CARBOHYDRATE POLYMERS
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2022
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IF 10.723
Liang Qi,Yu-jing Zhou,Zhi-gang Luo,Qun-yu Gao,Yong-Cheng Shi
To develop recyclable biocatalyst used in Pickering interfacial systems, the pH-responsive monomer [2-(dimethylamine)ethyl methacrylate] (DMAEMA) was grafted onto the maize starch molecule via free radical polymerization . Subsequently, combined with the gelatinization-ethanol precipitation and lipase ( Candida rugosa ) absorption process, an enzyme-loaded starch nanoparticle with DMAEMA grafting (D-SNP@CRL) was tailor-made, showing a nanometer size and regular sphere. X-ray photoelectron spectroscopy and confocal laser scanning microscopy confirmed a concentration-induced enzyme distribution within D-SNP@CRL, thereof the outside-to-inside enzyme distribution was proved to be optimum in achieving the highest catalytic efficiency . Benefited from the tunable wettability and size of D-SNP@CRL under pH variation, the generated Pickering emulsion could be readily applied as the recyclable microreactors for the n-butanol/vinyl acetate transesterification . This catalysis exhibited both highly catalytic activity and good recyclability, making the enzyme-loaded starch particle a promising green and sustainable biocatalyst in the Pickering interfacial system.
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JOURNAL OF COLLOID AND INTERFACE SCIENCE
·
2019
·
IF 6.361
Hongbo Suo,Lili Xu,Chao Xu,Xiang Qiu,He Huang,Yi Hu
We prepared ionic liquids (ILs) modified magnetic alginate nanoparticles and used these as supports for lipase immobilization. The novel supports were characterized using Fourier transform infrared (FTIR) spectroscopy, nuclear magnetic resonance ( 1 HNMR), vibrating sample magnetometry (VSM), thermogravimetry (TG), transmission electron microscopy (TEM) and water contact angle (WCA) measurements. The immobilized lipase (PPL-IL-MSA) exhibited high activity, 2.1-fold higher than that compared to free lipase and 1.59-fold higher compared to immobilized lipase without IL (PPL-MSA). In addition, the pH and temperature application range of PPL-IL-MSA were both found to be broader than that of free lipase and PPL-MSA. The thermal stability, denaturation stability, and reusing stability of PPL-IL-MSA were also higher than those of other samples. After 10 times of reuse, the residual activity of PPL-IL-MSA was 89.7% higher than that of PPL-MSA (84.4%). Furthermore, the kinetic constant K m of PPL-IL-MSA was 13.7 mg/mL lower than that of free lipase (21.2 mg/mL) and PPL-MSA (18.4 mg/mL). Circular dichroism (CD) was used to study the secondary structure of enzymes in order to explain the mechanism of the performance improvement of PPL-IL-MSA. This work involving the development of a new supports for enzyme immobilization may serve as a reference for further studies in this field.
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Materials Science & Engineering C-Materials for Biological Applications
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2018
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IF 5.08
Hongbo Suo,Zhen Gao,Lili Xu,Chao Xu,Dinghua Yu,Xinran Xiang,He Huang,Yi Hu
We developed magnetic chitosan nanoparticles (CS‑Fe 3 O 4 ) with mean diameter of 15–20 nm. Subsequently, these inorganic-organic composite nanoparticles were modified using an imidazole-based functional ionic liquid (IL). The prepared support (IL‑CS‑Fe 3 O 4 ), which was used to immobilize porcine pancreatic lipase (PPL), was characterized using Fourier transform infrared (FTIR) spectroscopy, vibrating sample magnetometry (VSM), thermogravimetry (TG), transmission electron microscopy (TEM) and X-ray diffraction (XRD). Circular dichroism (CD) was used to analyze the secondary structure of immobilized PPL. The immobilized PPL (PPL‑IL‑CS‑Fe 3 O 4 ) exhibited 1.93-fold higher specific activity than PPL‑CS-Fe 3 O 4 when triacetin was used as the substrate, and showed 95 mg/g of lipase immobilization capacity and 382% of activity recovery. The residual activity of PPL‑IL‑CS‑Fe 3 O 4 was above 60% of the initial activity after incubation at 50 °C for 6 h, as was higher than that of PPL‑CS‑Fe 3 O 4 which showed 40% of the initial activity. In addition, PPL‑IL‑CS‑Fe 3 O 4 retained 84.6% of the initial activity after 10 cycles, whereas PPL‑CS‑Fe 3 O 4 retained only 75.5% activity. Furthermore, the kinetic parameters, apparent K m and V max of PPL‑IL‑CS‑Fe 3 O 4 were 2.51 mg/mL and 1.395 U/mg respectively, these results indicated that the immobilized PPL had better affinity towards the substrate, especially when the nanoparticles were modified by functional IL. Besides, the magnetic chitosan nanoparticles loaded with PPL were easily recovered. A novel, efficient, and practical method for enzyme immobilization was developed.
