JOURNAL OF COLLOID AND INTERFACE SCIENCE
·
2021
·
IF 8.128
Zhengqiang Qin,Nuan Feng,Yao Li,Xu Fei,Jing Tian,Longquan Xu,Yi Wang
Lipase is the most widely used enzyme in industry. Due to its unique “lid” structure, lipase can only show high activity at the oil–water interface, which means that water is needed in the catalytic esterification process. However, the traditional lipase catalytic system cannot effectively control “micro-water“ in the esterification environment, resulting in the high content of free water, which hinders the esterification reaction and reduces the yield. In this paper, a promising strategy of esterification catalyzed by polyacrylamide hydrogel immobilized lipase is reported. The porous polyacrylamide hydrogel microspheres (PHM) prepared by inverse emulsion polymerization are used as carrier to adsorb lipase by hydrogen bonding interaction. These hydrogel microspheres provide a ”micro-water environment“ for lipase in the anhydrous reaction system, and further provide an oil–water interface for ”interface activation“ of lipase. The obtained lipase-porous polyacrylamide hydrogel microspheres (L-PHMs) exhibit higher temperature and pH stability compared with free lipase, and the optimum enzymatic activity reach 1350 U/g (pH 6, 40 °C). L-PHMs can still remain about 49% of their original activity after 20 reuses. Furthermore, L-PHMs have been successfully applied to catalyze the synthesis of conjugated linoleic acid ethyl ester . The results suggest that this immobilization method opens up a new way for the application of lipase in ester synthesis.
研究领域:
生物化学
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酶工程
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材料科学
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DOI
PubMed
高影响因子
ACS Applied Materials & Interfaces
·
2022
·
IF 10.383
Jihang Zhang,Zhaoxin Wang,Wei Zhuang,Hesamoddin Rabiee,Chenjie Zhu,Jiawei Deng,Lei Ge,Hanjie Ying
Graphene-based materials are widely used in the field of immobilized enzymes due to their easily tunable interfacial properties. We designed amphiphilic nanobiological interfaces between graphene oxide (GO) and lipase TL (Thermomyces lanuginosus) with tunable reduction degrees through molecular dynamics simulations and a facile chemical modulation, thus revealing the optimal interface for the interfacial activation of lipase TL and addressing the weakness of lipase TL, which exhibits weak catalytic activity due to an inconspicuous active site lid. It was demonstrated that the reduced graphene oxide (rGO) after 4 h of ascorbic acid reduction could boost the relative enzyme activity of lipase TL to reach 208%, which was 48% higher than the pristine GO and 120% higher than the rGO after 48 h of reduction. Moreover, TL–GO-4 h’s tolerance against heat, organic solvent, and long-term storage environment was higher than that of free TL. The drawbacks of strong hydrophobic nanomaterials on lipase production were explored in depth with the help of molecular dynamics simulations, which explained the mechanism of enzyme activity enhancement. We demonstrated that nanomaterials with certain hydrophilicity could facilitate the lipase to undergo interfacial activation and improve its stability and protein loading rate, displaying the potential of the extensive application.
研究领域:
材料科学
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生物技术
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酶工程
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纳米技术
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DOI
PubMed
高影响因子
Antioxidants
·
2022
·Vol. 11
·期 10
·1906
·
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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DOI
PubMed
高影响因子
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
·
2024
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IF 3.1
Wenxiang Hu,Jiayun Li,Xindan Zhang,Yangbin Lv,Hongwei Ye,Chenyue Li,Ehu Liu,Chu Chu
Enzyme immobilization by metal organic frameworks (MOFs) is an efficient way for screening active constituents in natural products. However, the enzyme’s biocatalysis activity is usually decreased due to unfavorable conformational changes during the immobilization process. In this study, sodium cholate was firstly used as the modifier for zeolitic imidazolate framework-8 (ZIF-8) immobilized lipase to increase both the stability and activity. More importantly, with the help of solubilization of sodium cholate, a total of 3 flavonoids and 6 alkaloids candidate compounds were fished out. Their structures were identified and the enzyme inhibitory activities were verified. In addition, the binding information between the candidate compound and the enzyme was displayed by molecular docking. This study provides valuable information for the improvement of immobilized enzyme activity and functional active ingredients in complicated medicinal plant extracts.
