FOOD CHEMISTRY
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2026
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IF 9.8
Shengli Ding,Mengqi Wang,Guiqing Lin,Yanrong Song,Ji Zhang,Yufei Zhang,Mingming Zheng
Inspired by the natural crystal evolution trajectory of corals, this study introduces a mild two-step “defective pre-growth/crystallization” strategy to in situ encapsulate Candida antarctica lipase B (CaLB) within covalent organic frameworks (COFs). Rapidly formed amorphous polymer microspheres serve as the core skeletal structure. Upon enzyme adsorption onto their surfaces, these microspheres undergo crystalline readjustment to embed the enzymes and form a protective exoskeleton. The resulting CaLB@TPB-TFPB COF-I biocatalyst demonstrates superior thermal stability, organic solvent tolerance, and reusability compared to both free lipase and commercial Novozym 435. It achieves a 95.7% conversion rate for caproic acid esterification under anhydrous conditions and maintains over 90% conversion efficiency across seven consecutive cycles. This work also elucidates the multiple critical roles of water in enzymatic ester synthesis. This coral-inspired encapsulation approach leverages the tunable properties of COFs to enhance enzyme performance, offering an efficient solution for the biocatalytic synthesis of flavor esters.
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
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2017
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IF 3.154
Shi-Lin Cao,Xiao Deng,Pei Xu,Zi-Xuan Huang,Jian Zhou,Xue-Hui Li,Min-Hua Zong,Wen-Yong Lou
A novel deep eutectic solvent (DES)–DMSO cosolvent system has been, for the first time, successfully used as the reaction medium for the enzymatic acylation of dihydromyricetin (DMY) catalyzed by the immobilized lipase from Aspergillus niger (ANL). The cosolvent mixture, ChCl:Glycerol–DMSO (1:3, v/v) proved to be the optimal medium. With the newly developed cosolvent, the initial reaction rate of enzymatic acylation of DMY achieved 11.1 mM/h and the conversion of DMY was 91.6%. ANL@PD-MNPs is stable and recyclable in this cosolvent, offering 90% conversion rate after repeated use of 5 times. The lipid-solubility of DMY-16-acetate was 10 times higher than that of its raw materials DMY. The results showed that the DMY-16-acetate product exhibits good antioxidative activity. The present research illustrated that the use of DES–DMSO cosolvent may become a feasible alternative for the synthesis of DMY ester.
研究领域:
生物催化
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绿色化学
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酶工程
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药物化学
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天然产物化学
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ANALYTICA CHIMICA ACTA
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2026
·
IF 6
Mengxue Tang,Jiale Zhang,Qixuan Mu,Keyan Chen,Yibing Ji
Background Enantiomers may have differences in biological effects, pharmacological activity, and toxicity. Currently, global regulatory authorities are imposing increasingly stringent approval requirements for single-enantiomer drugs. Coupled with the continued growth of the chiral pharmaceutical market, this makes the development of chiral separation technology an urgent scientific task. Therefore, the separation and analysis of chiral drug enantiomers are directly related to human health. Enzyme-based chiral stationary phase (CSP) is a promising platform. Unfortunately, the fragility of natural enzymes, as well as the complexity and low efficiency of the preparation process, hinder their practical application in chiral separation. Results Metal organic frameworks (MOFs), which have enormous potential in the fields of enzyme immobilization and capillary electrochromatography (CEC) separation, were explored as support materials with good enzyme immobilization performance and CSP with separation abilities. Lipase (from porcine pancreatic) was encapsulated into a metal organic framework (MOF) under the concept of "in situ". Effective enzyme loading capacity enables composite materials (Lipase@HKUST-1) to inherit lipase's natural chiral recognition ability. On this basis, inspired by the same concept, Lipase@HKUST-1 was directly grown in the open column for capillary electrochromatography (CEC). By optimizing the interface combination method and simplifying the column preparation steps, the efficiency and performance of capillary column preparation have been effectively improved. Enantiomer separation of multi-chiral drugs such as naproxen and chlorpheniramine has been achieved. Theoretical calculations further explore potential chiral recognition mechanisms. Significance The effective combination of cost-effective lipase (from porcine pancreatic) and MOF materials enriches the library of chiral materials for enantioseparation. The understanding of the chiral recognition mechanism inspires the design of ideal performance materials. The highly stable MOF separation platform for biological functions has introduced a pioneering research paradigm for the CSP development of OT-CEC.
