FOOD CHEMISTRY
·
2025
·
IF 9.8
Wen-Yu Liu,Xin-Yue Jia,Hao-Yue Zheng,Hui-Hui Zhang,Jun-Xia Xiao,Guo-Qing Huang
The Pickering emulsion stabilized by ovalbumin/pectin polyelectrolyte complex with porcine pancreatic lipase (PPL) dissolved in the aqueous phase was investigated for its feasibility in biphasic catalysis. CLSM and QCM-D analysis revealed that PPL discretely adsorbed to emulsion interface, though they were both negatively charged. The hydrolysis of p-NPP was favored in low stabilizer concentrations and could be saturated by PPL, and the optimum conditions were pH 6.5, ovalbumin to pectin mass ratio 1:3, complex concentration 0.25 %, and PPL dosage 0.6 %. Under these conditions, the Pickering emulsion conferred a conversion rate of 0.87 μmol/h and product yield of 46.8 % after reaction for 5 h, which were significantly lower than 1.37 μmol/h and 73.6 % of the conventional oil/water system. Hence, Pickering emulsions stabilized by protein/polysaccharide polyelectrolyte complexes might not be ideal media for biphasic catalysis, possibly due to the viscoelastic property of the complexes that could better cover emulsion interfaces.
研究领域:
食品科学
·
生物化学
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DOI
PubMed
高影响因子
Catalysts
·
2026
·Vol. 16
·期 6
·511
·
IF 4.5
Fan Zhang,Xuejin Zhang,Lezhao Liu,Zhi Wang
The present work establishes a sustainable and environmentally benign biocatalytic strategy for the construction of multisubstituted cyanopyrazoles via [3+2] cycloaddition, employing lipase as a highly efficient and practical catalyst. Under the optimized mild reaction conditions, this protocol enables the preparation of structurally diverse cyanopyrazole derivatives with high to excellent isolated yields. The substrate used in this method is the in situ-generated diazoacetonitrile. The corresponding conversion was carried out under mild aqueous conditions, avoiding the flammable and explosive characteristics of diazoacetonitrile. The established protocol exhibits a representative substrate scope and good functional group compatibility. Molecular docking was employed to investigate the reaction, highlighting the significant impact of the active-site architecture of the lipase on this reaction. This biocatalytic approach not only enriches the synthetic toolbox for the preparation of valuable cyanopyrazole scaffolds but also highlights the potential of lipase-catalyzed promiscuous reactions in the green synthesis of pharmaceutically relevant heterocyclic compounds.
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高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2025
·
IF 8.5
Qingqing Liu,Yue Tang,Mingming Xiong,Yunting Yang,Yanting Liu,Zhengping Duan,Wei Luo,Yisha Xie,Yongjun Yuan
Lipase is widely used in the food industry, but its catalytic efficiency is limited by the insufficient enzyme-substrate contact. To address this issue, chitosan-zein complex particles immobilized lipase (CZPs-lipase) and the corresponding Pickering emulsion catalytic system (PEC) were fabricated. The results showed that the incorporation of zein increased the three-phase contact angle of the particles and decreased the particle size, facilitating lipase immobilization. However, the reduced ζ-potential of the particles was unfavorable for the lipase immobilization by electrostatic adsorption. As a compromise, the maximum immobilized lipase activity was obtained at a chitosan:zein mass ratio of 1:2 (CZPs 1:2 -lipase). In addition, the PEC stabilized by CZPs-lipase had a significantly ( P < 0.05) smaller particle size than that stabilized by chitosan-lipase particles. Consequently, after 120 min of reaction, the hydrolysis rate of p-nitrophenol palmitate in the PEC stabilized by CZPs 1:2 -lipase was 1.66 and 3.67 times that of the free lipase emulsion and the free lipase biphasic catalytic system, respectively. Meanwhile, after 180 min of reaction, the hydrolysis rate of corn oil and soybean oil in the PEC reached 75.68 ± 1.85 % and 96.27 ± 2.26 %, respectively, significantly ( P < 0.05) higher than that in the free lipase emulsion. After five cycles, the relative hydrolysis rate remained at approximately 85 %. This efficient and PEC has considerable potential for applications in the food industry.
研究领域:
食品科学
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生物技术
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DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Jihang Zhang,Jiale Chen,Yu Sha,Jiawei Deng,Jinglan Wu,Pengpeng Yang,Fengxia Zou,Hanjie Ying,Wei Zhuang
When it comes to enzyme stability and their application in organic solvents, enzyme biocatalysis has emerged as a popular substitute for conventional chemical processes. However, the demand for enzymes exhibiting improved stability remains a persistent challenge. Organic solvents can significantly impacts enzyme properties, thereby limiting their practical application. This study focuses on Lipase Thermomyces lanuginose , through molecular dynamics simulations and experiments, we quantified the effect of different solvent-lipase interfaces on the interfacial activation of lipase. Revealed molecular views of the complex solvation processes through the minimum distance distribution function. Solvent-protein interactions were used to interpret the factors influencing changes in lipase conformation and enzyme activity. We found that water content is crucial for enzyme stability, and the optimum water content for lipase activity was 35 % in the presence of benzene-water interface, which is closely related to the increase of its interfacial activation angle from 78° to 102°. Methanol induces interfacial activation in addition to significant competitive inhibition and denaturation at low water content. Our findings shed light on the importance of understanding solvent effects on enzyme function and provide practical insights for enzyme engineering and optimization in various solvent-lipase interfaces.
