epoxy supports were innovatively imported onto magnetic nanoparticles (Fe3O4–polymer hybrid nanospheres) for immobilizing enzymes. This new support has a coating layer with dual functional groups (epoxy and amino-epoxy). Consequently, this support has great anionic exchange power and a high number of epoxy groups. The acquired immobilized Penicillium expansum lipase in combination with this heterofunctional support represents a novel class of heterogeneous catalyst towards the synthesis of 1,3-dibutylurea from ethylene carbonate and butylamine, which has not been very commonly catalyzed by enzymes. After optimization of the reaction conditions, the yield of 1,3-dibutylurea was 77% under solvent free conditions at 60 °C. Moreover, after completion of reaction, the catalyst was simply recovered by an external conventional magnet and recycled without significant loss in the catalytic activity (up to ten cycles).
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DRUG DELIVERY
·
2016
·
IF 4.843
Li-hua Luo,Pin-jing Zheng,Hua Nie,Yu-chao Chen,Dan Tong,Jin Chen,Yi Cheng
The purpose of this study is to synthesize a novel galactosylated cholesterol derivative, cholesterol-diethenyl decanedioate-lactitol (CHS-DD-LA) through lipase-catalyzed esterification in non-aqueous and to evaluate the preparation, pharmacokinetics and biodistribution of docetaxel (DOC) liposomes modified with CHS-DD-LA (G-DOC-L), which may actively gather at the liver compared with the conventional DOC liposomes (DOC-L) and commercial dosage form of DOC injection (DOC-i). A rapid and simple liquid chromatography-tandem mass spectrometry (LC-MS/MS) assay was developed for the determination of the DOC concentration in plasma and tissues with Taxol as the internal standard (IS). To measure the liver-targeting effect of the G-DOC-L, relative uptake rate (Re), peak concentration ratio (Ce), targeting efficiency (Te) and relative targeting efficiency (RTe) were reduced as the evaluation parameters. The results showed that the entrapment efficiency, particle size and Zeta potential of G-DOC-L was 76.8 ± 3.5%, 95.6 nm and 27.19 mV, respectively. After i.v. administration at the dose of 2.5 mg/kg in rats, a decrease in the AUC, MRT and an increase in CL (p < 0.05) were observed in the G-DOC-L group compared with DOC-L. All these results suggested that galactose-anchored liposomes could rapidly be removed from the circulation in vivo. The tissue distribution of G-DOC-L was widely different from that of DOC-L. The Re of G-DOC-L, DOC-L on liver was 4.011, 0.102; Ce was 3.391, 0.111; Te was 55.01, 3.08, respectively, demonstrating that G-DOC-L had an excellent effect on liver-targeting, which may help to improve the therapeutic effect of hepatic diseases.
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