Food Bioscience
·
2021
·
IF 4.24
Fuqiang Liang,Yumeng Shi,Weiwei Cao,Jiayi Shi
This study aimed to elucidate the inhibition mechanism of apigenin against porcine pancreatic lipase (PPL), and, moreover, to comprehensively reveal the molecular basis of its anti-obesity via network pharmacology approach. The results showed that apigenin inhibited PPL with an IC 50 value of 0.377 ± 0.041 mM. Spectroscopic techniques combined molecular docking suggested that apigenin could bind into the PPL active pocket, affecting its normal spatial conformation. Moreover, molecular dynamic (MD) simulations revealed that the open conformation of PPL tended to transit to the closed in the presence of apigenin, which might one important reason for the inhibition of PPL catalytic ability. Network pharmacology analysis revealed that a total of 49 proteins could be identified as potential targets for the anti-obesity effects of apigenin. According to the protein-protein interaction (PPI) network analysis, six hub targets were extracted including IGF1 , ESR1, MMP9 , PPARA , MAPK14 and NR3C1. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment indicated that the 49 potential targets could be mapped to 30 pathways (p<0.05). Among them, PI3K-Akt signaling pathway and insulin resistance can be considered as two major pathways regulated by apigenin. Further docking studies indicated that apigenin can bind into the binding pocket of the six hub target proteins identified according to the PPI network. The results indicated that in addition to inhibiting PPL, apigenin could exhibit anti-obesity benefit through the molecular mechanisms uncovered by network pharmacology. This study proposes a new strategy to reveal the mechanisms of dietary polyphenols at the level of network pharmacology.
✓ 已验证
产品关联
DOI
高影响因子
BIORESOURCE TECHNOLOGY
·
2023
·
IF 11.4
Jing-jing Guo,Yi-tong Wang,Zhen Fang
Magnetic biochar was synthesized via chelation of Fe 3+ with carboxymethyl cellulose and pyrolysis for covalently immobilizing Eversa® Transform lipase. The magnetic biochar had 75.8 mg/g lipase loading that was 54.1 % higher than that without magnetism. The immobilized lipase achieved 91.3 mg/g lipase loading with 19.2 U/mg lipase activity after optimization. It showed good thermal and acid stability with 82.5 % and 98.2 % relative activity at 45 °C and pH 4, respectively. Its relative activity was 90.8 % after stored for 30 d at 4 °C. After magnetically separated for 10 cycles, it still kept 70.1 % activity due to the strong covalent bonding. The lipase further catalyzed one-pot esterification and transesterification of high acid value oil (38 mg KOH/g) with 95.7 % biodiesel yield and cycled for 10 times at 85.7 % yield. Kinetic study gave the activation energy of 28.7 kJ/mol. The covalently immobilized lipase could find practical applications.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF MOLECULAR LIQUIDS
·
2021
·
IF 6.165
Sha Li,Xing Hu,Junhui Pan,Deming Gong,Guowen Zhang
The inhibition of pancreatic lipase by apigenin, a natural dietary flavonoid, was investigated by various spectroscopic techniques and computational simulation. The results showed that apigenin reversibly inhibited pancreatic lipase activity in a competitive manner with an IC 50 value of 0.45 ± 0.03 mM, and its combination with orlistat showed a synergistic effect. Formation of a complex between apigenin and pancreatic lipase driven by hydrogen bonds resulted in the fluorescence quenching of the enzyme through a static manner. The binding constant of apigenin with the enzyme was (5.47 ± 0.01) × 10 4 L mol −1 at 298 K, and the kinetic process of their interaction was characterized by the resolved concentration profiles and pure spectra of different components from the multivariate curve resolution-alternating least squares algorithm. The inhibition of pancreatic lipase by apigenin was mainly attributed to the tighter structure of the enzyme and the interaction between apigenin and the amino acid residues in the active center of the enzyme to prevent the substrate from being oxidized, as demonstrated by the analysis of circular dichroism spectra and molecular docking. Molecular dynamics simulation further characterized the binding conformation and property of apigenin-pancreatic lipase complex. This study provides novel insights into the mechanism of apigenin as pancreatic lipase inhibitor and the development of apigenin as an anti-obesity nutrient.
