LANGMUIR
·
2025
·
IF 3.9
Yuan Bai,Weiting Huang,Jie Liu,Kexin Hu,Haoyu Zheng,Xintong Shen
The removal of dye pollutants from water bodies is a significant global issue due to their negative effects on both ecosystems and human health. For this purpose, effective and selective α-FeOOH-Fe3O4@Chitosan-LDHs@Lipase (MF@CS-LDHs@LIP) magnetically bionanomaterials were synthesized via co-precipitation and cross-linking methods for uptake of Congo red (CR) from wastewater. Comprehensive characterization of both the carrier and MF@CS-LDHs@LIP was performed using SEM, FTIR, XRD, BET, VSM, and EDX. The analytical results confirmed the successful immobilization of lipase on the composite carrier. The immobilization conditions and enzymatic properties of the enzyme were investigated. The results demonstrated that the immobilized lipase maintained over 60% relative activity within a pH range of 7.0–11.0. Notably, at pH 11.0, its activity was 1.69 times higher than that of free lipase. Both immobilized and free lipase exhibited significant activity reduction at temperatures exceeding 40 °C. At 55 °C, the immobilized lipase exhibited 2.32 times higher relative activity compared to its free counterpart. However, after five reuse cycles, the immobilized lipase retained 40.30% of its initial activity. Furthermore, after being stored at 4 °C for 30 days, the relative activity of immobilized lipase was slightly higher than that of free lipase, approximately 24.32% and 14.81%, respectively. The adsorption kinetics and isotherm studies revealed that the adsorption process followed pseudo-first-order kinetic and the Temkin isotherm model. A maximum adsorption capacity of 87.82 mg/g was present in CR solution at 25 °C, pH = 6.0, 420 min, 50 mg dosage, and 100 mL of an initial concentration of 120 mg/L. Furthermore, the immobilized lipase exhibited excellent reusability, maintaining a CR removal efficiency above 70% after 5 consecutive cycles.
研究领域:
环境科学
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纳米技术
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生物技术
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水处理
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酶工程
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材料科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
COLLOIDS AND SURFACES B-BIOINTERFACES
·
2025
·
IF 5.6
Xing Ni,Luyi Chen,Xue Zhang,Jiaojiao Xia,Qiongya Lu,Yani Zhao,Bin Zou
In this study, alkali lignin (AL), a low-cost and renewable biopolymer, was innovatively selected as the precursor. Modified lignin, namely aminated lignin (AAL), sulfomethylated lignin (SML) and phosphorylated lignin (PAL), were synthesized and combined with nano-MgO to serve as a template. Subsequent carbonization of these mixtures produced mesoporous carbon (MC) carriers denoted as AL-MC, AAL-MC, SML-MC and PAL-MC. Rhizomucor miehei lipase (RML) immobilization onto these carriers was effectively achieved through physical adsorption under mild conditions. Through optimization of the preparation parameters, high-performance immobilized enzymes (IM-AL-MC, IM-AAL-MC, IM-SML-MC, IM-PAL-MC) were developed. Notably, IM-AAL-MC exhibited superior enzyme activity (0.037 U/mg immobilized lipase), loading capacity (0.145 mg protein/mg immobilized lipase) and immobilization efficiency (84.5 %). The catalytic efficiency and stability of IM-AAL-MC were comprehensively examined. Characterization of the carriers and immobilized enzymes was conducted using Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), Brunauer-Emmett-Teller surface area analysis (BET) and transmission electron microscopy (TEM). Results indicated that IM-AAL-MC displayed significantly improved stability compared to free lipase. Remarkably, IM-AAL-MC retained 99.49 % activity in n-hexane, far exceeding the free lipase (43.53 %). Additionally, IM-AAL-MC preserved 86.2 % of its relative activity after six consecutive reuse cycles.
研究领域:
生物技术
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酶工程
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材料科学
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绿色化学
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纳米技术
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF PHYSICAL CHEMISTRY B
·
2025
·
IF 2.9
Lei Wang,Zhen-Zhen Li,Gong-Ji Chen,Mi-Zhuan Li,Yan Cheng,Zhong-Xiu Chen
The activity of lipase was inhibited or promoted by different macromolecular colloids, but the underlined general rules were not clear. In this paper, lipase activity was systematically analyzed in different macromolecular media. The detailed factors that affect the enzyme activity were extracted for quantification. Three functions, including viscosity, the crowding effect, and soft interactions, were established to describe the macromolecular medium effect. The medium parameter based on the Huggins constant and Kramer constant was able to characterize the quality of the macromolecular media. A multivariate nonlinear regression model was proposed for the correlation or prediction between three groups of factors and enzyme activity, and a crowding enzyme factor CCef was proposed. This study pioneered the qualification and prediction of the multiple factors that affect the enzyme activity in complex media. It is also significant for scientifically predicting the efficacy of functional macromolecules related to healthy food and the formulation of dietary fibers.
