Journal of Future Foods
·
2025
·Vol. 6
·期 1
·66-72
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IF 7.2
Hao Zhang,Bin Wu,Yanping Xian,Ming Liang,Yunjian Ma,Yonghua Wang
Musk macrolides are a kind of rare flavors structurally featuring 14−16 membered rings in the flavour and fragrance industry. While various chemical synthesis routes for musk macrolides exist, there is a growing interest in biocatalytic approaches. In this study, a new biocatalytic approach is proposed for the synthesis of musk macrolides from fatty acids using unspecific peroxygenases (UPOs) in combination with lipase. Specifically, the UPO from Marasmius rotula ( Mro UPO) was utilized as an oxidation catalyst together with the choline oxidase from Arthrobacter nicotinate ( An ChOx) for the in situ generation of H 2 O 2 . The enzymatic cascade process involved the hydroxylation of fatty acids using Mro UPO as a catalyst to prepare terminal hydroxylated fatty acids. Under the optimized conditions, 14-hydroxy tetradecanoic acid, 15-hydroxy pentadecanoic acid and 16-hydroxy hexadecanoic acid were obtained at concentrations of 11.1, 18.2 and 17.1 mg/L in a 50-mL reaction system, respectively. These hydroxylated fatty acids were then separated and esterified by lipase Novozymes 435 to produce the desired macrolides. Various ω -hydroxy fatty acids were successfully converted into macrolides, with the concentrations of cyclotetradecanolide, cyclopentadecanolide and cyclohexadecanolide reaching 11, 29 and 23 mg/L, respectively, in a 10-mL reaction system. This new biocatalytic approach represents a promising method for synthesizing valuable natural flavour compounds.
研究领域:
生物催化
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酶工程
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天然产物化学
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风味化学
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分子生物学
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绿色合成
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DOI
高影响因子
BIOCHEMICAL ENGINEERING JOURNAL
·
2020
·
IF 3.475
Yu Zhang,Xiaohui Di,Wen Wang,Miaojia Song,Qiang Yu,Zhongming Wang,Zhenhong Yuan,Xiaoyan Chen,Huijuan Xu,Ying Guo
Methyl-2-furoate (MF) is a high-value compound, and can be produced via esterification of furoic acid derived from biobased furfural. Herein, CAL-B and [bmim][PF 6 ] were the most efficient lipase and organic medium for MF production, respectively. Based on mass action law and reaction reversibility, a mathematical model was developed. Data analysis showed the newly proposed binary regression was apparently more suitable compared to the commonly used unitary regression. The enzymatic promotion factor m i for esterification and hydrolysis was 1.8159 and 0, while the alcohol inhibition factor n i was 0 and 0.06436, respectively. Both the activation energy E a, i for esterification and hydrolysis was 84 kJ/mol, and the pre-exponential factor A i was 7.1408×10 13 and 7.8962×10 13 , respectively. Kinetics study demonstrated that CAL-B held significantly more dominant esterification activity compared to hydrolysis activity, whereas alcohol just inhibited hydrolysis activity instead of esterification activity, and the relationship between esterification/hydrolysis rate constants k i and temperature agreed with Arrhenius equation. The maximum MF yield was 82.5 % at 24 h, and the yield decreased to 75.4 % after 1 re-use of CAL-B, but maintained about 20 % for next 4 cycles. Totally, the developed model and binary regression analysis method is ideal for in-depth examination of lipase-catalyzed kinetics in heterogeneous system.
