RSC Advances
·
2017
·Vol. 7
·期 21
·12518-12523
·
IF 3.108
Pengfei Zhou,Xuping Wang,Bo Yang,Frank Hollmann,Yonghua Wang
Epoxides are important synthetic intermediates for the synthesis of a broad range of industrial products. This study presents a promising solution to the current limitation of enzyme instability. By using simple deep eutectic solvents such as choline chloride/sorbitol, significant stabilization of the biocatalyst has been achieved leading to more robust reactions while using environmentally more acceptable solvents as compared to ionic liquids.
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CHEMICAL PAPERS
·
2017
·Vol. 69
·期 10
·1298-1311
·
IF 1.258
Shao Yong-Bo,Jing Tao,Tian Jing-Zhi,Zheng Yong-Jie,Shang Ming-Hui
In this paper, Fe 3 O 4 nanoparticles coated with mesoporous silica were prepared successfully, noted as Fe 3 O 4 at the mobile composition of matter No. 41 (MCM-41). Also, Fe 3 O 4 at MCM-41 was grafted by both 3-aminopropyltriethoxysilane (APTS) and 3-chloropropyltriethoxysilane (CPS), noted as Fe 3 O 4 at MCM-41/APTS and Fe 3 O 4 at MCM-41/CPS. The compounds were characterized by X-ray powder diffraction, scanning electron microscopy, transmission electron microscopy, Fourier transform infrared spectroscopy, vibrating sample magnetometry, thermogravimetry and N 2 adsorption/desorption. Then, the enzyme, porcine pancreas lipase (PPL), was immobilized onto these modified nanoparticles by covalent attachment, physical adsorption and cross-linking, noted as Fe 3 O 4 at MCM-41/CPS-PPL, Fe 3 O 4 at MCM-41-PPL and Fe 3 O 4 at MCM-41/APTS-PPL, respectively. The results showed that Fe 3 O 4 at MCM-41/CPS was the best nanomaterial for PPL immobilization, exhibiting enhanced immobilization efficiency (maximum 96%), maximum relative activity (up to 96%), high stability and reusability (83% 56 days and 86.7% ten cycles). Additionally, it offered some other advantages, such as easy recycling and reuse, complying with the trend of green chemistry. Therefore, Fe 3 O 4 at MCM-41/CPS in combination with a relevant method can be proposed for commercial applications.
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Journal of Environmental Chemical Engineering
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2024
·
IF 7.4
Jing Li,Xiang-Dong Xu,Jian Zhang,Xin-Yi Sui,Jian-Bo Qu
Macroporous polystyrene microspheres have been extensively used as an efficient carrier for lipase immobilization owing to the hydrophobic surface , excellent mechanical strength and chemical stability, easy to recycle and low cost. However, conventional polystyrene microspheres usually have a pore size of less than 100 nm and an extremely hydrophobic surface lacking functional groups, which bring a series of problems such as low enzyme loading, activity recovery, reusability, serious leakage, and high substrate diffusion limitation. In this work, a novel generation of gigaporous polystyrene microspheres with moderately hydrophilic surfaces was specifically designed as an enzymatic carrier. The microspheres were featured with micropores (∼ 9 nm), mesopores (∼ 54 nm), and gigapores (∼ 948 nm), ensuring native enzyme structure preservation and high loading capacity. After epoxy activation, the lipase PS from Burkholderia cepacia (PPL) was site-specifically immobilized onto the microspheres. The resultant immobilized PPL exhibited 95 % activity recovery at a maximum loading of 115.3 mg/g. Also, the immobilized PPL surpassed free PPL in pH and temperature tolerances, temperature and storage stabilities, and achieved a 91.6 % yield in benzyl cinnamate biosynthesis. Besides, excellent reusability of the immobilized PPL was demonstrated with an 80.1 % yield after 10 cycles. Overall, these gigaporous microspheres show great potential for the highly efficient immobilization of lipase and enhanced benzyl cinnamate production.
