INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2018
·
IF 3.909
Jike Lu,Pei Wang,Zhaodi Ke,Xin Liu,Qiaozhen Kang,Limin Hao
In order to study the effect of metal ions on the enzymatic hydrolysis of hemp seed oil by Candida sp. 99–125, the spectroscopy, stability and hydrolytic activity of the biocatalyst were investigated in presence of Ca 2+ , Mg 2+ , Fe 2+ , Fe 3+ , Cu 2+ , Sn 2+ , Pb 2+ , Zn 2+ and Ba 2+ metal ions, respectively. The UV spectroscopy showed that all the metal ions enhanced the absorbance but the decrease of fluorescence intensity was observed. All the metal ions could improve the lipase thermal stability except Cu 2+ and Ba 2+ . Hydrolysis of hemp seed oil proved that Ca 2+ , Fe 3+ , Pb 2+ and Ba 2+ could significantly improve the hydrolytic rate, and metal ions could influence lipase selectivity. The study revealed that metal ions could improve lipase stability, hydrolysis activity in the hydrolytic process of hemp seed oil by Candida sp. 99–125.
✓ 已验证
DOI
PubMed
高影响因子
JOURNAL OF MOLECULAR LIQUIDS
·
2025
·
IF 5.2
Shan Zhao,Qiyan Huang,Yiran Wang,Yujing Wang,Wenyu Wang,BenxuYang,Aiguo Feng,Chao Li,Shufen Wu,Changlu Wang
Pancreatic lipase inhibitors are promising agents for reducing dietary fat absorption and improving obesity-related complications. This study systematically investigated the inhibitory effects of two Monascus yellow pigments, ankaflavin (AK) and monascin (MS), on porcine pancreatic lipase (PPL) using enzyme kinetics, spectroscopy, and molecular docking approaches. Both AK and MS exhibited dose-dependent and reversible non-competitive inhibition, with IC 50 values of 50.2 ± 1.4 μM and 120.6 ± 1.8 μM, respectively. Fluorescence and circular dichroism (CD) analyses revealed that AK and MS binding induced conformational changes in PPL, as evidenced by an increase in α-helix content and altered micro-environment around tyrosine (Tyr) and tryptophan (Trp) residues. Notably, AK elicited more pronounced structural perturbations than MS. UV–visible spectroscopy confirmed the formation of intermolecular charge-transfer (CT) complexes upon the binding of AK and MS to PPL, verifying their direct interaction. Molecular docking and chemical modification identified key residues (Lys, Arg, Glu, and Tyr) that were essential for inhibitor binding. Furthermore, the combination of AK, MS, and Orlistat produced a synergistic inhibitory effect on PPL activity (combination index <0.57). These results establish AK and MS as potent natural PPL inhibitors and suggest that their anti-obesity potential stems from the structural modulation of PPL.
✓ 已验证
产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2025
·
IF 8.5
Yan Li,Fan Yang,Xuemei Tan,Yitong Li,Chunjie Gong,Huanan Li,Wanli Cheng,Wenjing Xiao,Jiashu Liu,Zhengbing Jiang
2.5-Furandicarboxylic acid (FDCA) is considered a next-generation bio-based platform chemical that can serve as a precursor to polyethylene furanoate. This study established a dual-enzyme cascade system for FDCA production utilizing lipase from Burkholderia sp. RF7-non_BP1 ( BP 1-Lip) and alcohol oxidase from Colletotrichum gloeosporioides ( Cgl AlcOx). The reaction was carried out in two steps, the molar yield of 5-hydroxymethyl-2-furancarboxylic acid (HMFCA) reached 94.44 ± 3.02 %% after 24 h, and the molar yield of FDCA reached 100 ± 1.96 % after 84 h, with a productivity of 9.29 mg/L/h. In addition, the conversion of 50 mM HMF was successfully achieved by feeding batch substrate addition strategy. After a total reaction time of 264 h, the FDCA concentration reached 41.03 mM, with an FDCA productivity of 24.26 mg/L/h. Molecular docking analysis of BP 1-Lip with HMF showed that the aldehyde group is easily oxidized and can form multiple hydrogen bonds with residues such as Asn110, Lys127, and Asn130. etc.; Lys127 enhances binding stability by localizing substrates through salt bridges and π-cation interactions; Hydrophobic residues Val131 and Tyr292 stabilize the furan ring localization and maintain the ideal conformation of the substrate; The electronic/spatial effects of hydroxymethyl and furan conformations make it difficult for HMFCA and DFF to effectively bind, inhibiting further oxidation.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Materials Science & Engineering C-Materials for Biological Applications
·
2014
·
IF 2.736
Chunfeng Wang,Yanjing Li,Guowei Zhou,Xiaojie Jiang,Yunqiang Xu,Zhaosheng Bu