研究领域:
生物化学
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食品科学
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产品关联
DOI
PubMed
高影响因子
MICROCHEMICAL JOURNAL
·
2024
·
IF 4.9
Chongyang Mu,Mashooq Khan,Jinpeng Liu,Xinfeng Dong,Zhengtong Wang,Ping Song,Qiongzheng Hu,Li Yu
The development of new types of sensing platforms with excellent performance is always appealing. In this report, we demonstrate a low-cost and user-friendly sensing platform based on drying of the aqueous droplet on the surface. The principle relies on the transduction of the surfactant concentration into the area of the dried droplet on the surface. The screening of a lipase inhibitor is demonstrated as an example. When triacylglycerols (GT) and lipase are mixed, the aqueous droplet produces a large dried area on the surface. This phenomenon is attributed to the production of sodium oleate due to the enzymatic digestion of GT by lipase. It results in reduction of the surface tension and causes wetting and spreading of the droplet, leaving a large dried area on the surface. However, in the presence of orlistat, a lipase inhibitor, a small dried area is obtained due to the inhibition of lipase activity by orlistat. Using this method, the lipase inhibitor can be readily and effectively screened. Compared to previous studies, this method is simple, rapid, low-cost and avoids the use of labelled molecules and complex instrumentation, with an IC 50 value of 0.59 ± 0.09 μM for orlistat. In addition, it also works well with a portable microscope and a smartphone interface for data analysis. Overall, this study provides a new method for rapid and cost-effective screening of lipase inhibitors.
研究领域:
分析化学
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生物技术
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生物化学
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药学
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产品关联
DOI
高影响因子
RESEARCH ON CHEMICAL INTERMEDIATES
·
2024
·Vol. 50
·期 7
·3153-3177
·
IF 2.8
Hao Xiaohong,Zheng Xiangsheng,Zhang Qi,Da Xiongzhi,Wang Yan
The main objective of this study was to produce biodiesel utilizing Fe 3 O 4 @ZIF-8-CRL as biocatalyst, employing high acid value waste oil. Candida Rugosa lipase (CRL) was immobilized onto a magnetic ZIF-8 organometallic framework through physical adsorption, resulting in significantly enhanced stability and chemical compatibility. The study extensively investigated the impacts of enzyme dosage, alcohol-to-oil ratio, ultrasonic power, temperature, time, and the addition of deep eutectic solvents on the conversion of fatty acid ethyl esters. The findings revealed that under the conditions of biocatalyst addition of 5.7 wt.%, alcohol–oil ratio of 6:1 mmol/g, ultrasonic power of 87.297 W, reaction temperature of 40 °C, and reaction time of 2 h, the innovative biocatalyst facilitated a conversion efficiency of fatty acid ethyl esters reaching 82.06 ± 1.63%, with a retention rate of 74.52% after three cycles. Additionally, characterization of the biocatalyst using a vibrating sample magnetometer and scanning electron microscopy demonstrated its favorable magnetic recovery potential and morphology. Coupled with its straightforward and efficient synthesis, this biocatalyst proves to be competitive in the catalysis of biodiesel preparation.
研究领域:
生物化学
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能源科学
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催化技术
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产品关联
DOI
高影响因子
EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY
·
2024
·
IF 1.8
Xin Yu,Xinyi Yang,Junqing Qian,Hui Guo
Mangiferin is one of the main bioactive ingredients in leaves of Mangifera indica . But the poor liposolubility and low bioavailability restrict its application. This study aimed to esterify mangiferin with lipase to improve its lipophilicity, and evaluate its antioxidant activity and hypoglycemic properties. Four fatty acids (palmitic acid, lauric acid, stearic acid, oleic acid) were selected for enzymatic esterification with mangiferin by single-factor experiments. Under the following optimum reaction conditions of tetrahydrofuran (THF): tert -amyl alcohol (2:1) was used as solvent, water activity was 0.31, TLIM lipase was 45 mg mL –1 , The ratio of mangiferin to fatty acid was 1:50, and the substrates were pretreated by ultrasonic for 0.5 h, then reacted at 55°C for 21 h, the resulting conversion rates of mangiferin-esterified derivatives exceeded 70.0%. Lipophilicity, antioxidant, and PTP1B inhibitory activity of mangiferin-esterified derivatives were determined. The results demonstrated that compared with mangiferin, the ability to scavenge DPPH radicals decreased by about 9%, but the lipophilicity was increased by 10–30 times, and the lipid antioxidant capacity was also improved significantly. Moreover, the inhibitory activity of protein tyrosine phosphatase 1B (PTP1B) exhibited minimal alteration. This indicates that esterification can not only improve the lipophilicity of mangiferin, but also improve its lipid antioxidant capacity. Practical Applications : In the study, a series of mangiferin-esterified derivatives were synthesized and their lipophilicity, antioxidant properties, and PTP1B inhibitory activity were determined. The results indicated that, compared with the untreated mangiferin, the mangiferin-esterified derivatives exhibited superior lipid antioxidant and hypoglycemic activities. Furthermore, the enzymatic esterification method employed in this study offered greater economic and environmental advantages when compared to chemical catalysis. Therefore, the preparation of mangiferin derivatives through enzymatic esterification were deemed feasible with potential application value for enhancing lipid antioxidant capacity in high-fat foods.