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RSC Advances
·
2024
·Vol. 14
·期 16
·10953-10961
·
IF 3.9
Shi-Yi Zhang,Guo-Neng Fu,Li-Hua Du,Hang Lin,Ao-Ying Zhang,Han-Jia Xie,Zhi-Kai Sheng,Miao-miao Xue,Bing-lin Yan,Yi Liu,Zhi-Xuan Ruan,Bing-Le Pan,Tong-Yao Zhou,Xi-Ping Luo
Purine nucleoside ester is one of the derivatives of purine nucleoside, which has antiviral and anticancer activities. In this work, a continuous flow synthesis of purine nucleoside esters catalyzed by lipase TL IM from Thermomyces lanuginosus was successfully achieved. Various parameters including solvent, reaction temperature, reaction time/flow rate and substrate ratio were investigated. The best yields were obtained with a continuous flow microreactor for 35 min at 50 °C with the substrate ratio of 1 : 5 (nucleosides to vinyl esters) in the solvent of tert-amyl alcohol. 12 products were efficiently synthesized with yields of 78–93%. Here we reported for the first time the use of lipase TL IM from Thermomyces lanuginosus in the synthesis of purine nucleoside esters. The significant advantages of this methodology are a green solvent and mild conditions, a simple work-up procedure and the highly reusable biocatalyst. This research provides a new technique for rapid synthesis of anticancer and antiviral nucleoside drugs and is helpful for further screening of drug activity.
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FOOD CHEMISTRY
·
2025
·
IF 9.8
Xiaolu Liu,Yao Li,Xuan Ji,Xu Fei,Jing Tian,Longquan Xu,Yi Wang
Lipase-catalyzed esterification for enhancing oil quality has garnered extensive attention due to its eco-friendly and efficient merits. Nevertheless, during the catalytic esterification process at the oil-water interface to reduce acid value, the immobilized lipase is prone to detachment as a result of continuous mechanical agitation. In this study, inspired by the aerodynamic theory of golf ball surfaces, a novel immobilized enzyme system is designed and fabricated to improve the quality of Antarctic krill oil and prolong its storage time. The surface of the poly-pullulan hydrogel microspheres is chemically modified to expose numerous active reaction sites, forming a pitted structure similar to that of a golf ball. These pits on the surface of the microspheres can effectively mitigate the impact of the oil phase fluid on the immobilized enzyme on the surface of the carriers during the catalytic process, reducing lipase shedding and enhancing the catalytic reuse rate of the immobilized enzyme system. The obtained immobilized enzyme microspheres can still retain 70.1 % of the initial activity after 10 reuses. The high acid value of Antarctic krill oil (10.14mgKOH/g) can be effectively esterified and deacidified, and the acid value can be decreased to 2.18mgKOH/g.
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Food Bioscience
·
2024
·
IF 4.8
Yuyang Zhang,Ting Feng,Xing Ni,Jiaojiao Xia,Hongbo Suo,Lishi Yan,Bin Zou
In this study, Candida rugosa lipase (CRL) was immobilized on the silica carrier SBA-15 by physical adsorption , then mixed with hydrophobically modified sodium alginate and dropped into calcium chloride solution. Finally, the adsorption-embedding immobilized lipase (L-SBA-15-Mgel) was successfully prepared. The conformation of the carrier before and after lipase immobilization were analyzed by scanning electron microscopy (SEM), thermogravimetric analysis (TGA), Fourier transform infrared spectroscopy (FT-IR) and other characterization techniques. The molecular docking and molecular dynamics simulation of CRL and modifier dodecyl glycidyl ether (DGE) ligand were carried out to analyze the potential influence of modifier on enzyme characteristics. The basic enzymatic properties including the activity, stability and reaction kinetic parameters of the immobilized lipase L-SBA-15-Mgel were studied. L-SBA-15-Mgel showed good storage stability and reusability. After 16 days of storage, the activity retention was 47.85%, and there was still 63.20% of the residual activity after seven cycles of reuse. The immobilized lipase was applied to the efficient synthesis of food flavor ester isoamyl acetate . Under the reaction conditions of 50 °C and 200 rpm, the highest yield of isoamyl acetate catalyzed by L-SBA-15-Mgel was 85.19%.
