CHINESE JOURNAL OF CHEMICAL ENGINEERING
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2019
·
IF 1.911
Yifeng Li,Chunyu Zhang,Yan Sun
Enzyme immobilization has attracted great attention for improving the performance of enzymes in industrial applications. This work was designed to create a new support for Candida rugosa lipase (CRL) immobilization. A porous poly(vinyl acetate–divinyl benzene) microsphere coated by a zwitterionic polymer, poly(maleic anhydride- alt -1-octadecene) and N,N -dimethylethylenediamine derivative, was developed for CRL immobilization via hydrophobic binding. The catalytic activity, reaction kinetics, stabilities and reusability of the immobilized CRL were investigated. It demonstrated the success of the zwitterionic polymer coating and subsequent CRL immobilization on the porous microsphere. The immobilized lipase (p2-MS-CRL) reached 27.6 mg·g −1 dry carrier and displayed a specific activity 1.5 times higher than free CRL. The increase of V max and decrease of K m were also observed, indicating the improvement of catalytic activity and enzyme-substrate affinity of the immobilized lipase. Besides, p2-MS-CRL exhibited significantly enhanced thermal stability and pH tolerance. The improved performance was considered due to the interfacial activation regulated by the hydrophobic interaction and stabilization effect arisen by the zwitterionic polymer coating. This study has thus proved the advantages of the zwitterionic polymer-coated porous carrier for lipase immobilization and its potential for further development in various enzyme immobilizations.
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Catalysis Science & Technology
·
2018
·Vol. 8
·期 18
·4718-4725
·
IF 5.365
Jiang-Wei Shen,Jia-Mei Qi,Xiao-Jian Zhang,Zhi-Qiang Liu,Yu-Guo Zheng
Candida antarctica lipase B (CALB) is a versatile and robust lipase with high activity and enantioselectivity in the resolution of alcohols and amines. Poor specific activity toward carboxylic esters that are branched or substituted in close proximity to the carboxyl group limits the application of CALB. In this study, a semi-rational engineering approach was successfully applied to tailor CALB for efficient synthesis of the moxifloxacin chiral intermediate through enzymatic resolution of cis-(±)-dimethyl 1-acetylpiperidine-2,3-dicarboxylate. The combinatorial active-site saturation test was performed on CALB and two key residue sites, 189 and 190, were identified in the determination of hydrolytic activity. The specific activity and catalytic efficiency (kcat/Km) of the best variant mut-I189K were increased by 286- and 193-fold, respectively, without impacting its enantioselectivity. With 0.1 g L−1 of purified mut-I189K loading, 1 M substrate was asymmetrically hydrolyzed with 49.9% conversion within 5 h, resulting in a space–time yield of 583.8 g L−1 d−1. These results demonstrated that mut-I189K is a competitive biocatalyst for large-scale preparation of the moxifloxacin chiral intermediate.
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CATALYSIS COMMUNICATIONS
·
2013
·
IF 2.915
Hong-De Yan,Qun Zhang,Zhao Wang
A lipase from Aspergillus oryzae WZ007 exhibited high esterification activities toward a series of short-chain acids and alcohols. Moreover, it displayed a strong tolerance for high substrate concentration of up to 2.0 M and presented a highest initial rate of 276 mmol·L − 1 ·h − 1 at this concentration. After a reaction time of 48 h, the conversion rates of acids were higher than 80% for the synthesis of a majority of heptanoic acid esters, some octanoic acid esters and n -propyl hexanoate. These results implied that A. oryzae WZ007 lipase was a promising biocatalyst in the production of flavor esters.
