LWT-FOOD SCIENCE AND TECHNOLOGY
·
2019
·
IF 3.714
Xi Cao,Linmeng Liao,Fengqin Feng
Lipase catalysis has become the most promising technique for enrichment of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) due to its mild and green conditions. In this study, Trichosporon sp. F1-2 was newly isolated from oil-contaminated sludge, and its extracellular lipase was purified using ammonium sulfate precipitation and DEAE-Sepharose chromatography. The molecular weight of the lipase was estimated to be 32.6 kDa. The optimal temperature and pH for lipase activity were 50 °C and 8.0, respectively, and the optimal storage conditions were found to be temperatures below 45 °C and pH 7.0–9.0. The lipase did not require metal ions as cofactors and was significantly inhibited by Zn 2+ . It was stable in various organic solvents with different log P values, and n-hexane, toluene, dichloromethane, diethyl ether and glycerol even enhanced its activity. It had sn -1,3 regioselectivity and the highest activity towards a medium-chain fatty acid (C8) ester. This study demonstrated the lipase has good potential as a catalyst in enrichment of EPA and DHA in fish oil. The content of EPA and DHA reached 22.9 and 25.4 mol%, respectively, using 100 U of the lipase within 24 h, and the enrichment efficiency of DHA was higher than that of EPA.
✓ 已验证
产品关联
DOI
高影响因子
ACS Applied Nano Materials
·
2023
·
IF 5.9
Jiawei Lu,Ying-Nan Li,Youran Li,Huilin Zhu,Guiyang Shi
The reusability of immobilized lipases, including their hydrolysis activity, is greatly affected by lipase leakage, mass transfer channel blockage, and compound deposition on the outside surface. In this study, Candida antarctica lipase B (CALB) was immobilized on Fe3O4 nanoparticle-polyacrylonitrile (PAN) composite magnetic beads through phase inversion (L/FP). The hydrolysis activity of lipase was investigated using p-nitrophenyl palmitate (p-npp) as a model ester. To overcome the limitations of immobilized lipase in ester hydrolysis, three modification strategies were employed. First, lipase was covalently immobilized on Fe3O4 nanoparticles modified with methallyl (M9) and chloro (M13) silane modifiers, which exhibited faster immobilization with reduced lipase leaching and higher activity expression and stability. Second, poly(ethylene glycol) (PEG6000) and polylactic acid (PLA) were added to the precursors to physically modify the composite structures of L/FP, resulting in modified beads with larger specific surface area (15.26 m2·g–1) and smaller average pore size (19 nm). The modified beads, L/FP-9-M and L/FP-13-M, demonstrated superior reusability in long-term hydrolysis activity over 250 cycles. L/FP-9-M retained 63 and 34% of the initial activity at the 100th cycle and the 250th cycle, respectively. L/FP-13-M retained 55 and 36% of the initial activity at the 100th cycle and the 250th cycle, respectively. Furthermore, even after 250 repeated uses, the unit activities (U·gsupport–1) of both L/FP-9-M and L/FP-13-M remained higher than the initial activity of Novo 435.
✓ 已验证
产品关联
DOI
高影响因子
INDUSTRIAL CROPS AND PRODUCTS
·
2023
·
IF 5.9
Xiaoyan Ji,Rui Xu,Fei Wang,Xun Li
Biodiesel is recognized as green and renewable energy with low carbon intensity and less environmental impacts. The preparation of an economical immobilized lipase becomes much urgent challenge in the enzymatic production of biodiesel. In this study, recombinant Thermomyces lanuginosus lipase (TLL) was immobilized on the surface of silica-containing materials mediated by solid-binding peptides (SBPs). The obtained immobilized biocatalysts were effective in converting the oil from Jatropha curcas into biodiesel. The appropriate attachment mode of SBPs and TLL was investigated firstly, and the results showed that the activity of TLL was not negatively affected only when SBPs were fused at the C-terminus of TLL. Secondly, the immobilization efficiency of different SBPs (CecA, EctP1, VKT) on different silica-containing materials (SiO 2 , zeolite ZSM-5, SAR-100, MCM-41 and Na-Y) was systematically studied and it was concluded that the best immobilization efficiency was achieved for TLL-EctP1 immobilized on zeolite ZSM-5 (TLL- EctP1 @ZSM-5). TLL-EctP1 @ZSM-5 was found great performance in stability of pH, temperature, elution and storage. Eventually, biodiesel yield of 93 wt% was achieved using TLL-EctP1 @ZSM-5 as a biocatalyst to catalyze J. curcas oil for 48 h, and 81% of its initial yield was retained after 7 cycles of reuse. These results highlight the application of solid-binding peptides in enzyme immobilization for biocatalysts used in preparation of biodiesel or other chemicals.