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PROCESS BIOCHEMISTRY
·
2024
·
IF 3.7
Shihao Liang,Wei Zhuang,Zhenfu Wang
In this work, isocyanate-based strategy was developed for efficient immobilization of Candida antarctica lipase B (CALB). Of 41 commercial resins, EP109 was chosen and hydrophobized with hydroxyl-terminated polydimethylsiloxane (HTPDMS) for tert-butyl isocyanate (tBIC)-based CALB immobilization due to high loading amount and specific activity. The tBIC-based strategy exhibited shorter immobilization time, higher loading and activity than adsorption strategy by hydrophobic interaction. When compared with free CALB, EP109-HTPDMS-tBIC@CALB owned improved stability (against acid, alkali, and heat) and storability. Subsequently, EP109-HTPDMS-tBIC@CALB was employed in the bio-synthesis of 1,3-diacylglycerol in a solvent-free system with a yield of 76.31%, which was higher than commercial Novozym 435 (53.93%). EP109-HTPDMS-tBIC@CALB exhibited 76.34% of residual activity after 20 repeat uses.
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JOURNAL OF COLLOID AND INTERFACE SCIENCE
·
2018
·
IF 5.091
Chunyu Zhang,Xiaoyan Dong,Zheng Guo,Yan Sun
Enzymes are promising biocatalysts for the production or degradation of chemical compounds, but low stabilities of free enzymes restrict their industrial applications. Therefore, development of effective immobilization methods to maintain or increase enzyme activity and stability remains a challenge. In this work, a novel support made of zwitterionic polymer-grafted silica nanoparticles (p-SNPs) was fabricated and Candida rugosa lipase (CRL) was covalently attached onto the p-SNPs. The zwitterionic polymer was a product of the reaction between poly(maleic anhydride- alt -1-octadecene) and N,N -dimethylenediamine and contained a cetane side chain. The hydrolytic activity , reaction kinetics, thermal stability, pH tolerance, storage stability and reusability of the immobilized CRL (SNPs-CRL) were investigated. It revealed that the specific activity of SNPs-CRL was two to four times higher than the free CRL in the temperature range of 25–60 °C. It is considered mainly due to the interfacial activation effect regulated by the cetane side chains of the zwitterionic polymer. Kinetic studies revealed remarkable improvement of the enzymatic reaction efficiency by the immobilized enzyme as demonstrated by the significant increases of the reaction rate constant and the decreases of Michaelis constant (i.e., increase of enzyme-substrate affinity) determined with two different substrates ( p -nitrophenyl acetate and p -nitrophenyl palmitate). Moreover, the immobilization improved the enzyme stabilities and SNPs-CRL displayed good reusability. Finally, the SNPs-CRL was proven to catalyze the hydrolysis of methyl mandelate to produce mandelic acid at an activity three times higher than the free enzyme. The results indicate that zwitterionic polymers deserved further development for enzyme immobilization.
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FOOD CHEMISTRY
·
2024
·
IF 8.5
Xuan Liu,Chunjin Huang,Dongming Lan,Weifei Wang,Yonghua Wang
Degumming is essential to eliminate undesired phospholipids from crude vegetable oils before being processed into high-quality products. The degumming efficiency is hampered by the separation of oil and water. To overcome this problem, we introduced an innovative enzymatic degumming strategy for various vegetable oils (rice bran, peanut and flaxseed oil) by combining phospholipase A1 with monoacylglycerol lipase. Compared to using phospholipase A1, the combination of the two enzymes significantly reduced phosphorus content, indicating better hydrolysis of phospholipids. Additionally, the primary hydrolysates by the combined enzymes were glycerylphosphorylcholine and glycerylphosphorylethanolamine that were more affinitive to water to improve oil-water separation and oil yield. Characteristic markers obtained from Partial Least Squares Discriminant Analysis model confirmed the advantages of combined enzymes over single enzyme. This advantage of combined enzymes was further validated in a simulated degumming process. Our findings provide a new enzymatic degumming strategy to expand the toolkit for crude oil refinery.