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BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
·
2016
·Vol. 64
·期 2
·251-258
·
IF 1.429
Hong-De Yan,Zhao Wang,Jun-Qing Qian
A mycelium-bound lipase from Aspergillus oryzae (AOL) exhibited excellent enantioselectivity for kinetic resolution of ( RS )-1-phenylethanol (( RS )-1-PE) in organic solvent. The various reaction parameters affecting the conversion and enantioselectivity were studied, including type of acyl donor, solvent, molar ratio, temperature, enzyme amount, and substrate concentration. The optimum reaction conditions were found to be transesterification with vinyl acetate at 30 °C in methyl tert -butyl ether with a vinyl acetate: ( RS )-1-PE molar ratio of 1:1 and an enzyme concentration of 60 g/L. At the optimum reaction conditions, the conversion could reach above 46% with >99% enantiomeric excess of the product, ( R )-1-phenylethyl acetate, when the substrate concentration was below 1.4 M. The enzyme displayed an excellent enantioselectivity with an E -value of >200 and a strong tolerance for high substrate concentration of up to 1.8 M. Those results indicated that AOL was a promising biocatalyst in the kinetic resolution of ( RS )-1-PE.
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MOLECULES
·
2017
·Vol. 22
·期 10
·1598
·
IF 2.861
Jing Chen,Yuchao Chen,Yi Cheng,Youheng Gao
Mannose-diester lauric diacid-cholesterol (Man-DLD-Chol), as a liposomal target ligand, was synthesized by lipase catalyzed in a non-aqueous medium. Its chemical structure was confirmed by mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy. Glycyrrhetinic acid (GA) liposomes containing Man-DLD-Chol (Man-DLD-Chol-GA-Lp) were prepared by the film-dispersion method. We evaluated the characterizations of liposomes, drug-release in vitro, the hemolytic test, cellular uptake, pharmacokinetics, and the tissue distributions. The cellular uptake in vitro suggested that the uptake of Man-DLD-Chol-modified liposomes was significantly higher than that of unmodified liposomes in HepG2 cells. Pharmacokinetic parameters indicated that Man-DLD-Chol-GA-Lp was eliminated more rapidly than GA-Lp. In tissue distributions, the targeting efficiency (Te) of Man-DLD-Chol-GA-Lp on liver was 54.67%, relative targeting efficiency (RTe) was 3.39, relative uptake rate (Re) was 4.78, and peak concentration ratio (Ce) was 3.46. All these results supported the hypothesis that Man-DLD-Chol would be an efficient liposomal carrier, and demonstrated that Man-DLD-Chol-GA-Lp has potential as a drug delivery for liver-targeting therapy.Keywords:lipase-catalytic acylation;mannose-diester lauric diacid-cholesterol;glycyrrhetinic acid liposomes;mannose receptor;liver-targeting
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BIOPROCESS AND BIOSYSTEMS ENGINEERING
·
2024
·
IF 3.5
Liu Jiale,Zhao Shufan,Wei Wan,Yu Shupeng,Wang Zhao,Zheng Jianyong
Lipase is one of the most widely studied and applied biocatalysts. Due to the high enzyme leakage rate of the immobilization method of physical adsorption, we propose a new lipase immobilization method, based on the combination of macroporous resin adsorption and organic polymer coating. The immobilized Candida antarctica lipase B (CALB@resin-CAB) was prepared by combining the macroporous resin adsorption with cellulose acetate butyrate coating, and its structure was characterized by various analytic methods. Immobilized lipase was applied for biodiesel production using acidified palm oil as the starting material, the conversion rate achieved as high as 98.5% in two steps. Furthermore, the immobilized lipase displayed satisfactory stability and reusability in biodiesel production. When the aforementioned reaction was carried out in a continuous flow packed bed system, the yield of biodiesel was 94.8% and space–time yield was 2.88 g/(mL∙h). The immobilized lipase CALB@resin-CAB showed high catalytic activity and stability, which has good potential for industrial application in the field of oil processing.