✓ 已验证
产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2018
·
IF 3.909
Ming Ying,Manjunath D. Meti,Hong Xu,Yuhan Wang,Jialiang Lin,Zhibing Wu,Qingguo Han,Xu Xu,Zhendan He,Wenxu Hong,Zhangli Hu
The interaction of lipase with Ligupurpuroside B was studied by multiple spectroscopic techniques , enzyme activity and molecular modeling under simulative physiological condition. According to Stern-Volmer equation, fluorescence of lipase was quenched by Ligupurpuroside B via a static quenching mechanism because of formation of Ligupurpuroside B-lipase complex. Binding constants , number of binding sites & thermodynamic parameters were evaluated. The values of Δ G o (−25.085 kJ mol −1 ), Δ H o (−12.14 kJ mol −1 ) and Δ S o (+43.45 J mol −1 K −1 ) at 298 K indicated that Ligupurpuroside B-lipase interaction is spontaneous and hydrophobic interaction is the main force stabilizing the Ligupurpuroside B-lipase complex. The enzyme activity assay showed that Ligupurpuroside B inhibited lipase activity efficiently. Synchronous fluorescence spectra (SFS) suggested that Ligupurpuroside B is closer to Trp residues than to Tyr residues. All above experimental results were confirmed by molecular docking studies, which further indicated the binding site of Ligupurpuroside B on the surface of lipase, and the amino acid residues of lipase interacting with Ligupurpuroside B. Our present research work gives valuable information on the design of drugs with lipase as a carrier and should be useful for food industries.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH
·
2019
·
IF 3.375
Dewei Wan,Chaoren Yan,Qiuyu Zhang
Multifunctional magnetic polydopamine (PDA) nanospheres have become a research hotspot, especially in the field of biocatalysis, owing to their good biocompatibility and abundant functional groups. However, facile and rapid synthesis of hollow magnetic mesoporous PDA (HM-MPDA) with high saturation magnetization, large tailored pore size, excellent structural thermal stability, and controllable shell thickness is still a challenge. Herein, HM-MPDA nanospheres with ultrahigh magnetization (∼82.2 emu/g), ultra-large tunable pore sizes (11.53–49.53 nm), rigid pore structures (at 550 °C), and controllable shell thickness (23–178 nm) are synthesized based on a novel nanoemulsion co-assembly approach. Impressively, the hollow magnetic mesoporous PDA nanoflowers (HM-MPDA-NFs) are obtained by simply adjusting the amount of 1,3,5-trimethylbenzene and the P123/F127 weight ratios. Considering their unique properties, lipases were successfully immobilized on the pore walls of HM-MPDA-NFs, which were employed for the preparation of biodiesel. Under the optimum esterification conditions, the conversion of biodiesel can reach up to 87.9% and still exceed 71.3% after six times of recycling. More importantly, this study opens up a new way to fabricate hollow magnetic mesoporous nanocarriers, which can provide many applications in biocatalysis, dye adsorption, electrochemistry, and biosensing.