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ENZYME AND MICROBIAL TECHNOLOGY
·
2019
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IF 3.553
Yue Zhang,Wenhui Sun,Nora Mohamed Elfeky,Yuepeng Wang,Dongying Zhao,Hao Zhou,Jingyun Wang,Yongming Bao
Lipase ZC12, a cold-adapted lipase derived from Psychrobacter sp. ZY124, can be effectively activated by Ca 2+ . Inspired by this significant property, we developed a novel immobilized lipase ZC12/Ca 3 (PO 4 ) 2 hybrid nanoflowers (LHNs). The LHNs have been characterized as a regular hierarchical flowerlike structure nanoflowers by scanning electron microscopy (SEM). Compared with free lipase ZC12, the LHNs exerted enhanced enzymatic activity of 206% and 2.31-fold in k cat / K m value, especially high specific activity at low temperature. After 7 successive cycles, the LHNs could still maintain its initial activity, demonstrating superior durability than the free lipase ZC12. Meanwhile, its stability basically kept unchanged in a wide range of temperature and pH. Finally, fructose laurate was transformed by the LHNs with 57.39% conversion rate which is twice as much as the free lipase. To sum up, these results validated that LHNs could emerge as an efficient immobilized lipase and possess the promising potential for practical applications.
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ELECTROCHIMICA ACTA
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2018
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IF 5.116
Baokai Ma,Ling-Zhi Cheong,Xinchu Weng,Chin-Ping Tan,Cai Shen
Organophosphorus pesticides especially p -nitrophenyl pesticides (methyl parathion) have neurotoxic effects and it is a difficult to remove organophosphorus pesticides residues from contaminated water. Present work has developed a sensitive, direct and rapid lipase@ZIF-8/chitosan/glassy carbon electrode (GCE) and lipase@amine-modified ZIF-8(An-ZIF-8)/chitosan/GCE biosensors for detection of methyl parathion . ZIF-8 and An-ZIF-8 nanoparticles which are a type of metal-organic frameworks with large surface area and high porosity have been facilely prepared under mild biocompatible conditions and used as lipase immobilization matrixes in the biosensors. The optimized lipase@ZIF-8/chitosan/GCE and lipase@An-ZIF-8/chitosan/GCE biosensors can detect methyl parathion with a wide linear range, good repeatability, recovery and limit of detection as low as 0.28 μM. The as-prepared biosensors can be stored in 0.05 M PBS (pH 7) at 4 °C and reused for at least 20 days with a retainment of at least 80% of its initial response to methyl parathion. This indicated that both ZIF-8/chitosan and An-ZIF-8/chitosan are suitable for immobilization of lipase that favors generation of p -nitrophenol from methyl parathion; and subsequent electrochemical oxidation and electron transfer of the p -nitrophenol.
