FOOD CHEMISTRY
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2024
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IF 8.5
Liang Wang,Zheng Zhou,Ji Wang,Xu-Song Wang,Da-Yong Zhou,Lei Qin,Xu-Hui Huang
The regulation of reaction rate differentiation, catalytic precursor differentiation, and end-product differentiation during enzyme-mediated reactions within complex lipid systems is a key area of research in flavor regulation. A multilayer lipid oxidation model, utilizing Plaice bone oil (PBO), lipase, and lipoxygenase, was employed to investigate oxidation differences between various lipids and corresponding flavor formation patterns. Lipase treatment resulted in higher levels of non‑oxygenated volatile compounds and saturated aldehydes, whereas lipoxygenase treatment increased oxygenated compounds, particularly (E)-2-hexenal, 1-penten-3-one, and 2-pentylfuran. The hydrolysis of triglycerides by lipase significantly raised the concentration of monounsaturated fatty acids. Lipoxygenase catalyzed the formation of position-specific oxidation products at the ω-6 carbon position of PUFAs, such as 15-hydroperoxy-EPA and 17-hydroperoxy-DHA. These enzymatic treatments altered the lipid profile, leading to distinct flavor formation patterns. This study provides valuable insights into the mechanisms underlying enzyme-mediated volatile substance variations in food.
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Journal of Oleo Science
·
2021
·
IF 1.601
Xiumei Wang,Xiaoxu Zhao,Xiaoli Qin,Zexin Zhao,Bo Yang,Yonghua Wang
n-3 polyunsaturated fatty acids (PUFA)-rich triacylglycerols (TAG) with many beneficial effects are still difficult to be synthesized efficiently and rapidly by current synthetic techniques. This study reports the fatty acid specificity of immobilized MAS1 lipase and its efficient synthesis of n-3 PUFA-rich TAG by esterification of glycerol with n-3 PUFA in natural deep eutectic solvents (NADES) systems. Immobilized MAS1 lipase showed the highest preference for capric acid [C10:0, the highest specificity constant (1/α)=1] whereas it discriminated strongly against docosahexaenoic acid (DHA) and eicosapentaenoic acid (EPA) due to their lowest specificity constants (1/α=0.19 and 0.2). Moreover, the highest n-3 PUFA-rich TAG content (55.8%) with similar n-3 PUFA composition to the substrate was obtained in choline chloride/glycerol (CG) system. There was a 1.38-fold increase of TAG content in CG system compared with that in the solvent-free system. Interestingly, immobilized MAS1 lipase exhibited no regiospecificity in the solvent-free and various NADES systems. Besides, the potential reaction mechanism of immobilized MAS1 lipase-catalyzed esterification of glycerol with n-3 PUFA in NADES systems was described. It was found that the use of NADES as solvents could greatly enhance TAG content, and make it easy to separate the product. These results indicated that immobilized MAS1 lipase is a promising biocatalyst for the efficient synthesis of n-3 PUFA-rich TAG by esterification of glycerol with n-3 PUFA in NADES systems.
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JOURNAL OF COLLOID AND INTERFACE SCIENCE
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2024
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IF 9.4
Le Zhong,Zhongjie Wang,Xiaohong Ye,Jiandong Cui,Ziyuan Wang,Shiru Jia
The catalytic performance of immobilized lipase is greatly influenced by functional support, which attracts growing interest for designing supports to achieve their promotive catalytic activity. Many lipases bind strongly to hydrophobic surfaces where they undergo interfacial activation. Herein, the behavioral differences of lipases with distinct lid structures on interfaces of varying hydrophobicity levels were firstly investigated by molecular simulations. It was found that a reasonable hydrophilic/hydrophobic surface could facilitate the lipase to undergo interfacial activation. Building on these findings, a novel “nest”-like superhydrophobic ZIFs (ZIFN) composed of hydrophobic ligands was prepared for the first time and used to immobilize lipase from Aspergillus oryzae (AOL@ZIFN). The AOL@ZIFN exhibited 2.0-folds higher activity than free lipase in the hydrolysis of p-Nitrophenyl palmitate (p-NPP). Especially, the modification of superhydrophobic ZIFN with an appropriate amount of hydrophilic tannic acid can significantly improve the activity of the immobilized lipase (AOL@ZIFN-TA). The AOL@ZIFN-TA exhibited 30-folds higher activity than free lipase, and still maintained 82% of its initial activity after 5 consecutive cycles, indicating good reusability. These results demonstrated that nanomaterials with rational arrangement of the hydrophilic/hydrophobic surface could facilitate the lipase to undergo interfacial activation and improve its activity, displaying the potential of the extensive application.