✓ 已验证
产品关联
DOI
高影响因子
Food Bioscience
·
2024
·
IF 4.8
Xiaoqiang Zou,Mudassar Hussain,Imad Khan,Yanxi Wang,Bangzhi Jiang,Lei Zheng,Yuechao Pan,Jijie Hu,Azqa Ashraf
Medium- and long-chain structured lipids (MLSLs) rich in docosahexaenoic acid (DHA) and eicosapentaenoic acid (EPA) were synthesized by acidolysis of fish oil (Omax 1812, a mixture of sardine and anchovy oils) with caprylic acid (CA) using a lipase bio-imprinted with fatty acids as a catalyst. A bio-imprinted lipase for the acidolysis reaction was first prepared under optimal conditions, and its activity was 1.43 times higher than that of the non-bioimprinted. The bio-imprinted lipase was used as a catalyst to produce such MLSLs, and the reaction conditions were optimized. Under the optimal conditions, equilibrium was achieved in 8 h, and the total and the sn -1, 3 CA contents in the obtained product were 28.72% and 42.26%. Additionally, the total and the sn -2 DHA contents were 14.23% and 21.10%, respectively, and the total and the sn -2 EPA contents were 16.43% and 10.14%, respectively. These obtained MLSLs, rich in sn -1, 3 CA, and sn -2 DHA, EPA can deliver significant health benefits.
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF FOOD BIOCHEMISTRY
·
2017
·Vol. 41
·期 5
·e12395
·
IF 1
Shuai Cui,Qin-Wei Zhou,Xiao-Ling Wang,Si-Qi Yang,Kai Chen,Zhi-Yuan Dai,Yao-Wen Huang,Tao Zhou
Bovine pancreatic lipase was immobilized onto N -succinyl-chitosan beads by using N -(3-dimethylaminopropyl)- N ′-ethylcarbodiimide (EDC)/ N -hydroxysuccinimide (NHS) as the activating agent. The immobilized lipase was characterized by Fourier transform infrared spectra and scanning electron microscopy. The activity of the immobilized lipase obtained under the optimized immobilization conditions was found to reach 1,480 U/g, with enzyme activity recovery of 74.5%. Compared to the free lipase, thermal stability of the immobilized lipase was greatly improved. The reusability study indicated that the immobilized lipase retained 76.6% of its initial activity after being recycled five times. A preliminary study indicated that the prepared immobilized lipase can effectively enrich the polyunsaturated fatty acid in fish oil (increasing from 45.1 to 67.7%), of which the combined docosahexaenoic acid and eicosapentaenoic acid contents increased from 16.3 to 27.1%. Practical applications To overcome the drawbacks of using free lipase, an effective method was developed by immobilization of lipase onto N -succinyl-chitosan beads using EDC/NHS as the activating agent. The immobilized lipase prepared by this method may find application in the enrichment of polyunsaturated fatty acids of fish oil.
✓ 已验证
产品关联
DOI
高影响因子
RSC Advances
·
2016
·Vol. 6
·期 9
·7339-7347
·
IF 3.289
Shilin Liu,Ya Zhu,Wei Li,Yan Li,Bin Li
Surface modification of the magnetic cellulose particles has been conducted by using AEAPS, the modified magnetic cellulose particles were then used for the immobilization of lipase for catalysis reaction. The highest specific activity for AEAPS modified magnetic cellulose scaffold was increased to about 30 fold that of the free lipase without support. Furthermore, the reusability of the immobilized lipase on AEAPS modified magnetic cellulose particles was also improved, the relative activity of the ARCM-2 and AMRCM1-2 after being reused for 5 times still remained 72.8% and 71.2%, respectively. Moreover, the immobilized lipase on AEAPS modified magnetic cellulose particles was easily recovered without significant decrease in the specific activity. The immobilization of lipase on AEAPS modified magnetic cellulose particles led to the improvement in stability of activity and reusability for non-aqueous transesterification.
✓ 已验证
产品关联
DOI
高影响因子
PROCESS BIOCHEMISTRY
·
2014
·
IF 2.524
Ru Jia,Yi Hu,He Huang
Porcine pancreatic lipase (PPL) was chemically modified with various functional ionic liquids (ILs) to increase its catalytic performance in water-miscible IL. Catalytic activity and thermostability were tested with a p -nitrophenyl palmitate (pNPP) hydrolysis reaction. The native enzyme lost 18% of its initial activity in 0.4 M [MMIm][MeSO 4 ], whereas the activities of all the modified enzymes increased. The [HOOCBMIm][Cl] modification led to a 2-fold increase in activity in 0.3 M [MMIm][MeSO 4 ] than in aqueous. All the modified enzymes exhibited higher thermostability compared with the native enzyme at high temperature. In particular, the [HOOCBMIm][Cl] modification led to a 6-fold increase in thermostability at 60 °C. Conformational changes were confirmed by fluorescence spectroscopy and circular dichroism spectroscopy to elucidate the mechanism of catalytic performance alteration.