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COLLOIDS AND SURFACES B-BIOINTERFACES
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2017
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IF 3.887
Yuling Su,Lili Zhao,Fancui Meng,Quanxin Wang,Yongchao Yao,Jianbin Luo
In order to improve the antibacterial activities while decrease the cytotoxity of silver nanoparticles, we prepared a novel nanocomposites composed of silver nanoparticles decorated lipase-sensitive polyurethane micelles (PUM-Ag) with MPEG brush on the surface. The nanocomposite was characterized by UV–vis, TEM and DLS. UV–vis and TEM demonstrated the formation of silver nanoparticles on PU micelles and the nanoassembly remained intact without the presence of lipase. The silver nanoparticles were protected by the polymer matrix and PEG brush which show good cytocompatibility to HUVEC cells and low hemolysis. Moreover, at the presence of lipase, the polymer matrix of nanocomposites is subject to degradation and the small silver nanoparticles were released as is shown by DLS and TEM. The MIC and MBC studies showed an enhanced toxicity of the nanocomposites to both gram negative and gram positive bacteria, i.e. E. coli and S. aureus , as the result of the degradation of polymer matrix by bacterial lipase. Therefore, the nanocomposites are biocompatible to mammalian cells cells which can also lead to activated smaller silver nanoparticles release at the presence of bacteria and subsequently enhanced inhibition of bacteria growth. The satisfactory selectivity for bacteria compared to HUVEC and RBCs make PUM-Ag a promising antibacterial nanomedicine in biomedical field.
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JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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2013
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IF 2.823
Jian-Yong Zheng,Sheng-Fan Wang,Yin-Jun Zhang,Xiang-Xian Ying,Yu-guang Wang,Zhao Wang
A chemoenzymatic methodology for the asymmetric synthesis of d -biotin intermediate lactone ((3a S , 6a R )-tetrahydro-1,3-dibenzylhexahydro-1 H -Furo[3,4-d] imidazole-2,4-dione) 1 has been demonstrated. The key step of the synthetic routes is Lipozyme RM IM catalyzed desymmetrization of meso-diols 3 . The highest enantiomeric excess ( e.e. > 98%) and yield (>90%) of the product was achieved with Lipozyme RM IM in Dioxane/Toluene (1:3, v/v) at 35 °C. Furthermore, Lipozyme RM IM showed an excellent operational stability, retaining above 80% of the initial activity after 10 cycles of reaction. d -Biotin intermediate lactone 1 was obtained subsequently by Jones oxidation, basic hydrolysis and lactonization.
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JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
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2024
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IF 1.9
Wenlin Li,Sen Lin,Dongming Lan,Yonghua Wang
Vitamin E succinate has gained substantial attention as a potential therapeutic agent for cancer treatment due to its biomedical activities. One of the prominent methods of synthesizing vitamin E succinate is through enzymatic processes, which, although advantageous, presents inherent challenges related to optimization, scalability, and particularly, the poor stability of lipases in organic solvents. Our study addresses these challenges by conducting a comprehensive comparative analysis between Lipase UM1 and three other immobilized commercial lipases, demonstrating Lipase UM1's enhanced resistance to organic solvents and its superior efficiency in vitamin E succinate production. Further optimization experiments with Lipase UM1 led to an unprecedented conversion of 99%. Additionally, we scaled the reaction to a proof-of-concept industrial level. The synthesized product was verified using Fourier transform infrared spectroscopy and nuclear magnetic resonance analysis, ensuring its quality and consistency. This study validates Lipase UM1 as an efficient catalyst for vitamin E succinate synthesis, offering a promising avenue for industrial production with potential applications in cancer therapy and beyond. Graphical Vitamin E succinate (VES) was synthesized through the catalysis of the organic solvent-stable Lipase UM1, resulting in an exceptional conversion.
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Molecular Catalysis
·
2024
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IF 3.9
Xiaoyuan Zhang,Yunjian Ma,Bo Ouyang,Yonghua Wang,Fanghua Wang
Ceramide III (CER III) series compounds are essential constituents in cosmetic formulations and dermatological applications. As the cosmetics industry trends toward more sustainable practices, the development of an eco-friendly synthesis method for these vital compounds is increasingly critical. This research introduces a sustainable technique for producing CER III series compounds, using lipase-catalyzed amidation of phytosphingosine with various fatty acid esters or natural oils in an eco-compatible solvent. Through an extensive examination of various lipases and eco-friendly solvents, we first identified Novozym 435 as the most efficient biocatalyst and cyclopentyl methyl ether (CPME) as the preferred solvent. This combination established a high-efficiency reaction system for CER III series compounds synthesis. We further optimized the enzymatic conditions - a substrate molar ratio of 1:1, lipase loading at 30 wt%, at 65 °C, which presented an impressive yield of 94 % for ceramide IIIB (CER IIIB). We also investigated the reusability of enzymes in this synthetic system and further extended the scope of acyl donors using natural oils, results indicating the method excellent potentiality in industrial settings. In summary, this study provides a green and efficient pathway for synthesizing CER III series compounds, aligning with the growing eco-conscious trends in cosmetic science and technology.