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Green Synthesis and Catalysis
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2026
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IF 7
Siqi Zhu,Jie Sheng,Yuhan Li,Kunyi Tong,Chunjie Wu,Chenhao Zhang,Hui Li
Enzymes catalyze stereoselective transformations under mild conditions, yet their industrial deployment remains constrained by intrinsic fragility, poor recyclability, and prohibitive cost. While immobilization on solid carriers can circumvent these limitations, conventional methods suffer from enzyme leaching or diffusional barriers. Covalent organic frameworks (COFs) offer an ideal solution by combining high surface area, tunable pore environments, and robust covalent linkages; however, the narrow pore apertures of conventional two-/three-dimensional scaffolds (< 2 nm) preclude efficient loading of enzymes whose hydrodynamic diameters typically exceed 5 nm. Here we demonstrate that a one-dimensional, pyrene–phenanthroline COF (PhenCOF) overcomes this steric mismatch by presenting densely distributed, surface-exposed imine groups that serve as anchoring points for covalent enzyme attachment. Candida antarctica lipase B (CALB) was immobilized via an Ugi-type three-component reaction to afford CALB@PhenCOF. The resultant hybrid exhibits exceptional catalytic performance in the kinetic resolution of racemic 1-phenylethanol, achieving 99% conversion, 2.4-fold higher than free CALB. The 1D architecture and hydrophobic microenvironment facilitate substrate diffusion while stabilizing the enzyme's active conformation, as evidenced by retention high activity under wide pH ranges, extreme organic solvents, and temperatures up to 140°C. Notably, covalent immobilization endows unparalleled recyclability, with 95% efficiency maintained over 10 cycles. This work establishes 1D COFs as a paradigm for promising enzyme carriers, merging atomic precision with industrial robustness to address longstanding challenges in biocatalysis.
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SENSORS AND ACTUATORS B-CHEMICAL
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2023
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IF 8.4
Jinpeng Liu,Mashooq Khan,Yong Wei,Anna Liu,Tao Wang,Qiongzheng Hu,Li Yu
High-throughput screening of lipase inhibitors is critical for developing anti-obesity drugs. Herein, a robust and versatile sensing platform based on the difference in the sliding time of droplets on liquid crystal-infused porous surfaces (LCIPS) is developed to detect lipase inhibitors. Lipase catalyzes glycerol trioleate (GT) to produce oleate that can adsorb at the solution/liquid crystal (LC) interface due to its high amphiphilicity, which impedes the sliding of droplets on LCIPS, resulting in an extended sliding time. However, in the presence of lipase inhibitors, the enzymatic hydrolysis of GT by lipase is inhibited, which shortens the sliding time. The screening of three lipase inhibitors, orlistat, cetilistat, and epigallocatechin gallate (EGCG), popular anti-obesity drugs, is demonstrated to have IC 50 values of 17.45 ± 3.15 nM, 72.15 ± 6.32 nM, and 2.19 ± 0.24 μM, respectively. This study provides a simple, inexpensive, portable, user-friendly, and instrument-free method for rapid, accurate, and high-throughput screening of lipase inhibitors. The LCIPS-based sensing platform is up-and-coming in developing advanced bioanalytical sensors.
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COMPOSITES SCIENCE AND TECHNOLOGY
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2023
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IF 9.1
Ge Tang,Kuaqian Deng,Panyang Li,Jiali Huang,Fanglin Dao,Hao Jiang,Jing Wang,Jianfang Jiang
Carrier, immobilization method and conditions are the most important factors affecting the performance of immobilized lipase . In this study, [email protected] is successfully prepared via an improved hydrothermal method combined with ion condensation. Then, we creatively adopt one-pot method, combining electrostatic adsorption with chemical crosslinking , to prepare lipase-nanocatalyst with excellent performance under mild conditions. [email protected] and lipase-nanocatalyst are characterized by FTIR, SEM, HRTEM , CLSM, CD, etc, the optimal conditions are explored in detail too. Lipase-nanocatalyst is 189 nm, and the loading ratio of free lipase is up to 67.6%. Compared with free lipase, specific activity is increased by 2.9 times, and it also broadens toleration to pH, thermal, organic solvents . In addition, lipase-nanocatalyst exhibits high storage stability and reusability . The residual activity is approximately 92.3% after the 10th recycle, and the cumulative catalytic activity is 13.4 times than that of free lipase. Finally, lipase-nanocatalyst is used to synthesize ethyl levulinate, with a production ratio of 68.6% for the first recycle, and the total output of EL is 12.9 times than that of free lipase after ten cycles. Thus, our findings provide a foundation for lipase-nanocatalyst showing several attractive features, such as easy preparation, excellent catalytic activity, good stability and reusability.