✓ 已验证
产品关联
DOI
高影响因子
BIOPROCESS AND BIOSYSTEMS ENGINEERING
·
2014
·Vol. 37
·期 11
·2353-2359
·
IF 1.823
Ganasen Ponnarasy,Khan Maksudur Rahman,Kalam M. Abul,Mahmud Mohd Sabri
This paper demonstrates Pseudomonas cepacia lipase catalyzed hydrolysis of p -nitrophenyl palmitate under irradiation of light with wavelengths of 250–750 nm. The reaction follows Michaelis–Menten Kinetics and the light irradiation increases the overall rate of hydrolysis. Using Lineweaver–Burk plot K
M and V
max values for the reaction in presence of light are found to be 39.07 and 66.67 mM/min/g, respectively; while for the same reaction under dark condition, the values are 7.08 and 10.21 mM/min/g. The linear form of enzyme dependent rate of reaction confirms that no mass-transfer limitations are present and the reaction is a kinetically controlled enzymatic reaction.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
COLLOIDS AND SURFACES B-BIOINTERFACES
·
2024
·
IF 5.4
Ting Feng,Jiani Shi,Jiaojiao Xia,Xuemei Ren,Onyinye Idowu Adesanya,Hongbo Suo,Bin Zou
In this study, the critical importance of designing an appropriate immobilized carrier and method for free lipase to ensure exceptional biological catalytic activity and stability was emphasized. Covalent organic frameworks (COF-1) were synthesized as a novel porous carrier with an azine structure (-C N-N C-) through the condensation of hydrazine hydrate and benzene-1,3,5-tricarbaldehyde at room temperature. Simultaneously, Rhizomucor miehei lipase (RML) was immobilized within the COF-1 carrier using an in-situ aqueous phase method. Characterization of the carrier and RML@COF-1 and evaluation of the lipase properties of RML and RML@COF-1 through p -Nitrophenyl palmitate hydrolysis were conducted. Additionally, application in the synthesis of 1, 3-dioleoyl-2-palmitoylglycerol (OPO) was explored. The results showed that RML@COF-1 exhibited a high enzymatic loading of 285.4 mg/g. Under 60℃ conditions, the activity of RML@COF-1 was 2.31 times higher than that of free RML, and RML@COF-1 retained 77.25% of its original activity after 10 cycles of repeated use, indicating its excellent thermal stability and repeatability. Under the optimal conditions (10%, 1:8 PPP/OA, 45℃, 5 h), the yield of OPO reached 47.35%, showcasing the promising application prospects of the novel immobilized enzyme synthesized via in-situ aqueous phase synthesis for OPO preparation.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Jinhang Chen,Tieliang Liu,Yi Zhang,Lu Zheng,Kheng-Lim Goh,Vladimir Zivkovic,Mingming Zheng
Flavor esters are used in food and cosmetic industries, but sustainable production remains a big challenging. This study proposed the ultrasound-assisted biosynthesis of cinnamyl acetate using self-made immobilized lipase CSL@OMS-C 8 , with computational fluid dynamics (CFD) and molecular simulations revealing the hydrodynamic properties and lipase-catalytic mechanisms. The results demonstrate that ultrasonication-intensified enzymatic reaction facilitated 96.6 % conversion of cinnamic alcohol, due to the ultrasound-assisted catalytic efficiency of 13.7 mmol/g·min. Molecular docking analysis identifies the lowest binding energy of −3.7 kcal·mol −1 between lipase and vinyl acetate, contributing to the highest conversion rates compared to acetic acid, ethyl acetate. CFD simulation indicates that ultrasonic energy waves promote substrate diffusion and mixing with lower shear stress. The catalytic stability of CSL@OMS-C 8 was confirmed by 60.1 % of relative activity after 10-time reuse. This paper theoretically and experimentally studied the ultrasonic-assisted enzymatic synthesis of cinnamyl acetate, showcasing huge potential for sustainable production of flavor esters.
✓ 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）