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LWT-FOOD SCIENCE AND TECHNOLOGY
·
2025
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IF 6.6
Tangyu Yang,Haiwei Jia,Yuting Song,Shiqi He,Bing Li,Lin Li,Xia Zhang
Sucrose fatty acid esters are increasingly valued as multifunctional surfactants, nutraceuticals, and bacteriostats due to their emulsifying and antimicrobial properties. While enzymatic synthesis provides an eco-friendly route to high-purity esters, challenges remain in optimizing lipase activity, reusability, and mass transfer. This study introduces a novel edible biomaterials-based catalytic system: lipase immobilized within shellac nanoparticle-coated chitosan microgels (SCL) for synthesizing sucrose laurate via Pickering interfacial catalysis (PIC). SCL stabilized oil-in-water (O/W) emulsions, with sucrose and vinyl laurate partitioned into aqueous and oil phases, respectively. Structural characterization (SEM, CLSM, Cryo-SEM) revealed SCL's localization at the O/W interface, with preferential oil-phase immersion and ordered interfacial alignment. Optimized conditions yielded a conversion rate of 55.35 ± 1.88 %, and the immobilized lipase retained >80 % activity over four cycles. Purified via solvent extraction and chromatography, the product was confirmed as 6-sucrose monolaurate (through FT-IR, NMR, XRD, and TG-DSC). Comparative analysis demonstrated its higher air/water interfacial stabilization versus commercial sucrose monoesters, evidenced by lower critical micelle concentration ( cmc ), enhanced emulsifying/foaming capacity, and improved pH/thermal stability. Collectively, this SCL-based PIC system achieved sustainable synthesis of 6-sucrose monolaurate with exceptional enzyme recyclability, overcoming limitations in lipase stability and mass transfer, and produced a surfactant with superior properties.
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PLANT JOURNAL
·
2025
·Vol. 123
·期 4
·e70440
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IF 5.7
Na Chen,Yu-Die Xiong,Chi Zou,Yu-Wei Zhong,Hui Du,Yu-Jie Chi,Chan Zhao,Shu-Sheng Liu,Xiao-Wei Wang
SUMMARY Piercing-sucking insects, such as whiteflies and aphids, cause massive economic losses in major crops around the world. During feeding, the stylets of piercing-sucking insects navigate cuticles, cell walls, epidermal cells, and mesophyll cells; thus, these barriers are vital for the resistance of plants to insects. However, the relationship between insect stylet probing behavior and the composition and structure of these barriers remains unclear. Here, we identified a tobacco Cuticle Related Factor ( NtCRF ), which was induced significantly by whitefly infestation. Bioassays showed that NtCRF positively regulated plant resistance against whiteflies and green peach aphids. Silencing of NtCRF did not affect plant jasmonic acid (JA) and salicylic acid (SA) defenses but shortened the stylet probing time of phloem-feeders. Further studies confirmed that silencing of NtCRF resulted in significant structure destruction of the leaf cuticle and led to increased epidermal permeability. Overexpression of NtCRF in Arabidopsis also significantly enhanced the plant's resistance against whiteflies and green peach aphids. Our findings expand understanding of plant–insect interactions and provide a strategy for genetic improvement of crop resistance against piercing-sucking insects.
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Catalysts
·
2024
·Vol. 14
·期 3
·180
·
IF 3.8
Xiaoxiao Dong,Chengnan Zhang,Prasanna J. Patil,Weiwei Li,Xiuting Li
Metal–organic frameworks (MOFs) are regarded as excellent carriers for immobilized enzymes due to their substantial specific surface area, high porosity, and easily tunable pore size. Nevertheless, the use of UIO−66 material is significantly limited in immobilized enzymes due to the absence of active functional groups on its surface. This study comprised the synthesis of UIO−66 and subsequent modification of the proline (Pro) on UIO−66 through post-synthetic modification. UIO−66 and UIO−66/Pro crystals were employed as matrices to immobilizeRhizopus oryzaelipase (ROL). The contact angle demonstrated that the introduction of Pro onto UIO−66 resulted in favorable conformational changes in the structure of ROL. The immobilized enzyme ROL@UIO−66/Pro, produced via the covalent-bonding method, exhibited greater activity (0.064715 U/mg (about 1.73 times that of the free enzyme)) and stability in the ester hydrolysis reaction. The immobilized enzymes ROL@UIO−66 (131.193 mM) and ROL@UIO−66/Pro (121.367 mM), which were synthesized using the covalent-bonding approach, exhibited a lowerKmand higher substrate affinity compared to the immobilized enzyme ROL@UIO−66/Pro (24.033 mM) produced via the adsorption method. This lays a solid foundation for the industrialization of immobilized enzymes.