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Foods
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2023
·Vol. 12
·期 6
·1289
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IF 5.2
Xiao-Yan Liu,Wei Chen,Cheng-Tao Wang
Egg white (EW) is frequently used in bakery products because of its excellent foaming capabilities. However, egg yolk (EY) contamination often degrades the foaming characteristics of EW. The purpose of this study was to investigate the effect of different concentrations of phospholipase A1 (PLPA1) and lipase (LP) on EW. The changes in particle size distribution and potential before and after enzymatic digestion of EW with contaminated 0.5 wt% and 1.0%wt EY were tested. The foaming rate and foam stability were measured after the dispersions were digested with different concentrations of PLPA1 and LP. Additionally, the dispersion samples were used to prepare batter and angel cake, and the modulus, density, and microstructure of the batter were analyzed. Results showed that the potential absolute value increased when the EY was hydrolyzed by PLPA1. The distribution of yolk particle size showed a new aggregation and the average particle size decreased after LP hydrolysis. The dispersion samples hydrolyzed by PLPA1 and LP recovered all the properties of the samples at enzymatic concentrations of 500 U/g and 2500 U/g. This may be attributed to the changes in yolk particles resulting from the enzymatic digestion of EY and the production of amphiphilic lysophospholipids, fatty acids, and glycerol.Keywords:egg white;foaming properties;yolk-contaminated;lipase enzymolysis
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ANALYTICAL CHEMISTRY
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2022
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IF 8.008
Shuang Xia,Fangchao Yin,Lulu Xu,Binglu Zhao,Wenli Wu,Yaohong Ma,Jin-Ming Lin,Yulin Liu,Mei Zhao,Qiongzheng Hu
Human pancreatic lipase is a symbolic biomarker for the diagnosis of acute pancreatitis, which has profound significance for clinical detection and disease treatment. Herein, we first demonstrate a paper-based lipase sensor via a phase separation-induced viscosity change. Lipase catalyzes triolein to produce oleic acid and glycerol. Adding an excess of Ca2+ produces calcium oleate. The remaining Ca2+ binds with sodium alginate, triggering hydrogelation with an “egg-box” structure. The viscosity change of the aqueous solution induced by the phase separation process can be quantified by measuring the solution flow distance on a pH test paper. The paper-based lipase sensor has high sensitivity with a detection limit of 0.052 U/mL and also shows excellent specificity. Additionally, it is also utilized for quantitative lipase analysis in human serum samples to exhibit its potency in acute pancreatitis detection. This method overcomes the drawbacks of low sensitivity, slow response, and poor reproducibility caused by the nonuniform distribution of the highly viscous hydrogel on the sensing interface in existing approaches. In conclusion, thanks to the prominent characteristics of high portability, low cost, and easy operation, it is prospective for simple quantitative detection of lipase and has great potential for commercialization.
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ACS Applied Materials & Interfaces
·
2022
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IF 10.383
Qi Zeng,Mengmeng Sun,Xin Xie,Yuli Zhang,Haoyue Hou,Xingyuan Fang,Ting Guo,Hao Yuan,Tao Meng
Pickering interfacial biocatalysis (PIB) paves the way for efficient enzymatic catalysis in the biphasic system. However, the Pickering interfacial biocatalysts located on the oil–water interface still face the inevitable deactivation when one of the phases contains the reactant that inactivates the enzyme. Herein, the positioning of lipase-entrapped colloidosomes (LECs) at the emulsion interface is rationally designed by physically tuning the wettability, which allows LECs to protrude into the selected phase to protect the lipase away from the damage of the reactant. As a proof of concept, LECs with different positioning at the interface are used as Pickering interfacial biocatalysts to produce biodiesel by esterification of lauric acid and methanol. Impressively, the LECs that protrude into the oil phase possess an optimal catalytic performance to protect more lipases away from the damage of the reactant of short-chain alcohol, which shows an 8.18-fold enhancement in specific activity relative to the free lipase, reach a biodiesel yield of 80.37% after 8 h, and retain the 96.44% of relative activity after 10 cycles. This study provides a novel and robust platform for Pickering emulsion-enhanced biocatalysis.