Lipase from Candida rugosa (CRL) was chemically and physically immobilized onto four types of rod-shaped mesoporous silica (RSMS). RSMS prepared using surfactant P123 and poly(ethylene glycol) as co-templates was functionalized with (3-aminopropyl)triethoxysilane (APTES) to obtain P-RSMS by post-synthesis grafting. Tetraethoxysilane was hydrothermally co-condensed with APTES to obtain C-RSMS. A two-step process using APTES and glutaraldehyde was also performed to obtain G-RSMS. The effects of modification methods (including post-synthesis grafting and co-condensation) and glutaraldehyde on the mesoscopic order, interplanar spacing d 100 , cell parameter a 0 , mesoporous structure, and wall thickness of RSMS were studied in detail. Results showed that all samples were mesoporous materials with 2D mesostructures ( p 6 mm ). Pore size and d 100 decreased, whereas the wall thickness increased after different modifications. CRL was used as a model enzyme to determine the effect of physical and chemical adsorption on loading amount and enzymatic activity. The possible mechanism of CRL immobilization on G-RSMS by chemical adsorption was systematically investigated. The chemical immobilization of CRL on G-RSMS increased the loading amount, hydrolytic activity, thermal stability, and reusability. Moreover, immobilized CRL was employed to catalyze the resolution of 2-octanol by esterification with caprylic acid. The enantiomeric excess of 2-octanol was 45.8% when the reaction was catalyzed by G-RSMS-CRL and decreased to about 38%–39% using the physically immobilized CRL, after 48 h of reaction in hexane.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
BIOMACROMOLECULES
·
2021
·
IF 6.988
Yu Zhang,Bo Xia,Yanyan Li,Xianfu Lin,Qi Wu
The synthesis of optically pure polymers is one of the most challenging tasks in polymer chemistry. Herein, Novozym 435 (Lipase B from Candida antarctica, immobilized on Lewatit VP OC 1600)-catalyzed polycondensation between d-/l-aspartic acid (Asp) diester and diols for the preparation of helical chiral polyesters was reported. Compared with d-Asp diesters, the fast-reacting l-Asp diesters easily reacted with diols to provide a series of chiral polyesters containing N-substitutional l-Asp repeating units. Besides amino acid configuration, N-substituent side chains and the chain length of diols were also investigated and optimized. It was found that bulky acyl N-substitutional groups like N-Boc and N-Cbz were more favorable for this polymerization than small ones probably due to competitively binding of these small acyl groups into the active site of Novozym 435. The highest molecular weight can reach up to 39.5 × 103 g/mol (Mw,Đ = 1.64). Moreover, the slow-reacting d-Asp diesters were also successfully polymerized by modifying the substrate structure to create a “nonchiral” condensation environment artificially. These enantiocomplementary chiral polyesters are thermally stable and have specific helical structures, which was confirmed by circular dichroism (CD) spectra, scanning electron microscope (SEM), and molecular calculation.
✓ 已验证
DOI
高影响因子
JOURNAL OF MOLECULAR STRUCTURE
·
2025
·
IF 4.7
Dantong Wang,Hanqing Xie,Yongqi Zeng,Fengxi Li,Lei Wang,Peng Chen,Zhi Wang
This study presented, for the first time, a method for synthesizing 4-amino-3,5-dicyano-6-aryl phthalates using porcine pancreatic lipase (PPL) as a catalyst. We synthesized 18 derivatives of 4-amino-3,5-dicyano-6-aryl phthalates employing aryl aldehyde, acetylenic esters, and malononitrile under optimal conditions for 4 h, with water serving as the primary reaction medium. The yields of the target products ranged from moderate to high, achieving 43 % to 95 %. This method demonstrates an excellent tolerance for various functional groups. Furthermore, this paper elucidates the reaction mechanism through molecular docking studies and confirms the interaction between the substrate and lipase. The data indicate that the measured distance from the substrate to the catalytic triad is 3.8 Å, with a binding energy of -4.6 kJ/mol, suggesting that PPL demonstrates the strongest catalytic potential in this specific reaction. Additionally, the aforementioned products underwent molecular docking analysis with three selected enzyme targets from Leishmania, highlighting their potential as lead compounds for anti-Leishmania activity.