研究领域:
生物化学
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酶工程
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高影响因子
Catalysts
·
2017
·Vol. 7
·期 2
·49
·
IF 3.082
Chenhui Wang,Haobo Han,Wei Jiang,Xiaobo Ding,Quanshun Li,Yanbo Wang
Here, core-shell structured polydopamine-coated Fe3O4nanoparticles were constructed to immobilize thermostable lipase QLM fromAlcaligenessp. Systematical characterization indicated that lipase QLM was successfully immobilized on the surface of nanoparticles with an enzyme loading of 21.4 ± 1.47 mg/g immobilized enzyme. Then, the immobilized enzyme was demonstrated to possess favorable catalytic activity and stability in the ester hydrolysis, usingp-nitrophenyl caprylate as the substrate. Further, it was successfully employed in the kinetic resolution of (R,S)-2-octanol, and satisfactory enantioselectivity and recyclability could be obtained with an enantiomeric ratio (E) of 8–15 over 10 cycle reactions. Thus, core-shell structured polydopamine-coated Fe3O4nanoparticles can be potentially used as a carrier for enzyme immobilization to improve their activity, stability, and reusability, which is beneficial for constructing efficient catalysts for industrial biocatalysis.Keywords:lipase;immobilization;polydopamine;Fe3O4nanoparticle;core-shell structure;ester hydrolysis;kinetic resolution
研究领域:
生物化学
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生物催化
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材料科学
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高影响因子
CHEMICAL RESEARCH IN CHINESE UNIVERSITIES
·
2014
·Vol. 30
·期 3
·396-399
·
IF 1.119
Jiang Ling,Yu Hongwei
“Amano” lipase AS(lipase from Aspergillus niger ), which naturally hydrolyzes triglycerides, was found promiscuously to catalyze multi-component reactions of aromatic aldehydes with malononitrile and β -naphthol to prepare naphthopyran derivatives in anhydrous organic solvents in moderate to good yields.
研究领域:
生物化学
·
有机合成
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DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2022
·
IF 8.025
Bozhi Tan,Yao Li,Xu Fei,Jing Tian,Longquan Xu,Yi Wang
Octenyl succinic anhydride (OSA) starch is an important edible additive in the food field, and its synthesis method has attracted much attention. Lipase as a biocatalyst can improve the synthesis efficiency of OSA starch, and significantly inhibit the occurrence of side reactions. However, free lipase has not been widely applied in the synthesis of OSA starch due to the difficulty of separation from starch and poor reusability. In this work, a promising strategy for the synthesis of OSA starch catalyzed by lipase immobilized on polydopamine magnetic hydrogel microspheres (PMHM) is reported. The prepared lipase-polydopamine magnetic hydrogel microspheres (L-PMHM) can be uniformly dispersed in starch slurry, which is conducive to the full contact between lipase and starch. L-PMHM (Km =2.6276 μmol/mL) exhibits better affinity to the substrate than free lipase (Km = 3.4301 μmol/mL). Compared with the OSA starch catalyzed by free lipase (DS = 0.0176), the degree of substitution of OSA starch catalyzed by L-PMHM is up to 0.0277 in a short reaction time. In cyclic catalysis, L-PHMM can remain about 48 % of their original activity after 20 reuses and can be quickly separated from the product. These results suggest that L-PMHM has great potential as a biocatalyst for the efficient synthesis of OSA starch.
研究领域:
食品科学
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生物技术
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化学工程
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DOI
PubMed
高影响因子
PeerJ
·
2019
·
IF 2.353
Xiao-Lin Qiu,Qing-Feng Zhang
Background Sinobambusa tootsik (Sieb.) Makino ( S. tootsik ) is one species of bamboo distributed in China, Japan and Vietnam. The chemical profile of its leaves and its potential application was unknown yet. Methods The chemical profile of S. tootsik was studied by HPLC and UPLC-DAD-QTOF-MS. The S. tootsik extract was prepared by extraction with 50% aqueous ethanol, followed by H103 macroporous resins adsorption and desorption processes. Pancreatic lipase inhibitory activity was determined using p -nitrophenyl palmitate as the substance, which was hydrolyzed by lipase to form coloured p- nitrophenol. Results Eighteen compounds were identified in S. tootsik . Most of them were the C -glycosylated derivatives of luteolin and apigenin, such as isoorientin, isoorientin-2″- O -rhamnoside and isovitexin. Isoorientin-2″- O -rhamnoside was the most dominant flavonoid in the sample. S. tootsik extract was prepared through resin adsorption/desorption with yield of 1.12 ± 015% and total flavonoids content of 82 ± 2 mg/g (in term of isoorientin). The extract exhibited pancreatic lipase inhibitory activity with IC50 value of 0.93 mg/mL. Conclusion The chemical profile of S. tootsik leaves was uncovered for the first time. C -glycosyl flavonoids were the main constituents in the plant. The extract exhibited pancreatic lipase inhibitory activity and may have potential for use as a food supplement for controlling obesity.