✓ 已验证
产品关联
DOI
高影响因子
NEW JOURNAL OF CHEMISTRY
·
2020
·Vol. 44
·期 34
·14379-14388
·
IF 3.288
Fenfen Zhu,Wei Xu,Xiao Li,Hao Meng,Yide Han,Junbiao Wu,Junli Xu,Yan Xu,Xia Zhang
Enzyme immobilization engineering is considered a valid strategy to improve the insensitivity of free enzymes to extreme conditions and thus extend their utilization in actual reactions. Although metal–organic frameworks (MOFs) are extensively applied as supports in enzyme immobilization, their separation from the liquid system after catalytic processes is problematic. In comparison, MOF-based membranes show more convenience in the subsequent solid–liquid separation. In this work, we constructed hybrid membranes by incorporating UiO-66 particles into porous polyvinylidene fluoride (PVDF) and then used them to immobilize lipase for the first time. Because of the strong affinity of UiO-66 towards lipase and the large cavity of PVDF, the hybrid membranes exhibited excellent immobilization ability towards lipase, and the resulting immobilized lipase showed an elevated operating temperature in the range of 40–70 °C with preserved activity and evidently improved thermal stability even after being stored at high temperatures for a definite time. The application of PVDF membrane makes the subsequent separation of the immobilized enzyme from the solutions easier. The immobilization kinetics, isotherm, and thermodynamics were analyzed in detail, and the immobilization mechanism was proposed. Furthermore, the immobilized lipase showed reusability and retained 48.2% of its initial activity after 7 cyclic reactions.
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF MOLECULAR LIQUIDS
·
2020
·
IF 5.065
Rongrong Wang,Wei Jin,Xirong Huang
In the present work, the sulfobetaine-type zwitterionic surfactant (SB- n ) was tried for the first time to construct hydrophobic ionic liquid (HIL)-based bicontinuous microemulsions . The composition-dependent phase behavior of the HIL/water (buffer)/SB- n ternary microemulsion system was determined by the method of T - γ fishlike phase diagram . It is found that the phase inversion temperature increases markedly with the increase of the alkyl chain length ( n ) of SB- n , but the surfactant efficiency changes little. The HIL greatly affects the phase behavior, depending on the ion structure. It is found that the SB-12 stabilized [C 8 mim][PF 6 ]-based microemulsion system has moderate phase inversion temperature, and moreover, its surfactant efficiency is the highest among the reported HIL-based bicontinuous microemulsions stabilized by conventional surfactants. The composition-dependent microstructure of the SB-12-stabilized [C 8 mim][PF 6 ]-based bicontinuous microemulsion was characterized by SAXS technique, and its influence on the catalytic performance of solubilized lipase was also explored. With the increase of the mass ratio of the HIL to water ( α ), the correlation length ( ξ ) changes slightly, but the microdomain size ( d ) decreases steadily. Unlike α , with the increase of the surfactant concentration ( γ ), the d changes little, but the ξ increases markedly. This abnormal change of ξ with γ should be ascribed to the interface rigidity of the microemulsion. The catalytic efficiency of lipase depends on the rigidity of the interface and its interfacial area. The above original studies not only enrich HIL-based microemulsion systems, but also provide scientific support for lipase-based green synthesis and transformation.