✓ 已验证
DOI
高影响因子
Foods
·
2025
·Vol. 14
·期 24
·4272
·
IF 5.1
Mengqi Wang,Yi Zhang,Yunqi Gao,Huanyu Zheng,Mingming Zheng
Ethyl butyrate is a typical flavor ester with pineapple-banana scents, but the poor yield from natural fruits limits its feasibility in food and fragrance industries. In this study, dendritic fibrous nano-silica (DFNS) was hydrophobically modified with octyl groups (DFNS-C 8 ) to immobilize Candida antarctica lipase B (CALB) for solvent-free esterification of ethyl butyrate. The immobilized lipase CALB@DFNS-C 8 , with the enzyme loading of 354.6 mg/g and the enzyme activity of 0.064 U/mg protein, achieved 96.0% ethyl butyrate conversion under the optimum reaction conditions where the molar ratio of butyric acid to ethanol was 1:3, with a reaction temperature and time of 40 °C and 4 h. Under the solvent-free catalytic reactions, CALB@DFNS-C 8 presented the maximum catalytic efficiency of 35.1 mmol/g/h and retained 89% initial activity after ten reuse cycles. In addition, the immobilized lipase can efficiently catalyze the synthesis of various flavor esters (such as butyl acetate, hexyl acetate, butyl butyrate, etc.) and exhibits excellent thermostability and solvent tolerance. A molecular docking simulation reveals that the hydrophobic cavity around the catalytic triad stabilizes the acyl intermediate and ensures the precise orientation of both acid and alcohol substrates. This work provides new insights into the sustainable production of flavor esters using highly active and recyclable immobilized lipases through rational carrier hydrophobization and structural confinement design.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
·
2013
·
IF 2.823
Jun Liu,Hongtao Guo,Qiongbo Zhou,Jianying Wang,Bokai Lin,Haibo Zhang,Zhanyang Gao,Chunlan Xia,Xiaohai Zhou
Herein, we demonstrated a environmental-friendly biocatalytic route for the synthesis of dimethyl carbonate (DMC), which is the first example to use enzyme in the process. Moreover, immobilization of Penicillium expansum lipase (PEL) using environmentally benign and biodegradable CMC–PVA polymer has significantly enhanced the catalytic activity thus making them an eligible biocatalyst for synthesis of DMC. The biocatalyst revealed high catalytic performance even under ambient pressure and low temperature (conversion of EC to 94%, yield of DMC to 93% and selectivity of DMC to 99%). The immobilized lipase was effectively recycled for four consecutive cycles providing good yields of the desired product. Accompanying with the intense requirement for the green chemicals and process, our work can provide a useful idea for “green and clean” of harmful chemical reaction.
✓ 已验证
DOI
高影响因子
PROCESS BIOCHEMISTRY
·
2026
·
IF 4.4
Haotian Ma,Peiting Li,Yuequn Liu,Xiuxia Wang,Keke Zhang,Wei Zhuang,Zhenfu Wang
Four fatty acids (lauric acid (LA), myristic acid, palmitic acid, and stearic acid were employed as the template molecules to imprint Rhizomucor miehei lipase (RML) for the synthesis of 1,3-dioleoyl-2-palmitoylglycerol (OPO) by acidolysis reaction. Results indicated that the catalytic activity of bio-imprinted RML was higher than non-imprinted RML but decreased as the aliphatic chain length of fatty acids increased. The mechanism was studied through molecular dynamics simulation, and we found that fatty acids-imprinting affected the whole conformation, lid domain, and active site of RML, thus resulting in the diverse effects of fatty acids with different aliphatic chain lengths on the substrate accessibility, catalytic triad, and the stability of catalytic intermediate of bio-imprinted RML. Finally, LA-imprinted RML was utilized to catalyze OPO synthesis. Upon the optimal reaction conditions, C52 content and ( sn -2, P)/P value of OPO product reached 58% and 65%, respectively. This study would provide structure-function insights for designing efficient bio-catalysts and contribute to the development of bio-catalysts for food industry.
