INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2025
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IF 8.5
Xiang Zhou,Jiahao Xu,Jiayao Sun,Hao Chen,Dechun Huang,Wei Chen,Hongliang Qian
1,3-Dioleoyl-2-palmitoylglycerol (OPO) is crucial for infant nutrition; however, conventional immobilized lipase requires high-purity enzymes, which increases costs and limits industrial scalability. Herein, Rhizomucor miehei lipase (RML) was immobilized on surface-modified magnetic nanoparticles using cross-linked enzyme aggregates (CLEAs) technology to produce Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs. This approach combines the separation and immobilization of enzymes, allowing for the use of lower-purity lipase, which enhances its suitability for industrial-scale processes. The optimized Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs exhibited excellent thermal, pH, and storage stability. The performance of Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs was evaluated by catalyzing the synthesis of OPO through the enzymatic hydrolysis of glycerol tripalmitate (PPP) and oleic acid (OA). Under optimal conditions, the OPO content in products reached 63.33 ± 0.30%, highlighting the high efficiency of the enzymatic process. After eight reuse cycles, the Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs retained around 75% of their relative activity. Therefore, this strategy of lipase immobilization using CLEA technology, coupled with magnetic nanoparticles, offers a promising approach for OPO synthesis.
研究领域:
生物催化
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纳米技术
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酶固定化
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食品化学
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工业生物技术
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产品关联
DOI
PubMed
高影响因子
Molecular Catalysis
·
2024
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IF 3.9
Maogen Liu,Lin Ma,Zhengjuan Zhang,Xiaoxuan Zhang,Weiwei Zhang
Developing a suitable biocatalyst with high catalytic efficiency, operational stability and wide substrate adaptability is crucial to promote the industrialization of biodiesel production from waste oil. Herein, Aspergillus oryzae lipase (1,3-specific) and Candida antarctica lipase B (non-specific) were co-immobilized onto Co 2+ -chelated magnetic metal-organic frameworks (MNPs@Fe-MOF) via metal-chelated affinity. The effect of processing variables in co-immobilization was thoroughly investigated using response surface methodology. The resulting co-immobilized lipases exhibited a notably increased catalytic efficiency and wide oil scope, achieving 95.3–98.5 % biodiesel yields toward six different oils within 9 h. Whereas, biodiesel yields of 38.5–56.1 % were obtained using a simple physical mixture of immobilized lipases at identical conditions, suggesting the remarkably motivated synergistic effect of lipases in co-immobilization. Moreover, MNPs@Fe-MOF demonstrated effective lipase protection against organic solvents and high temperatures, while providing rapid magnetic separation and simple recovery operations. Furthermore, the methanolysis efficiency of co-immobilized lipases retained above 80 % after five batches. After elution of inactivated lipases, the magnetic carriers could be recovered for next round of co-immobilization. Consequently, the affinity co-immobilization of lipases onto MNPs@Fe-MOF presents a sustainable avenue for efficient and economical biodiesel production.
研究领域:
生物化学
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可再生能源
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催化工程
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产品关联
DOI
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
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2019
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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.