研究领域:
生物技术
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药学
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生物化学
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天然产物化学
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产品关联
DOI
PubMed
高影响因子
BIOCATALYSIS AND BIOTRANSFORMATION
·
2024
·
IF 1.4
Yuyang Zhou,Rongchen Mang,Huiyi Long,Yamiao Li,Hua Zhou,Dingqiang Lu
Dioctyl sebacate is a long carbon chain dibasic acid ester with methylene as the main body. It is widely used in plasticizers because of its good cold resistance and high viscosity. And it has excellent properties of non-toxicity and easy biodegradation, so it can be used as a potential new green bio-based plasticizer. At present, most of the preparation methods of dioctyl sebacate are chemical methods, which have many by-products and cause environmental pollution. In this article, cellulose microspheres were used as a carrier to immobilize Candida antarctica lipase B (CALB) to catalyse the esterification of sebacic acid and n-octanol to prepare dioctyl sebacate. Through single factor experiments, the lipase immobilized on cellulose microspheres was optimized to determine the best process conditions: add 500 µL CALB to the erlenmeyer flask, and then add 0.02 mol/L PBS buffer (pH 8.0). After being prepared into a 5 mL system, 0.1 g of cellulose microspheres were added as a carrier and reacted for 3 h at 35 °C and 180 r/min. Added 0.5 vt% polyethylene glycol diglycidyl ether (PEGDEG) to the system for crosslinking. The final immobilization rate of lipase immobilized on cellulose microspheres was 80.06%, and the enzyme activity was 288.07 U/g. Using the cellulose-immobilized lipase as a catalyst, in the toluene system, the molar ratio of n (sebacic acid)/n (n-octanol) substrate was 1:3.5, the amount of immobilized enzyme was 0.04 g, 4 Å molecular sieve 1.5 g, 40 °C, and 150 r/min for 30 h, the conversion rate of dioctyl sebacate was 76.45%.
研究领域:
生物催化
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化学工程
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绿色化学
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材料科学
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DOI
高影响因子
MOLECULES
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2022
·Vol. 27
·期 22
·7798
·
IF 4.927
Yuelin Xu,Fengxi Li,Jinglin Ma,Jiapeng Li,Hanqing Xie,Chunyu Wang,Peng Chen,Lei Wang
Organophosphorus compounds are the core structure of many active natural products. The synthesis of these compounds is generally achieved by metal catalysis requiring specifically functionalized substrates or harsh conditions. Herein, we disclose the phospha-Michael addition reaction of biphenyphosphine oxide with various substituted β-nitrostyrenes or benzylidene malononitriles. This biocatalytic strategy provides a direct route for the synthesis of C-P bonds with good functional group compatibility and simple and practical operation. Under the optimal conditions (styrene (0.5 mmol), biphenyphosphine oxide (0.5 mmol), Novozym 435 (300 U), and EtOH (1 mL)), lipase leads to the formation of organophosphorus compounds in yields up to 94% at room temperature. Furthermore, we confirm the role of the catalytic triad of lipase in this phospha-Michael addition reaction. This new biocatalytic system will have broad applications in organic synthesis.Keywords:lipase;biocatalysts;promiscuity;C-P bonds;Michael addition reactions
研究领域:
有机化学
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生物催化
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酶学
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DOI
PubMed
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
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2026
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IF 6.7
Yuchen Wang,Lu Wang,Anjun Li,Jiangjing Gao,Shuyang Hu,Yan Xu,Xiao-Wei Yu
The thermostability of lipases represents a key advantage for expanding their application potential in the food industry. In this study, a thermotolerant lipase, rTaLip, was identified from Baiju Daqu and successfully expressed in Komagataella phaffii. After determining its enzymatic properties, we developed two thermostable mutants through rational engineering (V219C/D222C/S73F/V141T and V219C/D222C/S73F/V141D). Compared to the wild-type, the mutants showed 2.2-fold and 4.1-fold longer half-lives at 65 °C, and their catalytic efficiency increased to 455% and 119%, respectively. Molecular dynamics simulations elucidated the structural basis underlying the increased thermal stability and catalytic activity. In application tests, the mutant V219C/D222C/S73F/V141T improved palm oil hydrolysis efficiency from 63.01% to 88.77%. This study demonstrates that combining the mining of thermostable lipases from Baijiu Daqu with rational design-based engineering constitutes a valuable strategy for improving the industrial applicability of lipases in harsh processing environments.
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DOI
高影响因子
Green Chemistry Letters and Reviews
·
2013
·
IF 1.392
Zhang-Gao Le,Li-Tao Guo,Guo-Fang Jiang,Xiao-Bin Yang,Hui-Qiang Liu
The Henry reaction of aromatic aldehydes and nitroalkanes could be performed by catalyst of Lipase A from Aspergillus niger in organic/water medium, and the corresponding Henry products were obtained in yields up to 94%.
