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FOOD CHEMISTRY · 2021 · IF 7.514

Binding mechanism and functional evaluation of quercetin 3-rhamnoside on lipase

Di Wu,Ran Duan,Lan Tang,Xia Hu,Fang Geng,Qiaomei Sun,Yin Zhang,Hui Li

The interaction between lipase and quercetin 3-rhamnoside was studied by fluorescence spectroscopy, enzyme kinetics, and molecular dynamics simulation. The results showed that quercetin 3-rhamnoside had a strong quenching effect on the intrinsic fluorescence of lipase. The binding constant decreased with increasing temperature, and the number of binding sites approached 1. Thermodynamic parameters indicated that hydrogen bonding and van der Waals forces are the dominant forces when the interaction occurs. Circular dichroism spectroscopy and infrared spectroscopy proved that the ligand perturbed the structure of lipase. Enzyme kinetics results showed that quercetin 3-rhamnoside inhibited lipase, and the inhibitory effect was dose-dependent. Molecular dynamics simulation further explained the interaction mechanism and inhibitory effect. This study confirmed the inhibitory effect of quercetin 3-rhamnoside on lipase explained their binding mechanism, which will contribute to guiding the development of fat-reducing functional foods.

CAS / MDL: 522-12-3
研究领域: 生物化学 · 营养学 · 药理学
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CATALYSIS LETTERS · 2019 ·Vol. 150 ·期 5 ·1268-1276 · IF 2.372

Lipase-Catalyzed Highly Efficient 1,6-Conjugated Addition for Synthesis of Triarylmethanes

Yang Zeng-Jie,Wang Na,He Wei-Xun,Yu Yuan,Gong Qing-Tian,Yu Xiao-Qi

Lipase from porcine pancreas (PPL) is first reported to catalyze direct 1,6-conjugated addition for synthesis of triarylmethanes using p -quinonemethides ( p -QMs) and 2-naphthols. The catalytic activity of PPL was evaluated through investigating the solvent, the ratio of substrates, the enzyme loading and the temperature of the enzyme-catalyzed reactions. The present method proves to be environmentally friendly and efficient in terms of high yield, green catalyst and simple synthesis method. GraphicAbstract

CAS / MDL: 9048-46-8 9002-07-7
研究领域: 生物化学 · 有机合成 · 酶催化
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BIOCHEMICAL ENGINEERING JOURNAL · 2019 · IF 3.371

Virus-like organosilica nanoparticles for lipase immobilization: Characterization and biocatalytic applications

Yanjun Jiang,Huan Liu,Lihui Wang,Liya Zhou,Zhihong Huang,Li Ma,Ying He,Lujing Shi,Jing Gao

Hydrophobic virus-like organosilica nanoparticles (VOSNs) with a spherical core formed by mesoporous organosilica surrounded by epitaxial perpendicular nanotubes were successfully synthesized for the first time. These hydrophobic VOSNs were used for the immobilization of the lipase B from Candida antarctica (CALB) via covalent binding method, where glutaraldehyde was used as a spacer to form covalent bonds connect between the enzyme and support. Under optimized immobilization conditions, the specific hydrolytic activity which determined via the hydrolysis of p-NPP was 23200 U/g support , and the maximum CALB loading was 115.6 mg/g support . Compared to virus-like silica nanoparticles (VSNs), the hydrophobic VOSNs protected the CALB active conformation from a hazardous external environment due to stronger hydrophobic interactions between the VOSNs and CALB molecule. Thus, compared with CALB@VSNs and free lipase, CALB@VOSNs exhibited better pH, thermal stability, organic solvents tolerance and storage stability. The CALB@VOSNs was used to catalyze the esterification reaction of levulinic acid (LA) and n-lauryl alcohol, which was optimized by a response surface method. Under the optimal conditions (temperature, 51.2 °C; LA: n -lauryl alcohol, 1:11.5; time, 22.6 h), the CALB@VOSNs still retained 75.7% of the LA conversion, whereas the N435 only retained 29.8% of the conversion after 9 cycles. These results showed that hydrophobicity VOSNs could be an efficient support to prepare immobilized enzymes as well as to improve the properties of enzymes.