研究领域:
药用植物学
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植物化学
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营养保健品
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DOI
PubMed
高影响因子
APPLIED SURFACE SCIENCE
·
2026
·
IF 6.6
Jihang Zhang,Yihui Luo,Siwen Ji,Jinming Zhang,Xiang Chen,Lei Ge,Jinglan Wu,Zhuotao Tan,Sheng Xu,Bin Wu,Hanjie Ying,Wei Zhuang
Sequential coupling of hydrophobic orientation and rapid covalent locking. • Immobilized TLL exhibits >4000% relative activity via conformational tuning. • Interfacial microenvironment regulates partitioning and methanol tolerance. • Biocatalyst demonstrates exceptional durability and efficient conversion. Efficient multiphase bioprocessing for sustainable lipid valorization and biodiesel synthesis relies on robust solid–liquid biointerfaces. Their rational design is fundamentally constrained by severe reaction–diffusion constraints and the intrinsic activity–stability trade-off. Herein, we report a synergistic “orient-and-lock” strategy on bifunctional mesoporous SBA-15 to decouple these limitations. Hydrophobic domains first drive the oriented adsorption and “lid-opening” hyperactivation of Thermomyces lanuginosus lipase, followed by rapid isocyanide-mediated covalent anchoring to kinetically trap this metastable state without compromising structural flexibility. Molecular dynamics simulations elucidate a critical microenvironmental compartmentalization effect. This spatial partitioning selectively enriches lipophilic substrates while isolating polar inhibitors through localized hydrogen-bond networks and hydrophobic compartments, thereby effectively reducing substrate transfer resistance and minimizing active site blockage. Consequently, the immobilized biocatalyst exhibits an unprecedented 40-fold enhancement in apparent specific activity and a 57-fold increase in catalytic efficiency ( k cat / K m ) compared to the free enzyme. Its excellent tolerance to methanol enables a highly efficient one-step methanol addition reaction. The system demonstrates exceptional operational robustness, retaining 80% activity over 25 consecutive cycles and achieving a 96.8% biodiesel yield, establishing a synergistic paradigm of conformational engineering and transport regulation for high-performance heterogeneous biocatalysts. Download: Download high-res image (141KB) Download: Download full-size image
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产品关联
DOI
高影响因子
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES
·
2026
·
IF 2.5
Chuang Liu,Jianbin Ma,Qin Zhao,Yurong Du,Jun Dang
HPLC-FLD enabled recognition and tracking of PL-affinity peaks during separation. • PL-affinity peaks remained traceable across reversed-phase and HILIC separations. • Three compounds from S. tangutica , including 1 activator and 2 inhibitors. Background Translating biological recognition into chromatographic information that can continuously guide targeted isolation remains challenging in natural products. Methods HPLC coupled with fluorescence detection (HPLC–FLD) was combined with multimodal preparative chromatography to recognize, track, and isolate candidate pancreatic lipase (PL)-affinity ligands from Saxifraga tangutica . Their effects on PL were evaluated by activity and kinetic assays, with DFT calculations and molecular docking as complementary analyses. Results Three flavonoid glycosides with chromatographic purities above 95% were isolated: Q3XG (160.8 mg), Q3AG (167.9 mg), and Q3GG (623.1 mg). Q3XG activated PL with an EC₅₀ of 4.78 ± 0.95 μg/mL, whereas Q3AG and Q3GG inhibited PL with IC₅₀ values of 38.33 ± 1.97 and 43.86 ± 2.87 μg/mL, respectively. Kinetic analysis showed that Q3XG decreased the apparent K m and slightly increased the apparent V max, whereas Q3AG and Q3GG showed the opposite changes, consistent with mixed-type inhibition. DFT and docking analyses indicated differences in electronic properties and predicted PL-ligand interaction patterns. Conclusion Integration of HPLC–FLD with multimodal chromatography preserved the link between affinity signals and target peaks throughout chromatographic tracking, selectivity optimization, and preparative isolation, providing a practical route to functionally validated ligands from complex natural products. Download: Download high-res image (162KB) Download: Download full-size image