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Journal of Environmental Chemical Engineering
·
2024
·
IF 7.4
Jiandong Cui,Zhanxin Du,Lixue Zhao,Huihui Li,Zhongjie Wang,Zibei Huo,Yingjie Du,Zhaoming Zhang
Yellow water is a kind of Chinese liquor-making wastewater, and contains rich organic components such as alcohols and organic acids , if not treated, it can cause environmental pollution. Herein, continuous aromatic ester production from Chinese liquor yellow water by a packed-bed column bioreactor with immobilized lipase was achieved. Inspired by interface activation of lipase, lipase from Aspergillus oryzae (AOL) was immobilized on LX-1000HA resin with silicone DC1–2577 modification (SH-LX-1000HA) and oleic acid modification (LX-1000HA-NH 2 -OA), respectively. Benefiting from the hydrophobic properties of the surface, the resultant AOL@SH LX-1000HA and AOL@LX-1000HA-NH 2 -OA were 2.3-times and 1.5-times higher activity than that of free AOL, reached 240 U/g and 156 U/g respectively. Meanwhile, the AOL@SH LX-1000HA and AOL@LX-1000HA-NH 2 -OA exhibited higher thermal stability , storage stability, and recyclability than free lipase. Furthermore, the aromatic ester production from yellow water by an packed-bed column bioreactor increased from 1.293 g/L to 3.976 g/L. This efficient continuous bioprocess presents great industrial potential for high value utilization from Chinese liquor yellow water.
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FOOD CHEMISTRY
·
2025
·
IF 9.8
Yujie Wang,Juan Cheng,David Julian McClements,Jing Chen,Da Ma
This study explores the inhibitory effects of two migrants—2-mercaptobenzothiazole (MBT) and stearic acid—from dairy rubber contact materials on pancreatic lipase (PL). Enzyme assays showed significant, dose-dependent inhibition, with stearic acid being more potent. MBT and stearic acid exhibited reversible inhibition, with MBT acting competitively and stearic acid non-competitively. Fluorescence spectroscopy and circular dichroism indicated conformational changes in PL upon binding, while molecular docking confirmed specific interactions at the active site (MBT) and near it (stearic acid). Binding affinities for MBT-PL and stearic acid-PL complexes were − 24.90 and − 20.23 kJ/mol, respectively. High concentrations of both compounds exhibited synergistic inhibition, potentially affecting lipid digestion in dairy products. This study highlights the influence of rubber-derived migrants on PL activity and suggests limiting their use in food contact materials to safeguard dairy nutritional quality.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2025
·
IF 8.5
Xin-Yue Jia,Wen-Yu Liu,Guo-Qing Huang,Jun-Xia Xiao
Chitosan-lipase polyelectrolyte complexes are promising stabilizers for Pickering emulsion catalysis. In this work, three commercial chitosan species with low (50–190 kDa), medium (190–310 kDa), and high (310–375 kDa) molecular weights (MW), designated as LCS, MCS, and HCS respectively, were selected to coacervate with the lipase from Aspergillus oryzae (AOL) and the impacts of their MWs on the attributes of AOL were compared. It was found that MCS contributed the strongest interaction with AOL and its protein recovery and AOL loading ratios reached 81.40 and 91.82 % respectively. The complexed AOLs exhibited the same optimum pH and temperature, but MCS conferred the greatest substrate affinity decrease by 2.7 folds and highest V max increase by 0.65 folds compared with free AOL. Coacervation with chitosan enhanced the thermostability of the lipase and the most profound effect occurred in MCS, which contributed an increase in E a by 87.6 %. Circular dichroism results indicated that MCS induced the greatest α-helix content decrease in AOL by 45.6 %. Surface hydrophobicity and contact angle measurements demonstrated that the chitosan-AOL complexes possessed improved wettability. Hence, the MW of chitosan is a crucial parameter for the application of its AOL complex in Pickering emulsion catalysis and a medium MW favors this purpose.