研究领域:
生物技术
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酶学
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食品科学
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DOI
高影响因子
Antioxidants
·
2022
·Vol. 11
·期 10
·1906
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IF 7.675
Shanxiu Ming,Shuyi Li,Zhe Chen,Xujun Chen,Feifei Wang,Shaonan Deng,Krystian Marszałek,Zhenzhou Zhu,Wenxiang Zhang,Francisco J. Barba
Lipophilization is a promising way to improve the bioavailability of flavonoids. However, the traditional enzymatic esterification methods are time-consuming, and present low yields and purity. Herein, a novel membrane-based lipophilization technology—bioinspired lipase immobilized membranes (BLIMs), including CAL-B@PES, CAL-B@PDA/PES and GA/CAL-B@PDA/PES— were fabricated to improve the antioxidant flavanone glycoside hesperidin lipophilization. Via reverse filtration, PDA coating and GA crosslinking,Candida antarcticalipase B (CAL-B) was stably immobilized on membrane to fabricate BLIMs. Among the three BLIMs, GA/CAL-B@PDA/PES had the greatest enzyme activity and enzyme loading, the strongest tolerance of changes in external environmental conditions (temperatures, pH, heating time, storage time and numbers of cycles) and the highest hesperidin esterification efficiency. Moreover, the optimal operating condition for GA/CAL-B@PDA/PES fabrication was the CAL-B concentration of 0.36 mg/mL, operation pressure of 2 bar, GA concentration of 5% and crosslinking time of 1 h. Afterwards, the hesperidin esterification process did not affect the micromorphology of BLIM, but clearly improved the BLIM permeability and esterified product efficiency. The present study reveals the fabrication mechanism of BLIMs and offers insights into the optimizing strategy that governs the membrane-based lipophilization technology process.Keywords:Candida antarcticalipase B;enzymatic esterification;membrane separation;hesperidin lipophilization;bioinspired lipase immobilized membrane
研究领域:
生物化学
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食品科学
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制药工程
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产品关联
DOI
PubMed
高影响因子
PHYTOCHEMICAL ANALYSIS
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2023
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IF 3.3
Sihua Quan,Mengyi Wen,Ping Xu,Chu Chu,Hui Zhang,Kai Yang,Shengqiang Tong
Introduction Pancreatic lipase is one of the most important key targets in the treatment of obesity. Inhibition of pancreatic lipase can effectively reduce lipid absorption and treat obesity and other related metabolic disorders. Objectives The goal of this study is the efficient screening of pancreatic lipase inhibitors in the root and rhizome of Rheum palmatum using affinity ultrafiltration–high-performance liquid chromatography (AUF-HPLC) combined with high-resolution inhibition profiling (HRIP). Methods Potential pancreatic lipase ligands and pancreatic lipase inhibitors in ethyl acetate fraction of R. palmatum were screened using AUF-HPLC and HRIP, respectively. All screened compounds were identified by HPLC– quadrupole time-of-flight (Q-TOF)/MS. Eight compounds were screened out by both AUF-HPLC and HRIP, and six compounds were screened out by either AUF-HPLC or HRIP alone. The pancreatic lipase inhibitory activities of all screened compounds were verified by enzyme inhibition assay and molecular docking. Results Five new potent pancreatic lipase inhibitors were discovered, namely procyanidin B5 3,3′-di-O-gallate (IC 50 = 0.06 ± 0.01 μM), 1,6-di-O-galloyl-2-O-cinnamoyl-β-D-glucoside (IC 50 = 12.83 ± 0.67 μM), 1-O-(1,3,5-trihydroxy)phenyl-2-O-galloyl-6-O-cinnamoyl-β-D-glucoside (IC 50 = 17.84 ± 1.33 μM), 1,2-di-O-galloyl-6-O-cinnamoyl-β-D-glucoside (IC 50 = 18.39 ± 1.52 μM), and 4-(4′-hydroxyphenyl)-2-butanone-4’-O-β-D-(2”-O-galloyl-6”-O-cinnamoyl)-glucoside (IC 50 = 2.91 ± 0.40 μM). It was found that procyanidin B5 3,3′-di-O-gallate showed higher pancreatic lipase inhibitory activity than the positive control orlistat (IC 50 = 0.12 ± 0.02 μM). Conclusion The combination of affinity ultrafiltration–high-performance liquid chromatography (AUF-HPLC) and high-resolution inhibition profiling (HRIP) could reduce the risk of false-negative screening and missed screening and could achieve more efficient screening of bioactive compounds in complex natural products.
研究领域:
药理学
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分析化学
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天然产物研究
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
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2023
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IF 2
Miao Qiao,Xin Hua,Yongjun Yuan,Xi Cao
This work attempts to achieve the enrichment of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in acylglycerols as well as biodiesel production by investigating the performance of various lipases in ethanolysis. The ethanolysis activities of five immobilized lipases in decreasing order were as follows: Lipozyme TL IM, Novozym 40086/Lipozyme RM IM, Novozym 435 and Rhizopus oryzae lipase immobilized on polypropylene (RO PP). EPA could be enriched to a certain content by Lipozyme TL IM, Novozym 40086, Lipozyme RM IM, and RO PP. The enrichment of DHA was achieved well by those four sn -1,3 regioselective lipases, and DHA contents in acylglycerols were the highest when Lipozyme TL IM and Novozym 40086 were used, reaching 2.87-fold and 2.81-fold of the initial content. However, Novozym 435 could not enrich EPA and DHA effectively. Fatty acid ethyl esters produced in this work contained abundant palmitic acid and palmitoleic acid, which could be ideal biodiesel considering their chain length. The competitive factors of five lipases towards DHA were all significantly higher than those towards EPA. When Lipozyme TL IM and Novozym 40086 achieved the maximum DHA contents, their DHA recoveries in acylglycerols reached 91.87% and 89.00%, respectively. The DHA recoveries were all significantly higher than the corresponding EPA recoveries in the reactions catalyzed by five lipases. Moreover, Lipozyme TL IM could be a potential lipase for the separation of EPA and DHA. This study may promote the full use of fish oil and broaden the application of lipases.