研究领域: 生物化学 · 材料科学 · 酶工程
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NEW JOURNAL OF CHEMISTRY · 2019 ·Vol. 43 ·期 28 ·11082-11090 · IF 3.069

Synthesis of magnetic nanoflower immobilized lipase and its continuous catalytic application

Weifan Ren,Yao Li,Jihui Wang,Lin Li,Longquan Xu,Yuxuan Wu,Yi Wang,Xu Fei,Jing Tian

The enzyme–inorganic hybrid nanoflowers have attracted wide attention due to their high surface area, enhanced enzymatic activity, and excellent stability for enzyme immobilization. However, difficulties of separation limit their application in the field of food processing. In this work, novel magnetic lipase–Cu3(PO4)2 nanoflowers (lipase@MNFs) were successfully synthesized by the coprecipitation method. The lipase@MNFs are composed of a flower-like copper phosphate skeleton and magnetic ferroferric oxide core with lipase as the coupling agent. The magnetic nanoflowers can be separated quickly from the reaction system under an external magnetic field. Compared with free lipase (∼84.00 U g−1), the lipase@MNFs exhibited higher enzymatic activity (92.63 U g−1, at 37 °C and pH 7.4) and better thermal and pH stability (at 60 °C and pH 10.0). In addition, the magnetic nanoflowers have been applied in the solvent-free biosynthesis of benzyl acetate through benzyl alcohol and vinyl acetate. These results suggest that the design of magnetic nanoflowers opens up a new way to improve the catalytic activity and stability of lipase, and simplify the enzyme separation. The magnetic nanoflowers have potential applications in various enzymatic industrial processes.

研究领域: 生物化学 · 纳米技术 · 酶工程
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JOURNAL OF FOOD PROCESSING AND PRESERVATION · 2020 ·Vol. 44 ·期 4 ·e14370 · IF 1.405

Comparison of 11 rice bran stabilization methods by analyzing lipase activities

Cheng-wei Yu,Qi-rui Hu,Hao-wei Wang,Ze-yuan Deng

The production of rice bran oil is severely impeded because of the rapid rancidity caused by rice bran lipase. Eleven stabilization treatments including 6 heating treatments and 5 nonheating treatments were carried out in this research. Lipase activities as well as oil colors, oil compositions, and contents of vitamin E and γ-oryzanol after different treatments were investigated to evaluate the effect of stabilization and oil qualities. All the treatments had no significant influence ( p > .05) on the oil compositions and γ-oryzanol contents. Among six heating treatments, autoclaving had the best stabilization effect for 10.73% lipase activity remained and other heating treatments held about 30%–35% lipase activities residual except dry heating (68.88%). Heating treatments except steam heating resulted in the significant decreases ( p < .05) of oil acid values and significant increases ( p < .05) of peroxide values, meanwhile six heating treatments increased oil colors. Among five nonheating treatments, ultraviolet irradiation for 18 hr and extreme low temperature (−80°C) for 72 hr were found 57.08% and 58.85% lipase activities residual, respectively. Peroxide value was significantly increased ( p < .05) only by ultrasound. All nonheating treatments had little effect ( p > .05) on oil acid values and color. In conclusion, ultraviolet irradiation might be a potential, convenient, and energy-saving stabilization method with high oil quality. Practical applications Rice bran has a potential for producing about 8 million tons of rice bran oil worldwide but nearly 90% rice bran was wasted every year. The processing of rice bran is impeded because of the rancidity caused by lipase, so the stabilization of rice bran is very important. This research provided a new and time-saving method for evaluating stabilization efficacy instead of long time storage. Using this new evaluating method, 11 stabilization methods were compared and methods like microwave, extrusion, and ultraviolet irradiation were considered to be suitable methods for industrial processing. In additional, ultraviolet irradiation was found to be a potential, convenient, and energy-saving stabilization method without influencing oil quality and nutrient content.

研究领域: 食品科学 · 生物化学
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CHEMICAL ENGINEERING RESEARCH & DESIGN · 2018 · IF 2.795

Lipase-catalyzed synthesis of biodiesel in a hydroxyl-functionalized ionic liquid

Yunchang Fan,Xin Wang,Lina Zhang,Jing Li,Lei Yang,Pengfu Gao,Zhulin Zhou

In this work, the biodiesel production from soybean oil catalyzed by lipase in a hydroxyl-functionalized ionic liquid (IL), N -methyl- N -propanolpyrrolidinium bis(trifluoromethanesulphonyl)imide ([C 1 C 3 OHPyr]NTf 2 ), was investigated. Compared with the conventional solvents ( n -hexane and tert -butanol) and the dialkyl-based ILs, the use of [C 1 C 3 OHPyr]NTf 2 as the reaction medium significantly improved the biodiesel yield. The biodiesel yield was greatly affected by the dosages of IL, water and enzyme, the reaction time, temperature and the methanol/oil molar ratio. The IL phase and the enzyme could be recycled by washing with water and acetone respectively at the end of reaction. The catalytic performance of the recovered lipase decreased due to the blocking of lipase active sites by impurities, nevertheless, high biodiesel yield could be obtained for the recovered lipase via prolonging the reaction time from 2   h to 6   h.