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ENZYME AND MICROBIAL TECHNOLOGY
·
2012
·
IF 2.367
Jing-Yun Wang,Cui-Li Ma,Yong-Ming Bao,Pin-San Xu
Lipase from Burkholderia cepacia was encapsulated inside zirconia particles by biomimetic mineralization of K 2 ZrF 6 induced with protamine, a natural cationic protein. Scanning electron microscopy (SEM), transmission electron microscopy (TEM), and Fourier transform infrared spectroscopy (FT-IR) were employed for the characterization of the novel immobilized lipase. SEM and TEM images showed that both the zirconia particles with and without lipase have good spherical structures with average particle sizes of 150 nm. Fluorescence microscopy demonstrated that the lipase was indeed encapsulated inside the zirconia particles. The maximum immobilization capacity of the zirconia particles was 0.15 units/mg under optimum immobilization conditions. Biochemical characterization showed that the encapsulated lipase could retain most of its initial activity. Compared with free lipase, the encapsulated lipase exhibited improved thermal, pH, and recycling stabilities. After 8 weeks of storage, no substantial loss in catalytic activity was observed for the encapsulated lipase. The conversion of the kinetic resolution of ( R,S )-1-phenylethanol with vinyl acetate as acetyl donor catalyzed by zirconia-immobilized lipase reached 49.9% with higher ee s of 99.9% under the following optimal conditions: octane as solvent, 0.1 M ( R,S )-1-phenylethanol, 70 mg immobilized lipase, 180 rpm, 50 °C for 48 h. After 6 cycles (288 h), the conversion and ee s were still 43% and 85%, respectively.
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PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY
·
2025
·
IF 1.9
Junxin Zhao,Yiman Wu,Yuhan Yao,Tonglei Zhou,Yiming Xu,Jingyi Gui,Didi Guo,Xinshuo Yang,Deguo Wang,Xianghui Yan,Ping Yu,Zheling Zeng,Fugang Xiao
This study investigates the effects of atmospheric room temperature plasma (ARTP) mutagenesis on the morphological and genetic modifications of the lipase-producing strain Bacillus licheniformis NCU CS-5. While traditional strain improvement methods often suffer from low mutation rates and uneven mutation distribution, ARTP mutagenesis offers a powerful and efficient alternative. The significance of this study lies in its potential to enhance lipase production, a key enzyme in various industrial applications, through the generation of high-performance mutant strains. The gap in existing literature pertains to the limited understanding of ARTP-induced mutations in B. licheniformis and their impact on enzyme production. The novelty of this study is to explore the morphological and genetic changes induced by ARTP and to identify key genetic determinants contributing to these changes. Key findings include significant morphological alterations, higher intracellular Ca2+ levels, and numerous single-nucleotide variants (SNVs) and insertions/deletions (InDels) in the mutant strain. These findings imply that ARTP mutagenesis can effectively enhance lipase production, paving the way for optimized industrial microbial strains.
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JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
·
2020
·
IF 4.673
Junxin Zhao,Maomao Ma,Zheling Zeng,Ping Yu,Deming Gong,Shuguang Deng
A novel lipase, SCNL, was isolated from Staphylococcus caprae NCU S6 strain in the study. The lipase was purified to homogeneity with a yield of 6.13% and specific activity of 502.76 U/mg, and its molecular weight was determined to be approximately 87 kDa. SCNL maintained above 80% of its initial activity at a wide range of temperatures (20–50 °C) and pH values (6–11), with an optimal temperature at 40 °C and optimal pH at 9.0 with p-nitrophenyl palmitate as a substrate. SCNL exhibited a higher residual activity than the other staphylococcal lipases in the presence of common enzyme inhibitors and commercial detergents. The lipase activity was enhanced by organic solvents (isooctane, glycerol, DMSO and methanol) and metal ions (Na+, Ba2+, Ca2+, and Mn2+). The Km and Vmax values of SCNL were 0.695 mM and 262.66 s−1 mM−1, respectively. The enzyme showed a preference for p-NP stearate, tributyrin and canola oil. These biochemical features of SCNL suggested that it may be an excellent novel lipase candidate for industrial and biotechnological applications.
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