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高影响因子
MOLECULES
·
2025
·Vol. 30
·期 13
·2701
·
IF 4.6
Jie Zhou,Xinrui Wang,Yangyuxin Liu,Xiaochen Li,Mingze Huang,Helong Bai,Jingang Mo
Obesity is a chronic epidemic caused by abnormal fat metabolism. As a key digestive enzyme, pancreatic lipase (PL) is an important target for regulating fat metabolism. The inhibitory potential of 5,10,15,20-Tetrakis (4-aminophenyl) porphyrin (TAPP), 5,10,15,20-Tetrakis (4-hydroxyphenyl) porphyrin (THPP), meso-Tetra (4-carboxyphenyl) porphine (TCPP), Cu (II) meso-Tetra (4-carboxyphenyl) porphine (Cu-TCPP) on PL was studied by enzymatic kinetics, multi-spectral, and molecular simulation technology. THPP, TCPP, TAPP, and Cu-TCPP all had good PL inhibitory activity (IC50range: 97.49–248.70 μM) and were uncompetitive inhibitors. The order of inhibitory ability was: THPP > TCPP > TAPP > Cu-TCPP. The fluorescence quenching mechanism of THPP to PL was a mixed quenching dominated by static quenching, while TCPP, TAPP, and Cu-TCPP were static quenching. The binding of THPP, TCPP and TAPP to PL was mainly driven by hydrogen bonds and van der Waals forces, while Cu-TCPP was mainly driven by a hydrophobic interaction. Four porphyrin compounds changed the conformation of PL, affected the microenvironment of Tyr and Trp residues, and induced changes in the secondary structure of PL, thereby reducing the stability and catalytic activity of PL. Hydrogen bonds played an important role in the binding stability of THPP, TCPP, TAPP, and PL.
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产品关联
DOI
PubMed
高影响因子
Processes
·
2026
·Vol. 14
·期 2
·340
·
IF 2.8
Tao Luo,Weilu Sun,Jun Liang,Yaqian Bian,Qianhui Zheng,Honghai Wang
In this study, the thermodynamic and kinetic characteristics of the esterification reaction catalyzed by sol–gel immobilized enzyme in a batch reactor were systematically investigated. Parameters including catalyst particle diameter, stirring speed, initial molar ratio, catalyst dosage, reaction temperature, and catalyst reusability were studied and optimized. Finally, the esterification rate of methyl oleate reached 90.01%. The standard enthalpy change in the reaction was calculated using the Van’t Hoff equation. A pseudo-homogeneous (PH) model was employed to simulate the kinetic process of the reaction, and the simulation results provide a reference for the scale-up of the reaction process.
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产品关联
DOI
高影响因子
JSFA Reports
·
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
·
药理学
·
营养学
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DOI
CHEMICAL RESEARCH IN CHINESE UNIVERSITIES
·
2018
·Vol. 34
·期 2
·279-284
·
IF 1.248
Xu Chao,Yin Xuhan,Zhang Chuan,Chen Hongyue,Huang He,Hu Yi
Various imidazolium and choline-based functional ionic liquids(ILs) comprising different cations and anions were grafted onto Burkholderiacepacia lipase(BCL) through surface amino acids coupling. The catalytic ac-tivity, thermostability, organic solvent tolerance and adaptability to temperature and pH changes of the modified BCL were then evaluated in olive oil hydrolysis reaction. The results showed that different combinations of cations and anions in ILs had important influence on the catalytic performance of the modified lipases. BCL modified with IL [Choline][H 2 PO 4 ] was the most improved lipase, in which increases by 1.2 folds in relative activity, 2.5 folds in typi-cal proton solvent(10% methanol, volume fraction), and 1.4 folds in thermostability(after incubation at 70 °C for 2 h) were achieved in relative toits native form. BCL modified with [HOOCEPEG 350 IM][BF 4 ] had higher optimal tempe- rature and pH, and better thermosability compared with the native and other modified BCLs. The conformational changes of BCLs were also confirmed by fluorescence spectroscopy and circular dichroism spectroscopy.
研究领域:
酶工程
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生物催化
·
离子液体
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蛋白质修饰
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DOI
高影响因子
危险品化学品经营许可证（带存储）