研究领域:
生物化学
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食品科学
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酶工程
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产品关联
DOI
高影响因子
TALANTA
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2021
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IF 6.057
Jia Liu,Hai-Xia Zhang,Yan-Ping Shi
With a dramatic increase in the incidence of obesity, it is significant to screen lipase inhibitors from traditional herbal medicines as drugs to treat obesity. Lipase inhibitors currently used to treat obesity possess the defects of toxicity and off-target effects. Thus, there is an urgent need to explore more safe, effective and targeted anti-obesity drugs from traditional herbal medicines. In this work, amino functionalized magnetic cellulose microsphere was employed as a novel support to immobilize lipase through covalent bonding. Characterizations from fourier transform infrared spectroscopy, transmission electron microscopy and X-ray diffraction demonstrated the successful preparation of the support. In comparison with the free lipase, the immobilized lipase manifested the excellent properties of a wider range for pH and temperature endurance, better pH, thermal, storage stability and reusability. Through investigating the kinetics performances of the immobilized lipase, the Michaelis-Menten constant was calculated to be 2.05 mM and its inhibition constant for orlistat was ascertained to be 40.74 μM. Eventually, the established strategy was applied to screen lipase inhibitors from 7 traditional herbal medicines and Crataegus pinnatifida Bunge was screened out due to its significant lipase inhibitory activity. To sum up, our newly established method not only developed a platform for efficiently discovering novel anti-obesity drugs from traditional herbal medicines, but also laid a solid foundation for successfully exploring undiscovered medicinal value of the traditional herbal medicines.
研究领域:
药学
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生物技术
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药物发现
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传统医学
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产品关联
DOI
PubMed
高影响因子
INDUSTRIAL CROPS AND PRODUCTS
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2022
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IF 6.449
Shuai Wang,Yunxiao Wang,Shunxin Wang,Shuang Guo,Dongyu Gu,Jifeng Wang,Yi Yang
In this study, R. pseudoacacia flowers exhibited potential lipase ( Aspergillus niger ) inhibitory activity. To quickly explore the active compound, ligand fishing was adopted for screening the ligand from R. pseudoacacia flowers by lipase immobilized on magnetic polyamidoamine dendrimer-coated multi-walled carbon nanotubes . After ligand fishing, the target compound was separated purposefully by optimizing the separation conditions of high-speed counter-current chromatography (HSCCC). As results, kaempferol with the IC 50 of 327.64 ± 15.33 μg/mL was separated and identified. The further molecular docking results indicated that kaempferol was interacted with amino acid residue in the active site of lipase through van der Waals force, hydrogen bonds and Pi-Pi T-shaped interactions, yielding the binding energy of − 6.43 kcal/mol. The present method not only revealed the lipase inhibitory substances in R. pseudoacacia , but also provided an effective means for the screening of other natural substances.
研究领域:
生物化学
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纳米技术
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药理学
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植物科学
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产品关联
DOI
高影响因子
CLAY MINERALS
·
2019
·Vol. 54
·期 3
·293-298
·
IF 1.787
Dong Li,Min Shen,Guofan Sun,Huiran Jin,Peng Cai,Zhihui Wang,Yeling Jin,Jing Chen,Shijie Ding
A Pickering emulsion was prepared via synergistic stabilization of a lipase and palygorskite particles. The optimum conditions for the stabilization of the Pickering emulsion, such as the concentrations of the palygorskite particles and lipase, were explored. The morphology of emulsion droplets was examined using digital optical microscopy and polarizing optical microscopy. The palygorskite–lipase co-stabilized Pickering emulsions were investigated by determination of the adsorption rate, pH and zeta potential of the aqueous dispersion, as well as by determining the contact angle values of the lipase solution on a palygorskite disc that was immersed in toluene. The catalytic performance of the immobilized lipase in the Pickering emulsion was studied via the investigation of its thermal stability, storage stability and reusability. The immobilized lipase showed greater stability than the free lipase. The lipase immobilized by Pickering emulsion retained a high level of activity even after seven periods of recycling.