✓ 已验证
产品关联
DOI
高影响因子
ANALYST
·
2020
·Vol. 145
·期 23
·7595-7602
·
IF 3.978
Rui Duan,Yanzeng Li,Yichen He,Yonggui Yuan,Hanyang Li
In this study, we demonstrate a quantitative and sensitive strategy for monitoring the lipase concentration using a liquid crystal (LC) microfiber biosensor based on the whispering-gallery mode (WGM). An LC 4-cyano-4′-pentylbiphenyl (5CB) microfiber was doped with glycerol trioleate (GT) and used as both an optical microcavity and a sensing element. The self-assembled monolayer of a surfactant was formed at the LC/aqueous solution interface by the enzymatic reaction between lipase and GT, which resulted in the reorientation of the 5CB molecules from a planar to a homeotropic configuration. Interestingly, the structural change of the 5CB microfiber can be sensitively captured by the WGMs and quantitatively characterized by the wavelength shift. With this method, lipase with concentrations as low as 0.01 μg mL−1 in aqueous solution can be detected within 200 seconds, which is lower than the optimal value based on LC materials reported so far. In addition, our biodetection system is highly selective for lipase. We believe that the proposed biosensor has high potential for the detection of biochemical molecules.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
·
2020
·Vol. 192
·期 2
·392-414
·
IF 2.277
Chen Sunni,Li Jing,Fu Zejian,Wei Guohua,Li Hongyan,Zhang Bin,Zheng Liufeng,Deng Zeyuan
Phytosterols are regarded as compounds able to reduce total and low-density lipoprotein cholesterol in the blood, and their esterified derivatives could help to improve the effectiveness of this function. In the present study, the water/sodium 1,4-bis-2-ethylhexylsulfosuccinate (AOT)/isooctane reverse micelle (RM) system was set up as a reaction medium for Candida rugosa lipase AY30 (CRL AY30) to synthesize β-sitosterol laurate (β-SLE). The product was identified by TLC, FT-IR, and HPLC–APCI–QqQ–MS/MS and quantified by HPLC. Through stepwise optimization, it was found that CRL AY30 had the highest activity in the water/AOT/isooctane RM system where 50 mM PBS with a pH of 7.5 was adopted as water core to carry CRL AY30, and the proportion of [CRL AY30] (mg/mL), [water] (mM), and [AOT] (mM) was set in 3:375:25, respectively, in isooctane. After screened with single-factor experiments, the esterification reaction conditions in the CRL AY30–water/AOT/isooctane RM system were further optimized by the response surface method as follows: the mole ratio of β-sitosterol to lauric acid of 1:3.5 (25 mM β-sitosterol), the enzyme load of 18% (w/w total reactants), the reaction temperature of 47 °C, and the reaction time of 48 h. As a result, the maximum esterification rate was up to 88.12 ± 0.79%.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
COLLOIDS AND SURFACES B-BIOINTERFACES
·
2020
·
IF 4.389
Qing Li,Yingxuan Chen,Shaowei Bai,Xinxin Shao,Lin Jiang,Quanshun Li
Herein, thermophilic lipase QLM from Alcaligenes sp. has been successfully immobilized in bio-based metal-organic frameworks (MOFs) through biomimetic mineralization, using zinc acetate and adenine as metal ion and organic ligand, respectively. The morphology and structure of lipase@Bio-MOF was systematically characterized by scanning electron microcopy (SEM), transmission electron microcopy (TEM), powder X-ray diffraction (PXRD) and Fourier transform infrared spectra (FT-IR). The enzyme loading in immobilized enzyme was measured to be 15.9 % by thermogravimetric analysis (TGA). Further, it was demonstrated to possess favorable catalytic activity and stability under high temperature and alkaline conditions and in the presence of metal ions, using the hydrolysis of p -nitrophenyl caprylate as a model. Finally, the immobilized enzyme was successfully applied in the preparation of biodiesel through the trans-esterification of sunflower oil with methanol, obtaining a conversion of >60 % at a high oil/methanol ratio of 8:1. Meanwhile, it showed excellent recyclability during the biodiesel production, and no changes of morphology and crystal structure were observed after being used for 3 cycles. Overall, the immobilized lipase in bio-based MOFs provided an economically and environmentally viable biocatalyst for the synthesis of biodiesel.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
ENGINEERING IN LIFE SCIENCES
·
2019
·Vol. 19
·期 11
·805-814
·
IF 1.936
Yuanyuan Zhang,Quancai Yao,Zewen Li,Fengke Yang,Fanye Wang,Junhong Liu