CAS / MDL: 109-65-9 124-10-7
研究领域: 生物化学 · 可再生能源
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2021 · IF 4.952

In-vitro binding analysis and inhibitory effect of capsaicin on lipase

Di Wu,Ran Duan,Lan Tang,Dian Zhou,Zhen Zeng,Wen Wu,Jie Hu,Qiaomei Sun

Capsaicin is the main active ingredient in chilis. This study selected capsazepine as a comparative model and revealed the binding mechanism and inhibitory effect of capsaicin on lipase in vitro. Electrochemical results showed capsaicin has a moderate affinity to lipase with a 7.413 × 10 4  L/mol binding constant, which is higher than capsazepine (3.388 × 10 4  L/mol). Structural analysis displayed that capsaicin/capsazepine caused a slight disturbance (less than 1%) to the secondary structure of lipase. The capsaicin binding epitope on the lipase was characterized by nuclear magnetic resonance. H 47 , H 48 and H 49 were the protons mainly involved in the interaction. In the comparison model, the H 27 and H 26 were involved in the capsazepine-lipase system. Hydrogen proton binding epitope analysis combined with molecular docking showed the main elements involved in the binding details. Enzyme kinetics results showed that capsaicin could inhibit the activity of lipase, resulting in a decrease in its ability to hydrolyze the substrate varying hydrolysis rate from 0% to 33.33% in different capsaicin concentrations. The biological model in vitro established in this study will support the development of weight-loss-related functional foods.

CAS / MDL: 404-86-4 138977-28-3
研究领域: 生物化学 · 食品科学 · 分子生物学
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ACS Applied Nano Materials · 2021 · IF 5.097

SiO2-Coated Fe3O4 Nanoparticle/Polyacrylonitrile Beads for One-Step Lipase Immobilization

Jiawei Lu,Youran Li,Huilin Zhu,Guiyang Shi

Nanoscale particle-based enzyme immobilization carries a risk of dissolving or breaking the material when applied. One effective strategy to improve the stability and functionality of this type of nanomaterial is compounding with polymers. In this study, Fe3O4 nanoparticles were synthesized and coated with SiO2, after which magnetic hollow composite beads with nanoscale porous structures, named, lipase/Fe3O4/PAN (L/FP), were fabricated by compounding polyacrylonitrile and SiO2-coated Fe3O4 nanoparticles to immobilize Candida antarctica lipase B (CALB) in one step. Fourier transform infrared spectroscopy, scanning electron microscopy, the Brunauer–Emmett–Teller method, vibrating sample magnetometer measurements, and thermogravimetry analysis were used to analyze the structure of hollow beads. It was found that composite beads retained nanoscale channels and had a larger specific surface area (27.2 m2/g), a higher pore volume (0.09 cm3/g), and better saturation magnetization values (9.8 emu/g) than PAN hollow beads (6.2 m2/g, 0.03 cm3/g, and 0 emu/g, respectively). After optimizing fabrication and immobilization conditions, L/FP showed a high lipase capacity (50 mg protein/g support) at 2 mg/mL lipase, and the immobilized yield was up to 98.4% when the mass ratio of the starting lipase and support was 1.3 (mg lipase/g support). The immobilized lipase in L/FP showed greater thermal stability and resistance to alkali than free CALB. L/FP also had good stability in most organic solvents. In all tested cycles, it also had better reusability (78.4, 47.2, and 23.8% retained activity after 10, 20, and 30 cycles, respectively) in ester hydrolysis than CALB-immobilized Fe3O4 nanoparticles or PAN beads and had higher activity than the commercial immobilized lipase (Novo 435).

CAS / MDL: 1492-30-4
研究领域: 生物化学 · 材料科学
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BIOCATALYSIS AND BIOTRANSFORMATION · 2022 · IF 2.325

Biocatalytic synthesis of dioctyl sebacate in toluene using an immobilised lipase

Mingxin Zhu,Shuyi Guo,Rongchen Mang,Hua Zhou

Sebacic esters have excellent lubricity, thermal stability, and biodegradability and therefore are widely used as aerospace lubricants, metal working oil, or engine oil. They are mainly produced by chemical synthesis which, however, may cause environmental pollution, its enzymatic synthesis represents a more environmentally friendly alternative. A few reports have described the synthesis of sebacic esters employing immobilised lipases, but these biocatalytic reactions were exclusively carried out in solvent-free systems and thus, could have been limited by slow reaction rates and high reaction temperatures due to poor enzyme dispersion, low substrate solubility, and high viscosity of the reaction mixture. The current study investigated the biosynthesis of dioctyl sebacate in toluene by Novozym 435, a commercial immobilised lipase. The reaction parameters were investigated using the single factor approach and an orthogonal array design. The optimal conditions obtained were as follows: 10 mL toluene, sebacic acid,1 mmol (202.25 mg); molar ratio of sebacic acid to 1-octanol, 1:3; Novozym 435, 0.03 g; 4 Å molecular sieves, 1.5 g; reaction temperature, 40 °C; reaction time, 30 h. A dioctyl sebacate conversion rate of 93% was achieved under these optimal conditions. In particular, the addition of molecular sieves to the reaction mixture markedly improved the product yield. The reaction temperature was low enough to make the operation easy and energy-efficient and therefore, well suited for large-scale production.