研究领域:
生物化学
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酶工程
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DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2025
·
IF 8.5
Xiang Zhou,Jiahao Xu,Jiayao Sun,Hao Chen,Dechun Huang,Wei Chen,Hongliang Qian
1,3-Dioleoyl-2-palmitoylglycerol (OPO) is crucial for infant nutrition; however, conventional immobilized lipase requires high-purity enzymes, which increases costs and limits industrial scalability. Herein, Rhizomucor miehei lipase (RML) was immobilized on surface-modified magnetic nanoparticles using cross-linked enzyme aggregates (CLEAs) technology to produce Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs. This approach combines the separation and immobilization of enzymes, allowing for the use of lower-purity lipase, which enhances its suitability for industrial-scale processes. The optimized Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs exhibited excellent thermal, pH, and storage stability. The performance of Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs was evaluated by catalyzing the synthesis of OPO through the enzymatic hydrolysis of glycerol tripalmitate (PPP) and oleic acid (OA). Under optimal conditions, the OPO content in products reached 63.33 ± 0.30%, highlighting the high efficiency of the enzymatic process. After eight reuse cycles, the Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs retained around 75% of their relative activity. Therefore, this strategy of lipase immobilization using CLEA technology, coupled with magnetic nanoparticles, offers a promising approach for OPO synthesis.
研究领域:
生物催化
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纳米技术
·
酶固定化
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食品化学
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工业生物技术
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PubMed
高影响因子
BIORESOURCE TECHNOLOGY
·
2025
·
IF 9
Jihang Zhang,Siwen Ji,Jinming Zhang,Yihui Luo,Yanjun Chen,Jinglan Wu,Pengpeng Yang,Fengxia Zou,Hanjie Ying,Wei Zhuang
Lipase conformational dynamics at carrier interfaces dictate biocatalytic performance, yet their structural adaptability and molecular underpinnings remain unclear. This study elucidates how reduced graphene oxide (rGO) surface hydrophobicity modulates lipase activation through spectroscopy and molecular dynamics simulations, unveiling enzyme-specific mechanisms. By tuning rGO reduction, we found that rGO-4 h optimally enhanced Candida antarctica lipase B (CALB) activity by 201.4 % through rigidity-driven stabilization, as its non-blocking lid improved structural integrity and substrate affinity rather than undergoing interfacial activation. Rhizomucor miehei lipase (RML) and Porcine phospholipase (PPL), which rely on lid-dependent activation, exhibited increased activity (122.3 % and 165.4 %, respectively) due to enhanced lid opening and hydrophobic interactions. Molecular dynamics simulations revealed that PPL’s long lid required the highest flipping energy (−1112.9 kJ/mol), limiting activation. In contrast, RML’s short lid had a lower energy barrier (−596.1 kJ/mol), facilitating lid flipping and interfacial activation. Spectroscopic analysis confirmed that moderate hydrophobicity preserved α-helix structures, whereas excessive reduction induced α-to-β transitions. Radial distribution function analysis indicated that increased solvent accessibility at the active site facilitated RML and PPL activation. For CALB, enhanced van der Waals (vdW) interactions (−207.3 kJ/mol) and reduced electrostatic repulsion within the active pocket strengthened substrate binding, shortening the catalytic serine-substrate distance (2.89 Å vs. 3.38 Å) and improving efficiency. These findings establish that rigidity-dependent enzymes benefit from structural stabilization, whereas lid-dependent lipases require hydrophobicity-tuned flexibility for optimal activation. This study provides a structure–function framework for designing advanced immobilization platforms, with applications in biocatalysis, pharmaceuticals, and biofuel production.
研究领域:
生物催化
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酶工程
·
表面化学
·
分子生物学
·
计算生物学
·
纳米材料
·
光谱学
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DOI
PubMed
高影响因子
JOURNAL OF APPLIED POLYMER SCIENCE
·
2018
·Vol. 136
·期 12
·47221
·
IF 1.901
Liuen Liang,Junyuan Long,Guangji Li
This work developed a facile and environmentally friendly route for lipase-catalyzed synthesis of a hyperbranched polyester by introducing an autocatalytic prepolymerization of comonomers. Trimethylolpropane, 1,8-octanediol, and adipic acid as comonomers for synthesizing the hyperbranched polyester were first prepolymerized via the automatic catalytic effect of the reactants themselves to obtain an appropriate reaction substrate for further lipase-catalyzed polymerization, where immobilized lipase Novozym 435 was used as a biocatalyst. The acidity and fluidity of optimized oligomers after the autocatalytic prepolymerization provide a benign reaction substrate for the retention of enzymatic activity in the subsequent lipase-catalyzed esterification, which is crucial for the enzymatic polymerization. The optimum reaction temperature and reaction time for prepolymerization were determined to be 120 °C and 150 min. The molecular weight ( M w ) of the prepared polyester was approximately 26,300 g/mol. Quantitative analysis of 1 H-NMR and inverse-gated 13 C-NMR spectra confirmed the hyperbranched structure of the resulting polyester with a branching degree of 31.3%. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019 , 136 , 47221.