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Small
·
2025
·
IF 12.1
Qi Ao,Lin Jiang,Ying Song,Xinglai Tong,Tuohao Jiang,Jun Tang
Enzyme immobilization has emerged as a promising strategy to facilitate the industrialization of biomolecules. However, immobilized systems are now still facing great challenges such as maintaining enzyme activity, large-scale manufacturing recovery and leaching or conformational changes of enzymes. Therefore, advanced enzyme immobilization techniques (efficient, stable and tunable catalysis) are currently an important challenge in this field. Here, enzyme@cyclodextrin covalent organic framework films are synthesized by template method and further constructed three-dimensional (3D) hydrogen bond-enhanced efficient MXene/enzyme membrane reactor. This strategy provides a spacious microenvironment for the release of enzyme molecules, a simpler process, an easier-to-etch template, a more biocompatible carrier. Furthermore, a versatile platform for interfacial photothermal and fast mass-transfer by constructing films with MXene. The obtained biocatalysts have excellent reusability, high activity and stability, which can be used as efficient biocatalysts for important industrial reactions. The enzyme membrane reactor is constructed by the ‘smart capsule ’ with enzyme@cyclodextrin-COF structure. The strategy can solve the challenging problems of the original previous enzyme immobilization system. Overall, a new idea is provided for the green, efficient, stable and sustainable general enzyme catalytic platform.
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BIOCHEMICAL ENGINEERING JOURNAL
·
2025
·
IF 3.8
Hui Fang,Yuanyuan Deng,Zhihao Zhao,Jiarui Zeng,Mingwei Zhang,Pengfei Zhou
Improving catalytic performance represents a highly desirable but challenging objective for the immobilization of biocatalysts. A novel biocatalyst of ANL@Fe 3 O 4 -SiO 2 -APTES was fabricated by immobilizing Aspergillus niger lipase (ANL) onto amino-alkyl group-modified magnetic nanoparticles. This biocatalyst exhibited an enzyme loading of 127.68 mg/g and the specific activity of 1132.26 U/g. The superior activity and recyclability of ANL@Fe 3 O 4 -SiO 2 -APTES was validated. The outstanding performance for the enzymatic interesterification (EIE) of palm stearin (PS) and rice bran oils (RBO) was observed. The significantly decreased the solid fat content (SFC) and enhanced crystallization rate of oils was achieved, as well as the β' type of oils after EIE was obtained. Moreover, molecular dynamics simulations were conducted to elucidate the underlying catalytic mechanism of EIE. This study proposes a highly efficient and sustainable approach for the chemical modification of lipids, thereby promoting its broad application in the food industry.
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JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2025
·
IF 3.5
Kai Yu,Wenjing Jiang,Ningning Cheng,Baorui Li,Jiao Xie,Aizhen Zong,Ye Zhang,Hao Wang
BACKGROUND Naringin, a natural flavonoid compound, has demonstrated potential anti-obesity effects by modulating lipid metabolism. Pancreatic lipase plays a critical role in lipid digestion and absorption, making it a key target for obesity management. This study investigated the inhibitory mechanism of naringin on pancreatic lipase through in vitro , in vivo , and in silico experiments. RESULTS In vitro experiments revealed that naringin was a competitive inhibitor of pancreatic lipase, with a half-maximal inhibitory concentration (IC₅₀) of 6.93 ± 0.12 mmol/L. Multi-fluorescence spectroscopy confirmed that naringin induced secondary structure changes and static fluorescence quenching of pancreatic lipase, with a binding constant of 2.16 × 10 4 L/mol. Isothermal titration calorimetry indicated a spontaneous exothermic reaction (−26.08 kJ/mol), mainly driven by hydrogen bonding and electrostatic force. In vivo studies demonstrated that naringin decreased serum lipase activity by 24.54%, mitigated hepatic lipid accumulation, and down-regulated inflammatory cytokines in high-fat diet-induced obese rats. Molecular simulation further revealed that hydrogen bonding was the primary interaction force between naringin and pancreatic lipase. CONCLUSIONS Naringin effectively inhibits pancreatic lipase through competitive binding and structural modifications, reducing lipid digestion and absorption. The inhibitory effect of naringin on pancreatic lipase might provide new insights into the role of naringin in lipid metabolism regulation and potential application in obesity management. © 2025 Society of Chemical Industry.