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LWT-FOOD SCIENCE AND TECHNOLOGY
·
2024
·
IF 6
Lilang Li,Kuntai Li,Ruiguo Cui,Fengjun Li,Jianrong Wang
Lipase from Thermomyces dupontii (TDL) shows great potential to prepare long-medium-long structured lipids (LML-SLs), but its poor thermostability represents a significant obstacle to further industrial application. Herein, a rational design based on structure and sequence analysis (including disulfide bond calculation and sequence alignment) was used to generate a more thermostable mutant. Compared with wild-type TDL, mutant M3 displayed a 9.1-fold, 7.2 °C and 10 °C increase in half-life ( t 1/2 ) at 60 °C, the half-loss temperature ( T 50 ) at 15 min and optimum temperature, respectively. Remarkably, the specific activity of mutant M3 was 49.1% higher than that of wild-type TDL. Molecular dynamics (MD) simulations showed that the structural flexibility of mutant M3 was reduced, which might contribute to the enhanced thermostability. Additionally, LML-SLs were synthesized from ethyl linoleate and tricaprylin with wild-type TDL and mutant M3. Compared with the wild-type TDL group, the LML-SL content of the mutant M3 group increased by 8.1%. This study will pave the way for the industrial application of TDL and provide valuable insights for enhancing the thermostability of other lipases.
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JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY
·
2011
·Vol. 87
·期 4
·553-558
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IF 1.818
Xiao-Feng Wang,Xu-Guang Shen,Yong-Chuan Sun,He-Yun Zhao,Li Xu,Yun Liu,Yun-Jun Yan
BACKGROUND: Yarrowia lipolytica lipase LIP2 (YlLIP2) is an important industrial enzyme that has many potential applications. Although it has been successfully expressed in Pichia pastoris under the control of the AOX1 promoter ( pAOX1 ), there have been many efforts to develop new alternative promoters to pAOX1 in order to avoid using methanol in the fermentation. Investigation of YlLIP2 production in P. pastoris using the formaldehyde dehydrogenase 1 promoter ( pFLD1 ) is especially attractive, since little is known about its application in methanol-free culture strategies. RESULTS: Three fed-batch cultivations were performed to investigate the production of YlLIP2 in a pFLD1 -based system. When methanol was used as the fed-batch feeding substrate, the maximum YlLIP2 activity obtained in a 10-L bioreactor was 30 000 U mL −1 after 143 h of culture, whereas the maximum YlLIP2 activity was further increased to 35 000 U mL −1 by adopting a co-induction strategy with methanol and methylamine as a mixed fed-batch substrate. Furthermore, the maximum YlLIP2 activity reached 13 000 U mL −1 after 80 h of cultivation in a methanol-free culture. CONCLUSION: The expression levels of YlLIP2 in the pFLD1 -based system were comparable with those in a pAOX1 -based system. The results suggest that pFLD1 is an attractive alternative to pAOX1 , and may make it feasible to induce high yields of protein expression. Copyright © 2011 Society of Chemical Industry
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Nanoscale
·
2024
·Vol. 16
·期 6
·3113-3120
·
IF 5.8
Hongxin Zhang,Xuegang Li,Xue Zhou,Yanan Zhang,Yong Zhao
As a low-density lipoprotein, tributyrin plays an essential role in food safety and human health. In this study, a novel lipase-conjugated carbon nanotube (CNT) surface plasmon resonance (SPR) fiber-optic sensor is used to specifically detect tributyrin for the first time. In this work, CNTs can be used as an amplifying material to significantly increase the sensitivity of SPR sensors due to their high refractive index and large surface area. CNTs can also be used as an enzyme carrier to provide abundant carboxyl groups for the specific binding of lipases. Covering the surface of the sensor with CNTs can not only enhance the performance of the sensor, but also provide sufficient detection sites for subsequent biomass detection, reduce the functionalization steps, and simplify the sensor preparation process. The experimental results demonstrate that the refractive index sensitivity of the traditional multimode fiber (MMF)–single mode fiber (SMF)–MMF transmissive optical fiber sensor is 1705 nm RIU−1. After covering the sensor with CNTs, the sensitivity is 2077 nm RIU−1, and the sensitivity has been improved very well. In addition, there are abundant functional groups on CNTs, which can provide abundant binding sites. Conjugating lipase on carbon nanotubes helps to achieve linear detection in the range of 0.5 mM to 4 mM tributyrin, with a sensitivity of 4.45 nm mM−1 and a detection limit of 0.34 mM, which is below the 2.26 mM detection standard and meets food safety monitoring requirements. Compared with other sensors, the optical fiber biosensor proposed in this study expands the concentration detection range of tributyrin. Furthermore, the sensor also has good stability, anti-interference performance and specificity. Therefore, the sensor proposed in this paper has good application prospects in the fields of food safety and biomedicine.
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