研究领域:
食品科学
·
生物化学
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产品关联
DOI
高影响因子
COLLOIDS AND SURFACES B-BIOINTERFACES
·
2020
·
IF 4.389
Yi-Ping Cao,Yu-Pei Xia,Xiao-Fei Gu,Li Han,Queting Chen,Gao-Ying Zhi,Dong-Hao Zhang
Here, PEI@PMMA microspheres were prepared by grafting polyethyleneimine (PEI) on poly(methyl methacrylate) (PMMA) magnetic microspheres and successfully used to immobilize lipase. The results showed that PEI@PMMA microspheres had strongly adsorbed lipase (49.1 mg/g microsphere) via electrostatic attraction. To prevent lipase shedding, the adsorbed lipase was further crosslinked with PEI on microspheres using glutaraldehyde as crosslinker. Consequently, PEI-crosslinked lipase (2.14 U/mg) exhibited 2.6 times and 1.4 times higher activity respectively than the directly covalent lipase (0.82 U/mg) and the crosslinked lipase aggregates (1.57 U/mg), which was close to the activity of adsorbed lipase (2.20 U/mg). Conformational analysis from FTIR spectroscopy showed that PEI-crosslinked lipase retained its natural structure well. And the α-helix structure seemed to play a key role in enhancing lipase activity. Furthermore, the effects of various parameters on crosslinking reaction were investigated. Also, PEI-crosslinked lipase revealed higher pH and thermal stability. The Michaelis constant ( K m ) was increased and the optimum temperature of lipase was widened observably after crosslinking with PEI on PEI@PMMA magnetic microspheres.
研究领域:
生物化学
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酶工程
✓ 已验证
DOI
高影响因子
RSC Advances
·
2017
·Vol. 7
·期 56
·35169-35174
·
IF 3.108
Zhiming Chen,Leilei Liu,Renchun Yang
An effective strategy for enhancement of catalytic activity and stability of immobilized lipase by interfacial activation on Fe3O4@PVBC (Fe3O4@polyvinylbenzyl chloride) nanoparticles was developed, which involved the fabrication of core–shelled Fe3O4@PVBC nanoparticles via an emulsion polymerization process and the subsequent immobilization of lipase in phosphate buffer. Due to the magnetic nature of Fe3O4 cores and the presence of chloromethyl-functionalized polymer shells, the Fe3O4@PVBC nanoparticles were employed as valid magnetic carriers for lipase immobilization. Bradford assays indicated that the loading amount of lipase on the Fe3O4@PVBC nanoparticles was calculated to be 162.5 mg protein per g particles. The catalytic activity of the immobilized lipase retained about 99.6 ± 3.3% of the free enzyme activity, which was attributed to interfacial activation of lipase by Fe3O4@PVBC nanoparticles. Thermal and urea tolerance tests revealed that the immobilized lipase exhibited much better stabilities. Additionally, the immobilized lipase retained more than 69.8% of its initial activities after 10 times of reuse. It is believed that the results of the present investigation may provide a versatile approach for designing and fabricating biocatalysts with high activation and stability.
研究领域:
生物化学
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纳米生物学
·
酶工程
✓ 已验证
DOI
高影响因子
Food and Bioprocess Technology
·
2024
·
IF 5.3
Hu Jin,Yang Wencheng,Lan Huanling,Lin Xueyuan,Li Chang
Rice ( Oryza sativa ) bran is a by-product of rice processing, which contains rich nutrients and is a resource that can be fully utilized. However, lipase in rice bran can lead to rancidity of rice bran oil. Therefore, it is important to study the characteristics of rice bran lipase for the stable storage of rice bran. A new lipase from rice bran was isolated by DEAE Sepharose column and gel filtration column, respectively. The determination of lipase’s molecular weight and purity was conducted utilizing the SDS-PAGE technique, and the enzyme was identified through LC-MS/MS. Concurrently, an investigation was conducted on the characteristics of the lipase. The findings indicated that the lipase had a molecular weight of 36.352 kDa. Optimal catalytic activity for rice bran lipase (RBL) was observed at a temperature of 40 ℃ and pH value of 7.0, while it exhibited remarkable stability below 20 ℃ and within the pH range from 6.0 to 8.0. The stability of the RBL against various metal ions and high NaCl concentrations was observed to be relatively modest. Notably, the catalytic activity was significantly influenced by certain organic solvents (such as acetone, THF, and trichloromethane) as well as several inhibitors ( P < 0.05). Furthermore, RBL demonstrated a preference for hydrolyzing long-chain p-NP esters (C12-C16).