研究领域:
生物化学
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材料科学
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产品关联
DOI
高影响因子
JSFA Reports
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2024
·
IF 0
Rui-Yan Peng,Meng-Yao Hu,Hai-Xia Xu,Wen-Jun Wang,Zhong-Ping Yin,Ji-Guang Chen,Qing-Feng Zhang
Background Obesity is increasing seriously worldwide. Inhibiting pancreatic lipase (PL) is an important way to prevent obesity. Baicalein, a dietary flavone, shows various physiological activities and has anti-obesity potential. Therefore, the inhibitory activity of baicalein on PL was investigated in present study. Results Baicalein exhibited a significant inhibitory effect on PL with IC 50 value of 68 μg/mL. Inhibition kinetics indicated that baicalein was a mixed-type inhibitor of PL. Fluorescence titration showed that baicalein could induce fluorescence quenching of PL. The binding constant (logK a ) and number of binding sites were calculated as 5.40 and 1.11, respectively. In addition, synchronous fluorescence analysis revealed that the quenching ratio of baicalein to tryptophan was greater than that of tyrosine. Circular dichroism (CD) spectrum showed that the binding of baicalein affected the secondary structure of the enzyme protein. Through molecular docking analysis, it confirmed that baicalein could interact with amino acid residues in lipase, thus reducing the enzyme catalytic activity. In vivo studies showed that oral administration of baicalein with a does of 50 mg/kg bwt significantly reduced fat absorption and increased its fecal excretion in rats. Conclusion Baicalein showed inhibitory activity on PL in both in vitro and in vivo studies. It may be a safe and effective dietary supplement for obesity prevention.
研究领域:
生物化学
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药理学
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营养学
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DOI
MATERIALS LETTERS
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2021
·
IF 3.423
Chunyun Ma,Yan Zhang,Chuankai Yang,Miaorong Zhang,Jianguo Tang
Lipase was immobilized with Cu 3 (PO 4 ) 2 ⋅3H 2 O to synthesize lipase-Cu 3 (PO 4 ) 2 ⋅3H 2 O hybrid microflowers (Lip-MFs). Surfactants (Tween 80, Triton X-100 and CTAB) were added to study their effect on the morphology and activity of Lip-MFs. SEM images revealed that surfactants can increase the size of Lip-MFs and make the hierarchical structure more compact. Further, compared with other surfactants, the activity of CTAB-Lip-MFs was 1.45 times of that of free lipase, demonstrating CTAB is conducive to improve the activity of lipase.
研究领域:
生物化学
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材料科学
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产品关联
DOI
高影响因子
ChemistrySelect
·
2023
·Vol. 8
·期 29
·e202300512
·
IF 2.1
Kangjing Wang,Xinyi Dong,Ting Li,Qian Wang,Zhongyang Ding,Weifu Dong
Graphical The contact angle of modified starch was changed from 12.2° to 71.5°, and the particle size was changed from ∼10 μm to ∼300 nm. In the subsequent enzyme catalyzed reaction, the immobilized enzyme is adsorbed at the water oil interface, thereby improving the lipase activity. As a natural macromolecular material, starch is an ideal carrier for enzyme immobilization because of its widely available source, easy regeneration and excellent biodegradability. However, the natural starch cannot be directly used for immobilization due to the large particle size and excessive hydrophilicity. In this paper, the epoxy groups were grafted onto esterified starch by bifunctional reagents. The grafting efficiency of epoxy groups was increased by starvation drop addition. The changes of contact angle and particle size are conducive to the adsorption of immobilized enzyme at the water oil interface in the subsequent enzyme catalytic reaction, hence improve of the lipase activity. The maximum amount of lipase mobilized on such modified starch was ∼143.7 mg/g, which was near 40 mg/g higher than that of those from direct crosslinking. The immobilized enzymes showed excellent resistance to organic solvents and good reusability. Immobilization of lipases on epoxy-functionalized starch nanoparticles can potentially improves the possibility of enzymes industrial application.
研究领域:
生物技术
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材料科学
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酶工程
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产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）