✓ 已验证
产品关联
DOI
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2026
·
IF 7.1
Tianyu Cui,Lirui Sun,Yue Li,Jinhui Xie,Haixin Bi,Yan Wang,Chungu Xia,Jiaying Xin
Ball milling enhanced enzyme catalysis is a novel biocatalytic and conversion technology that offers significant potential for development in the food manufacturing industry due to its high efficiency and environmental friendliness. This study aims to investigate the effects of ball milling on lipase-catalyzed synthesis of starch ferulate (SF), focusing on multi-scale structure, physicochemical properties, and digestive characteristics. The results indicate that ball milling enhanced lipase-catalyzed treatment effectively disrupts the dense granular structure of starch, reducing its particle size distribution (425.4 ± 5.50 nm to 226.8 ± 10.18 nm), relative crystallinity (42.21 ± 1.24 to 13.27 ± 1.53), short-range ordered structure (1.69 ± 0.017 to 0.38 ± 0.17), and double helix structure (1.25 ± 0.035 to 0.84 ± 0.010). As well, the gelatinization temperature and viscosity of SF prepared by ball milling enhanced lipase-catalyzed treatment were significantly decreased, and the anti-aging property and the content of resistant starch (8.48 ± 0.52 to 24.83 ± 0.91) were significantly increased. These results provide both a new insight into the preparation methods for phenolic acid-modified starch and facilitate the development of low-viscosity, processing-stable, functional starch products and starch gels.
✓ 已验证
DOI
高影响因子
Catalysts
·
2026
·Vol. 16
·期 5
·377
·
IF 4.5
Sining Wei,Mahwish Aziz,Yilin Zhang,Jian Xiong,Cheng Cheng,Bin Wu
This study addressed the issue of insufficient activity in CALB lipase during the catalytic synthesis of key chiral intermediates for moxifloxacin. A structure-guided protein engineering strategy was employed to systematically modify its functional domains. Through molecular dynamics simulations of CALB-I189K, multiple regions exhibiting high conformational flexibility were preliminarily identified. Subsequently, by integrating 3D structural alignment with active site pocket distance analysis, the functionally most critical region (143–146) was selected. A site-directed saturation mutation library was constructed specifically targeting this region. Building upon the previously reported CALB-I189K, a mutant I189K/L144R/A146K was ultimately obtained through high-throughput screening combined with chiral HPLC validation. This mutant maintains excellent stereoselectivity (E = 206.52) while enhancing catalytic efficiency (kcat/Κm) to 273.73 min−1·mM−1, approximately 4.5-fold that of I189K. At a substrate concentration of 1 M, it achieves 50% conversion within 2.6 h, demonstrating kinetic resolution capabilities approaching industrial standards. Molecular simulation analysis indicates that the L144R and A146K mutations synergistically enhance catalytic performance primarily by optimizing spatial distances between catalytic residues. This study not only provides a high-performance catalyst for the efficient biosynthesis of moxifloxacin chiral intermediates but also offers new insights for enzyme rational design based on dynamic structural information.
✓ 已验证
DOI
高影响因子
FOOD CHEMISTRY
·
2026
·
IF 10.4
Hongli Chao,Jing Wang,Yi Wang,Jing Tian,Yi Yang
Flavor esters are extensively used in food and cosmetic industries, yet their sustainable production remains challenging. This study developed a lipase bioreactor through artificial antibody-antigen-mediated immobilization for biocatalytic flavor ester synthesis via transesterification. Artificial antigens were prepared by lipase modification with p -nitrobenzaldehyde, while artificial antibodies were synthesized using 2-(4-nitrophenyl)-1,3-dioxolane (acetal-protected p -nitrobenzaldehyde analogue) as template molecules. These components self-assembled into immobilized lipase with 82.24 ± 0.13% immobilization efficiency, 17.59 ± 0.12 mg/g capacity, and 8.81 ± 0.27 U/mg specific activity. Integrating molecular simulations with acyl donor screening, the bioreactor achieved 97.18 ± 0.93% yield for cinnamyl acetate synthesis from cinnamyl alcohol and vinyl acetate. The system demonstrated exceptional continuous catalysis and scalability, confirming industrial translation potential. Successful synthesis of cinnamyl butyrate (86.25 ± 3.34%) and benzyl acetate (90.68 ± 2.25%) further established its versatility as a platform for diverse flavor ester production.
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）