研究领域:
生物化学
·
食品科学
✓ 已验证
DOI
高影响因子
CHEMICAL ENGINEERING JOURNAL
·
2011
·
IF 3.074
Huaping Dong,Jianfa Li,Yimin Li,Liujiang Hu,Dongping Luo
Organobentonites were prepared from Na-bentonite (NB) by intercalation with cetyltrimethyl ammonium bromide (CTMAB), and used to support the lipase from porcine pancreas. The immobilized lipase showed higher activity in hydrolysis of olive oil than free lipase, with the highest specific activity of 347.8 U g −1 protein for lipase immobilized on bentonite-CTMAB 100 (BC 100 -lipase). The apparent activation energy ( E a ) of catalysis declined from 29.25 kJ mol −1 for free lipase to 16.31 kJ mol −1 for BC 100 -lipase, resulting in a higher catalytic efficiency of lipase. The improvement of catalytic activity was attributed to the interfacial activation by hydrophobic microenvironment and highly scattered surface created by organobentonite, according to the structural and morphological characterizations by Fourier transform infrared spectroscopy (FTIR) and Transmission electron microscopy (TEM). The immobilized lipase showed better resistance to pH and heating inactivation in comparison to the free lipase. After the storage of 8 days, BC 100 -lipase retained 80.7% of initial activity, which was 2.7 times higher than the residual activity of free lipase. Particularly, BC 100 -lipase kept 82.5% of initial activity after 6 continuous recycles under vigorous agitation, showing the excellent stability of the immobilized lipase by adsorption.
研究领域:
生物化学
·
材料科学
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF MATERIALS SCIENCE
·
2023
·
IF 4.5
Gao Nengwen,Liu Jing,Wang Xiaoli,Zhang Yu
Lipases are widely used in industry. Free lipases are difficult to recover and have poor stability under operational conditions. Herein, lipases are immobilized onto the methyltrimethoxysilane (MTMS)-modified ceramic membranes (~ 5 nm) with reverse filtration method, and further cross-linking by glutaraldehyde (GA) is used to improve the lipase stability. FTIR and XPS analyses demonstrate the successful immobilization of lipase. The immobilized lipases are used to hydrolyze glycerol triacetate (GT) to fatty acids and glycerol. Under the optimal immobilization conditions (MTMS concentration 0.1 M, lipase immobilization time 80 min, lipase concentration 3 mg/mL, and GA concentration 2%), the loading of lipases reaches 0.24 mg/g. Under the optimal operational conditions (temperature 45 °C, pH 7, pressure 0.2 MPa, GT concentration 0.05 M), the immobilized lipases have the highest catalytic activity of 25 U/mg. Moreover, the thermal and pH stabilities of immobilized lipases are found to be higher than those of the free lipases. In the long-term runs, the immobilized lipases still have 64% of the initial activity after 7 cycles, indicating good reusability. This paper provides a simple process for immobilizing lipase on ceramic membranes. The immobilized lipases have better stability at high temperature and basic environments (pH 7–9), which would have broad applications in lipase-catalyzed reactions. Graphical Abstract
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DOI
高影响因子
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
·
2013
·Vol. 171
·期 7
·1559-1567
·
IF 1.893
Wang Na,Zhang Wei,Zhou Long-Hua,Deng Qing-Feng,Xie Zong-Bo,Yu Xiao-Qi
A facile tandem route to α,β-unsaturated aldehydes was developed by combining the two catalytic activities of the same enzyme in a one-pot strategy for the aldol reaction and in situ generation of acetaldehyde. Lipase from Mucor miehei was found to have conventional and promiscuous catalytic activities for the hydrolysis of vinyl acetate and aldol condensation with in situ formed acetaldehyde. The first reaction continuously provided material for the second reaction, which effectively reduced the volatilization loss, oxidation, and polymerization of acetaldehyde, as well as avoided a negative effect on the enzyme of excessive amounts of acetaldehyde. After optimizing the process, several substrates participated in the reaction and provided the target products in moderate to high yields using this single lipase-catalyzed one-pot biotransformation.
研究领域:
生物化学
·
酶工程
✓ 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）