To reach the excellent yield as well as environmental friendliness, an efficient one-pot process for the synthesis of 2-methyl-3- n- butylaminoyl-1,4-benzoquinone, a mitomycin-like compound by the domino reaction of 2-methyl-1,4-hydroquinone and butylamine using laccase/lipase as co-catalysts, has been developed. In this present study, the process proposed here was further improved by optimizing the relevant factors using the response surface methodology based on Box–Benkhen Design. The optimum condition that afforded the highest yield (98%) of 2-methyl-3- n- butylaminoyl-1,4-benzoquinone was obtained as follows: molar ratio of amines to hydroquinones 1.16:1, activity ratio of laccase to lipase 1.14:2, and reaction temperature 38.9°C. The results obtained indicate that this process may be useful as a green alternative method for higher yield production of mitomycin analogs.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
BIOTECHNOLOGY LETTERS
·
2019
·Vol. 42
·期 2
·269-276
·
IF 2.154
Cai Xinyong,Zhang Mengjie,Wei Wei,Zhang Yinjun,Wang Zhao,Zheng Jianyong
A novel enzyme immobilization method employing metal–organic framework (MOF) encapsulation and macroporous resin adsorption was developed in this study. Candida antarctica lipase B (CALB) was firstly encapsulated onto metal–organic frame structures (Zeolitic imidazole framework-8, ZIF-8) and further bonded to macroporous resin by physical adsorption. Under optimized immobilization conditions, the activity of the prepared immobilized lipase (CALB-ZIF-8@D101) determined via the methyl esterification of oleic acid was 38.4 U/mg. Compared with free lipase, the immobilized lipase exhibited improved thermal and operational stability and organic solvent tolerance. These results demonstrate that the immobilization method of ZIF-8 encapsulation and macroporous resin adsorption enhanced enzyme properties at a superior level.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
BIOCHEMICAL ENGINEERING JOURNAL
·
2019
·
IF 3.371
Ning Chen,Chunyu Zhang,Yang Liu,Xiaoyan Dong,Yan Sun
Our recent work proved that Candida rugosa lipase (CRL) covalently bonded on poly(glycidyl methacrylate) grafted silica nanoparticles (S-pGMA) showed hyperactivation while on a zwitterionic polymer grafted silica exhibited higher stability. Inspired by the research, we have herein proposed to modify S-pGMA with cysteine (Cys) to introduce zwitterionic moieties on the polymer backbones. This design was to simultaneously achieve high activation and stability of immobilized CRL on the new supports. S-pGMA modified with low and high (complete) Cys modifications (S-pGMA-Cys-L/H) were synthesized and CRL was coupled via reactions with epoxy groups (CRL-1 on S-pGMA and CRL-2 on S-pGMA-Cys-L) and carboxyl groups (CRL-3 on S-pGMA-Cys-L and CRL-4 on S-pGMA-Cys-H). The results revealed the hyperactivation of the four enzyme preparations. Kinetic study proved that the immobilization resulted in significantly higher enzymatic reaction efficiency and enzyme-substrate affinity than the free enzyme. More importantly, CRL-2, -3, -4, especially CRL-4 on S-pGMA-Cys-H, presented superior thermal stability and pH tolerance than those of CRL-1. Enzyme coupling reaction also significantly affected the enzyme activation and stability. Taken together, the results indicate that zwitterionization of pGMA by modification with Cys is promising to provide supports for immobilized lipase of high activity and stability, and complete modification of Cys was favorable. The research has thus provided new insights into the development of new materials and methods for enzyme immobilization.
✓ 已验证
DOI
高影响因子
INDUSTRIAL CROPS AND PRODUCTS
·
2018
·
IF 3.849
Pei Wang,Zhaodi Ke,Juanjuan Yi,Xin Liu,Limin Hao,Qiaozhen Kang,Jike Lu
To enhance the stability of lipases, the additive method is attractive because of its high efficiency and simplicity, of which β-cyclodextrin (β-CD), as an additive has attracted attention. In the present study, the effects of β-CD on enzymatic hydrolysis of hemp seed oil by lipases were investigated. The stability, spectroscopy, and reusability of C andida sp.99–125 were compared by the addition of β-CD, respectively. The results showed that Candida sp.99–125 could produce the highest yield of α-linolenic acid (ALA, 18.27%, w/w) in the presence of β-CD after 24h, and the thermal stability of lipase was also improved. The UV spectroscopy showed that the absorbance of lipase decreased with increasing concentrations of β-CD and the fluorescence result was similar. Moreover, the reusability of lipase with β-CD was better than free lipase. This study revealed that β-CD could increase hydrolysis activity and stability of the lipase, thereby improving the hydrolytic process of hemp seed oil by Candida sp.99–125.
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）