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高影响因子
FOOD CHEMISTRY
·
2013
·
IF 3.334
Juan Zhang,Lin Xiao,Yucai Yang,Zhaoxia Wang,Genxi Li
In this paper, we find that the effect of lignin on pancreatic lipase (PL) is dependent on reaction medium and substrate used. Experimental results reveal that lignin can gradually bind to PL to form a PL–lignin complex, resulting in an increased activity of the enzyme. The binding process is spontaneous and the PL–lignin complex formation is an endothermic reaction induced by hydrophobic and electrostatic interaction. There is a non-radiation energy transfer from PL to lignin during the binding process, and the binding of lignin to PL conforms to a secondary exponential decay function. Moreover, the α-helix content of the enzyme will be changed and the rigidity of its side chain will be enhanced due to the formation of lignin–PL complex. This study has not only provided the activation effect of lignin on PL, but also given an insight into the interaction between lignin and the enzyme, which would benefit the application of lignin in the pharmacy and food industry, as well as other fields.
研究领域:
生物化学
·
酶学
·
食品科学
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DOI
PubMed
高影响因子
Catalysts
·
2017
·Vol. 7
·期 10
·302
·
IF 3.082
Ni Tu,Jianxin Shou,Huaping Dong,Jin Huang,Yimin Li
Clay/chitosan composite beads were prepared and used as the carrier to support lipase by adsorption, to improve the activity and stability of lipase in the hydrolysis of olive oil. Under conditions of pH 6.0, 25 °C and adsorption for 10 h, immobilized lipases on chitosan bead (CB–lipase) and three clay/chitosan composite beads, at different clay to chitosan proportions of 1:8 (CCB-8-lipase), 1:5 (CCB-5-lipase) and 1:3 (CCB-3-lipase), were prepared. By comparing the activity of these immobilized lipases, CCB-5-lipase showed the highest activity, followed by CCB-8-lipase > CCB-3-lipase > CB-lipase; this improvement was attributed to the synergetic effect of enrichment of olive oil by clay at the reaction surface and better biocompatibility of chitosan with lipase molecules. The optimum pH and temperature in the reaction respectively changed from 7.0 and 30 °C for free lipase to 7.5 and 35 °C for immobilized forms. Furthermore, the thermal stability and repeated usability of these immobilized lipases were sequenced as CCB-3-lipase > CCB-5-lipase > CCB-8-lipase > CB–lipase, due to greater rigidity of immobilized lipase with the addition of clay, which was further confirmed by SEM. The study shows that the incorporation of clay with chitosan creates a good synergetic effect to improve the catalytic performance of immobilized lipase on clay/chitosan composite.
研究领域:
生物催化
·
酶工程
·
材料科学
·
应用微生物学
·
分子生物学
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高影响因子
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
·
2015
·Vol. 64
·期 1
·87-91
·
IF 1.362
Hong De Yan,Qin Li,Zhao Wang
A lipase from Thermomyces lanuginosus (Lipozyme TL IM) exhibited high enantioselectivity for kinetic resolution of (±)-menthol in organic solvent. The various reaction parameters affecting the conversion and enantioselectivity were studied. The optimum reaction conditions for the transesterification reaction were found with vinyl acetate in the solvent of methyl tert -butyl ether with a vinyl acetate:(±)-menthol molar ratio of 5:1 and an enzyme concentration of 200 g/L at 30 °C. In these conditions, (−)-menthyl acetate with 99.3% enantiomeric excess was obtained, whereas the conversion was 34.7% with the reaction time of 12 H at the substrate concentration of 0.5 M. In addition, the enzyme allowed the substrate loading to be increased up to 1.5 M without the decrease of the enantioselectivity. These results indicated that Lipozyme TL IM was a promising biocatalyst in the resolution of (±)-menthol.
研究领域:
生物催化
·
酶工程
·
有机化学
·
立体化学
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DOI
高影响因子
CHEMICAL ENGINEERING RESEARCH & DESIGN
·
2018
·
IF 2.795
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.
研究领域:
生物化学
·
可再生能源
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DOI
高影响因子
FOOD CHEMISTRY
·
2021
·
IF 7.514
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.
研究领域:
生物化学
·
营养学
·
药理学
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PubMed
高影响因子
危险品化学品经营许可证（带存储）