研究领域:
有机化学
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生物催化
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酶催化
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DOI
高影响因子
FOOD CHEMISTRY
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2022
·
IF 9.231
Yan-Wei Liu,Ying Zhou,Guo-Qing Huang,Li-Ping Guo,Xiao-Dan Li,Jun-Xia Xiao
Coacervation of the lipase from Aspergillus oryzae (AOL) with chitosan was a feasible way to fabricate lipase-loaded particles and the optimum conditions were phase separation pH 5.5, chitosan to AOL mass ratio 1:5, and temperature 25 °C in the absence of NaCl, which conferred an AOL loading efficiency of up to 95.48% and activity recovery of 69.60%. The AOL-chitosan coacervates were highly porous and more susceptible to weight loss upon heating. Coacervation with chitosan increased the activity of AOL and shifted its optimum pH from 7.0 to 6.0, but exerted no effect on its optimum temperature (45 °C). Thermal deactivation kinetics analysis revealed that the coacervated AOL was more thermal stable, while the Michaelis-Menten kinetics analysis indicated that coacervation with chitosan increased the V max of AOL by 2.4 folds, but decreased its substrate affinity by 3.6 folds. Hence, the AOL-chitosan coacervates are potential in the construction of Pickering emulsion-based lipase catalysis systems.
研究领域:
生物化学
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酶工程
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DOI
高影响因子
ChemCatChem
·
2013
·Vol. 5
·期 7
·1935-1940
·
IF 5.181
Zong-Bo Xie,Na Wang,Long-Hua Zhou,Fang Wan,Ting He,Zhang-Gao Le,Xiao-Qi Yu
Graphical Lip synthing: A lipase-catalyzed, green, and efficient approach for the cross-aldol reaction promoted by water with high yield and good stereoselectivity is described. PPL, lipase from porcine pancreas, is first reported to catalyze direct asymmetric aldol reactions between aromatic aldehydes and cyclic ketones. More importantly, the catalytic activity of PPL was greatly promoted by a small quantity of water at 37 °C. A wide range of aromatic aldehydes reacted with cyclic ketones to provide the corresponding aldol products with high yields (up to 99 %) and moderate to good stereoselectivity (up to 90 % ee and 99:1 dr ).
研究领域:
生物化学
·
有机合成
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产品关联
DOI
高影响因子
Scientific Reports
·
2016
·Vol. 6
·期 1
·1-13
·
IF 5.228
Cui Jiandong,Zhao Yamin,Liu Ronglin,Zhong Cheng,Jia Shiru
Increasing numbers of materials have been extensively used as platforms for enzyme immobilization to improve catalytic performance. However, activity of the most of the enzymes was declined after immobilization. Here, we develop a surfactant-activated lipase-inorganic flowerlike hybrid nanomaterials with rational design based on interfacial activation and self-assembly. The resulting surfactant-activated lipase-inorganic hybird nanoflower (activated hNF-lipase) exhibited 460% and 200% higher activity than native lipase and conventional lipase-inorganic hybird nanoflower (hNF-lipase). Furthermore, the activated hNF-lipase displayed good reusability due to its monodispersity and mechanical properties, and had excellent long-time stability. The superior catalytic performances were attributed to both the conformational modulation of surfactants and hierarchical structure of nanoflowers, which not only anchored lipases in an active form, but also decreased the enzyme-support negative interaction and mass-transfer limitations. This new biocatalytic system is promising to find widespread use in applications related to biomedicine, biosensor, and biodiesel.
研究领域:
生物化学
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纳米生物学
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酶工程
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产品关联
DOI
PubMed
高影响因子
NEW JOURNAL OF CHEMISTRY
·
2018
·Vol. 42
·期 16
·13471-13478
·
IF 3.201
Weifan Ren,Xu Fei,Jing Tian,Yao Li,Muzi Jing,Huan Fang,Longquan Xu,Yi Wang
Enzyme–inorganic hybrid nanoflowers have drawn extensive research interest for enzyme immobilization owing to their enhanced enzymatic activity, high surface area, and excellent chemical stability. However, their low mechanical stability and challenging separation hinder their application. Herein, we report a facile and effective strategy to construct nanoflowers–PVA–chitosan composite (NPC) hydrogels that have excellent mechanical strength, high catalytic activity, and are easy to separate. Lipase–Cu3(PO4)2·3H2O nanoflowers were uniformly immobilized in hydrogel networks, and the substrate and the product can travel freely. The excellent mechanical properties of the hydrogels effectively protect the fragile nanoflowers from external stress, ensuring enzyme activity. Compared with free lipase (97.28 U g−1), NPC3 exhibited a higher enzymatic activity (146.12 U g−1) at 37 °C and pH 7.4. Furthermore, hydrogels as bulk materials can be processed into various physical forms, such as thin films and spheres. The product can easily flow out without the need for a separation process. It is expected that this immobilization method would have great potential in industrial catalysis.
研究领域:
生物化学
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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）