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MOLECULES
·
2024
·Vol. 29
·期 10
·2381
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IF 4.2
Liran Ji,Wei Zhang,Yifei Zhang,Binbin Nian,Yi Hu
The development of immobilized enzymes with high activity and stability is critical. Metal–organic frameworks (MOFs) have attracted much academic and industrial interest in the field of enzyme immobilization due to their unique properties. In this study, the amino-functionalized ionic liquid (NIL)-modified metal–organic framework (UiO-66-NH2) was prepared to immobilizeCandida rugosalipase (CRL), using dialdehyde starch (DAS) as the cross-linker. The results of the Fourier transform infrared (FT-IR) spectra, X-ray powder diffraction (XRD), and scanning electronic microscopy (SEM) confirmed that the NIL was successfully grafted to UiO-66-NH2. The CRL immobilized on NIL-modified UiO-66-NH2(UiO-66-NH2-NIL-DAS@CRL) exhibited satisfactory activity recovery (79.33%), stability, reusability, and excellent organic solvent tolerance. The research results indicated that ionic liquid-modified UiO-66-NH2had practical potential for application in enzyme immobilization.
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PROCESS BIOCHEMISTRY
·
2024
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IF 3.7
Hongbo Suo,Xinzheng Liu,Shu Chen,Qi Li,Xiangnan Liu,Lili Xu
Biodiesel is more environmentally friendly compared to traditional petroleum diesel. The method of producing biodiesel catalyzed by lipases, as a green chemistry technology, can further reduce its negative impact on the environment. In this work, lipase immobilized on magnetic cellulose was embedded in Cu(PABA), and then the biocomposite (MCL@Cu(PABA)) was used for biodiesel production. The good biocompatibility and flexible skeleton structure of cellulose can buffer the compression effect on enzyme molecules during the formation of Metal-Organic Frameworks (MOFs), and the MOFs protective layer can reduce the damage caused by denaturants to enzyme molecules. The biocatalyst showed enhanced activity and stability with a lower deactivation constant ( K d ). Under the optimized reaction conditions, the biodiesel yield can reach 78.4 %. After reused for 7 times, the biocatalyst can still achieve a biodiesel yield of 58.8 %. Moreover, after stored for 30 days, the biodiesel yield can still reach 70.3 %. For all experimental yields, the standard deviation (SD) ranged from 2.4 % to 4.5 %. Secondary structure analysis showed that the rigid structure and active conformation of lipase was enhanced after Cu(PABA) encapsulation.
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ACS Applied Polymer Materials
·
2024
·
IF 4.4
Xingxing Ding,Zhonglin He,Jin Mao,Qi Zhou,Qianchun Deng,Lei Zheng,Jie Shi
In this work, we presented an external stimulating Pickering interfacial biocatalyst (PIB), which is a gelatin and Candida rugosa lipase (CRL) complex containing polydopamine (PDA) nanobottles (PDA@G-CRL). This created PDA nanobottles are employed as emulsifiers and enzyme carriers for the PIB system, showing an excellent energy saving effect during the reaction. They are made utilizing the polystyrene (PS) template technique, and after lipase is entrapped with gelatin gel assistant, by exploiting the photothermal properties of PDA under near-infrared (NIR) irradiation, these nanobottles may efficiently stabilize the oil-in-water (O/W) emulsion and cause the release of gelatin–lipase complex, producing the PIB effect. The encapsulated lipase rate and minimum loading rate of lipase in PDA nanobottles are 50.76% and 263 mg g–1, respectively, which is 3.59 times higher than that of free lipase. In the biosynthesis phytosterol, the esterification rate of PIB reached 78% after 34 h of reaction, which was 3.4 times higher than that of free lipase in a single-phase system, and after 5 cycles, the relative activity remained at 51.33%. In particular, in terms of energy consumption, our proposed method is 227 times lower than that of traditional heating methods. It is believed that this smart PIB is able to contribute insights into green biocatalysis areas.
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