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Reaction Chemistry & Engineering
·
2023
·Vol. 8
·期 9
·2365-2374
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IF 3.9
Hongbo Suo,Qi Qi,Xusheng Dai,Xinyue Geng,Qi Li,Jie Yang,Guoyun Liu,Renmin Liu,Lili Xu
Recently, ionic liquids (ILs) have shown potential in enzyme activation and stabilization. In this work, ILs consisting of imidazolium-based cations coupled with [Tf2N]− anions were grafted onto a magnetic Ca2+-based metal–organic framework (CaBDC), and the composites were then employed to immobilize lipase. The support of ILs/MCaBDC and immobilized porcine pancreatic lipase (PPL) of PPL-ILs/MCaBDC were thoroughly characterized and fully investigated. Compared with a wild enzyme, PPL-ILs/MCaBDC showed 2.16 times higher activity. After introducing the ILs into the supports, PPL-ILs/MCaBDC showed enhanced thermal, storage, and stability properties compared with PPL–MCaBDC. After 10 cycles, PPL-ILs/MCaBDC retained a higher (83.2%) fraction of its initial activity than PPL–MCaBDC (73.4%). Furthermore, the relationship between the support–enzyme interactions and the structural changes of immobilized lipase was also analyzed in detail. Application of circular dichroism (CD) spectroscopy analysis helped us understand the changes of the enzyme secondary structure. Therefore, this work further confirmed the effectiveness of ILs for enzyme immobilization.
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LWT-FOOD SCIENCE AND TECHNOLOGY
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2022
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IF 6.056
Liqi Wang,Hairong Zhang,Ziyue Li,Jiayao Qu,Kaiwen Xing,Minghao Wang,Cuiping Han,Zeguo Qiu,Dianyu Yu
In recent years, photoelectrochemical (PEC) biosensors have shown great application prospects in biological analysis and food detection. In this work, we developed and tested a new PEC biosensor. Three-dimensional graphene oxide (3DGO) was generated and deposited on an indium tin oxides (ITO) electrode. The photoelectrically active poly[Nile blue] (PNb) was formed on this electrode by electropolymerization, and glycerol dehydrogenase (GDH) was immobilised to generate the GDH-PNb-3DGO-ITO biosensor. This newly developed PEC biosensor exhibited excellent photoelectric response to lipase activity under light conditions, with a detection range of 0.1–6 U/mL and a lower detection limit of 0.069 U/mL. When the GDH-PNb-3DGO-ITO sensor was used for PEC detection of lipase activity by the standard addition recovery method, the recovery rate of the standard addition was 98.68–105.41%, and the relative standard deviation (RSD) was 2.1–3.5%, with good storage stability and repeatability. Therefore, this work provides new ideas for the design and preparation of PEC biosensors and introduces a new detection method for monitoring lipase activity.
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Journal of Oleo Science
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2022
·
IF 1.628
Lihong He,Jiawei Zheng,Siting Feng,Li Xu,Nanjing Zhong
In this study, lipase A from Candida antarctica (CALA) was immobilized onto the macroporous resin NKA-9. Immobilization conditions (pH, time and CALA concentration) were studied, enzymatic activity and immobilization efficiency (IE) up to 968.89 U/g and 53.19% were respectively obtained under optimal conditions (immobilization pH 5.0, time 5 h and CALA concentration at 30 mg/mL). Then, the NKA-9 supported CALA (CALA@NKA-9) samples were used to catalyze glycerolysis in solvent-free system. With 0.25 g of the present CALA@NKA-9 (soybean oil 3.52 g and glycerol 0.184 g) and after 12 h reaction at 50 °C, diacylglycerols (DAG) content up to 64.37% and triacylglycerols (TAG) conversion at 83.33% were obtained. The relationship between temperature and TAG conversion was LnV 0 = 13.9310-6.4212/T for CALA@NKA-9. Meanwhile, the activation energy (Ea) of CALA@NKA-9 was calculated to be 53.39 kJ/mol. In addition, reusability in the glycerolysis reaction was also evaluated, and 57.82% of the initial glycerolysis activity was retained after 9 consecutive applications. Furthermore, the CALA@NKA-9 was also used to catalyze the esterification (esterification of fatty acids with glycerol), however, the present CALA@NKA-9 cannot initiate the esterification. Therefore, the present CALA@NKA-9 is shown to be potential for DAG production through glycerolysis reaction.
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