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MICROPOROUS AND MESOPOROUS MATERIALS
·
2024
·
IF 4.8
Yang Zhou,Zhenzhu xia,Frank Peprah Addai,Jinping Chen,Chengxiang Feng,Zongjian Zhen,Juan Han,Feng Lin,Zhirong Wang,Yun Wang
Most pristine metal organic frameworks (MOFs) are inherently microporous. To introduce desired porosity for easy enzyme infiltration and immobilization, polystyrene spheres was used as sacrificial template to design hierarchical ordered micro-mesoporous truncated single-crystalline ZIF-8 (SOM-ZIF-8). The surface area and pore diameter of the SOM-ZIF-8 were 821 m 2 /g and 7.09 nm which changed to 669 m 2 /g and 4.98 nm respectively, after lipase immobilization, suggesting the pores and surface of the SOM-ZIF-8 served as binding sites for the enzyme, and could reach a loading capacity of 134 mg/g after 24 h. The optimal conditions for achieving maximum lipase activity for free LipaseELP, ZIF-8@LipaseELP and SOM-ZIF-8@LipaseELP were pH 7.8 at 45 °C, and maintained 33.67 %, 45.6 % and 57.78 % residual activity after incubation at 80 °C for 2 h. The specific activity towards tributyrin and p-nitrophenyl acetate were observed to be SOM-ZIF-8@LipaseELP (0.25 and 45.85 U/mg) compared to ZIF-8@LipaseELP (0.211 and 43.62 U/mg) and LipaseELP (0.179 and 41.09 U/mg) respectively. The SOM-ZIF-8@LipaseELP could further be recovered and reused for 9 rounds while maintaining 73.8 % of its original activity. This study demonstrates that introducing mesoporous structures into ZIF-8 could improve its binding enzyme property for enhanced hydrolytic function.
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JOURNAL OF FOOD SCIENCE
·
2025
·Vol. 90
·期 5
·e70302
·
IF 3.4
Pengfei Zhou,Hui Fang,Zhihao Zhao,Guang Liu,Jiarui Zeng,Yuanyuan Deng,Mingwei Zhang
The precise regulation of enzyme conformation through the immobilization of enzymes on carriers using sewing techniques represents a key focus in the site-specific chemically modification engineering. Lipase-mediated enzymatic interesterification (EIE) is of considerable significance in lipid chemistry, having demonstrated substantial potential in the modification of lipids. In this study, we developed an innovative nanomaterial Fe 3 O 4 -SiO 2 -APTES for site-specific immobilization of Thermomyces lanuginosus lipase (TLL), achieving an immobilization yield of 51.98% and an enzyme loading capacity of 123.18 mg/g. The specific activity of the enzyme was 1034.09 U/g following lyophilization, representing increases of 2.6-fold compared to free TLL. The as-prepared biocatalyst TLL@Fe 3 O 4 -SiO 2 -APTES exhibited enhanced catalytic activity, remarkable tolerance to organic solvents, substrate selectivity, and recyclability over multiple cycles. Rice bran oils (RBO) and palm stearin (PS) were employed as substrates for EIE, yielding oils with better performance of solid fat content (SFC), crystallization rate, and thermodynamic properties compared to those of physical blending oils. Additionally, we investigated the catalytic mechanism of EIE using molecular docking analysis. The present study provides a theoretical foundation for the application of immobilized lipase as biocatalysts in food industrial settings. Practical Application : TLL@Fe 3 O 4 -SiO 2 -APTES, modified at specific sites using nanomaterials, not only enhances the catalytic efficiency of the enzyme but also facilitates its reuse across multiple batches. This fixed enzyme could effectively catalyze the transesterification between PS and RBO, resulting in high-quality of oils specifically designed for baking foods. The findings in this study provide valuable guidance for the green processing of oils and fats.
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2012
·
IF 2.823
Xiao-Li Qin,Bo Yang,Hui-Hua Huang,Yong-Hua Wang
Tripalmitin-enriched triacylglycerols were concentrated from palm stearin by acetone fractionation and as the substrate reacted with a mixture of equimolar quantities of fatty acids (C8:0–C18:3). The incorporation degree and acyl migration level of the fatty acids and acylglycerols composition were investigated, providing helpful information for the production of human milk fat substitutes. Higher incorporation degrees of the fatty acids were obtained with lipase PS IM, Lipozyme TL IM, and Lipozyme RM IM followed by porcine pancreatic lipase and Novozym 435-catalyzed acidolysis. During reactions catalyzed by Lipozyme TL IM, Lipozyme RM IM, and lipase PS IM, incorporation degrees of C12:0, C14:0, C18:1, and C18:2 were higher than those of other fatty acids at operated variables (molar ratio, temperature, and time), and the triacylglycerols content reached the highest (82.09%) via Lipozyme RM IM-catalyzed acidolysis. On the basis of significantly different levels of acyl migration to the sn-2 position, lipases were in the order of lipase PS IM < Lipozyme TL IM < Lipozyme RM IM.
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