研究领域: 化学工程 · 生物化学 · 环境科学
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2022 · IF 6.056

Time-temperature indicators based on Lipase@Cu3(PO4)2 hybrid nanoflowers

Lin Wang,Feng Li,Sufang Wang,Jinsong Wu,Wenhui Zhang,Yan Zhang,Wentao Liu

The application of enzyme-inorganic hybrid nanoflowers in time-temperature indicators (TTIs) was studied for the first time. Lipase@Cu 3 (PO 4 ) 2 hybrid nanoflowers were prepared by the interaction between lipase and copper ions. Compared with free lipase, the activity of lipase in the nanoflowers was increased by 137%, and the storage stability was also improved significantly. Based on the enzymatic reaction between lipase and glycerol triacetate, six TTI prototypes with different concentrations of lipase@Cu 3 (PO 4 ) 2 hybrid nanoflowers were investigated. The color of the six TTIs changed from purple to yellow, and finally to green, and the activation energies were 46.86 kJ/mol, 51.17 kJ/mol, 54.99 kJ/mol, 60.00 kJ/mol, 62.17 kJ/mol, and 65.63 kJ/mol, respectively. The shelf life of TTIs can be determined by changing the ratio of lipase@Cu 3 (PO 4 ) 2 hybrid nanoflowers to glycerol triacetate, therefore the TTIs can be easily applied to real-time safety evaluation of many perishable foods.

研究领域: 食品科学 · 生物化学
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NEW JOURNAL OF CHEMISTRY · 2023 · IF 3.3

Lipase/tannic acid magnetic hydrogel microspheres and its continuous catalytic application

Xuan Ji,Yao Li,Suo Wang,Xu Fei,Jing Tian,Longquan Xu,Yi Wang

The immobilization of enzyme by covalent bond usually uses toxic chemicals, which not only reduces the enzyme activity, but also is not conducive to its application in the food field. In this work, the surface of magnetic hydrogel microspheres was modified with tannic acid, which was oxidized into quinone, and then covalently linked to the lipase through Schiff base reaction. Further using the water absorption and water retention characteristics of hydrogel microspheres, a micro-water-oil interface can be provided for lipase in the organic phase reaction system, which provides favorable conditions for opening the α -helix "lid" of lipase active center and exposing the active center. Meanwhile, the synthesis of esterification catalyzed by lipase at the oil-water interface was promoted. In comparison to free lipase, the produced lipase/tannic acid magnetic hydrogel microspheres (L-PTAM2) exhibited superior temperature and pH stability and can basically sustain the activity of free lipase. After 20 consecutive cycles, L-PTAM2 still maintained about 57% of its original activity and could be quickly separated from the product. It was used for continuous catalytic production of benzyl acetate with a yield of 82%.

研究领域: 生物技术 · 材料科学 · 催化 · 酶工程
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Journal of Environmental Chemical Engineering · 2026 ·Vol. 14 ·期 4 ·123412 · IF 7.5

Near-infrared photothermal Candida antarctica lipase B /CuS/Cu-tetrakis (4-carboxyphenyl) porphyrin bioconjugate for remote real-time and precise control of lipase catalytic activity of glycerol esterification

Jiahao Ouyang,Yulin Chen,Xiaonuo Li,Jiahao Li,Qiu Xia,Kai Huang,Guangyang Wang,Yong Ye

To address enzyme inactivation upon immobilization and the underutilization of surplus glycerol from biodiesel production, a near-infrared (NIR)-responsive bioconjugate was developed which comprised Candida antarctica lipase B (CALB) immobilized on a CuS/Cu-TCPP support. In this design, Cu-TCPP (a porphyrin-based metal-organic framework) provides a high-surface-area scaffold, CuS nanoparticles act as NIR photothermal converters, and hydrophobic surface modification enhances lipase adsorption. XRD, XPS, SEM, and TEM confirmed the formation of covellite-structure CuS on Cu-TCPP and successful enzyme immobilization. The system achieves a photothermal conversion efficiency of 22.70% (defined as the ratio of heat generated to absorbed laser energy), retains 99.52% of its initial activity at 70 °C, and preserves 74.20% activity after five reuse cycles. During glycerol esterification under NIR irradiation (808 nm) at room temperature, oleic acid conversion reaches 69.2%, representing a 2.42-fold increase compared to the non-irradiated control (28.6%). Bandgap analysis (1.66 eV > 1.53 eV) confirms the absence of reactive oxygen species generation, preventing enzyme oxidative inactivation. This work enables remote, real-time, and precise control of lipase catalysis via localized photothermal heating, offering a green strategy for glycerol valorization.

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