Chinese Journal of Natural Medicines
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2016
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IF 1.382
Feng TIAN,Hao-Yu LV,Ji-Long ZOU,Yi WANG,Meng-Jun DUAN,Xiao-Qin CHU,Dan LI,Liang ZHU,Jian-Qin JIANG
The present study was designed to synthesize and evaluate a series of benzylisoquinoline derivatives. These compounds were synthesized by Bischler-Napieralski cyclization to yield 1-benzyl-3,4-dihydroisoquinolines, and the products were obtained by reductions. All these compounds were identified by MS, 1 H NMR and 13 C NMR. The inhibitory activities on pancreatic lipase and preadipocyte proliferation for the synthesized compounds and alkaloids from Nulembo nucifera were assessed in vitro . Most of the compounds showed inhibitory activities on both pancreatic lipase and preadipocyte proliferation. Particularly, compounds 7p–7u and 9d–9f exhibited significant inhibitory activity on pancreatic lipase while compounds 7c, 7d, 7f, 7g, 7i , and 7j potently inhibited the proliferation of 3T3-L1 preadipocytes. Our results provided a basis for future evaluation and development of these compounds as leads for therapeutics for human diseases.
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JOURNAL OF COLLOID AND INTERFACE SCIENCE
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2016
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IF 3.782
Ruipu Xin,Faez Iqbal Khan,Zexin Zhao,Zedong Zhang,Bo Yang,Yonghua Wang
The mechanism of lipase binding to the lipid-water interface is crucial for substrate specificity and kinetic properties. In this study, the chain-length specificity, regiospecificity and substrate specificity of Phospholipase A 1 (PLA 1 ) and its parent enzyme Thermomyces lanuginosus lipase (TLL) have been investigated using a classical emulsion system. The results show that both PLA 1 and TLL are 1,3-regioselective lipases. Additionally, the hydrolytic activity of PLA 1 is comparatively lower on short-chain triacylglyceride (TAG) and higher on phosphatidylcholine (PC) than the hydrolytic activity of TLL. Further, the results obtained with monolayer film techniques demonstrate that the C-terminal region regulates the binding of PLA 1 to PC. A hypothesis is presented according to which the α9 helix of C-terminal region in PLA 1 not only controls the opening of lid but also serves as a membrane anchor that assists in binding to PC. These findings bring new insight into rational design of novel lipases with intriguing functionalities.
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PHYTOCHEMISTRY
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2017
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IF 3.205
Miao Wang,Dongyu Gu,Haoquan Li,Qi Wang,Jie Kang,Tingting Chu,Hong Guo,Yi Yang,Jing Tian
A facile method based on gas chromatography–mass spectrometry (GC–MS) and molecular docking was established to analyze, identify, and predict lipase inhibitors in volatile oil from Pinus massoniana L. needles (PMLN). The volatile oil, with an IC 50 value of 15.25 ± 0.06 μg/mL, exhibited potential inhibitory activity against lipase in vitro. In total, 33 compounds were identified from the volatile oil through GC–MS analysis. The major compounds in the volatile oil were β-pinene (39.24%), α-pinene (14.68%), germacrene D (9.08%), caryophyllene (6.94%), α-terpineol (5.39%), β-phellandrene (4.82%), and D-limonene (3.93%). The identified compounds were individually docked with lipase as the target through molecular docking. Among the compounds, longifolene characterized by preferable binding energy and the good inhibition constant exhibited potential lipase inhibitory activity. The IC 50 value of longifolene was 25.10 ± 0.49 μM, indicating that this compound is the active ingredient responsible for the lipase inhibitory activity of PMLN volatile oil.
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JOURNAL OF THE BRAZILIAN CHEMICAL SOCIETY
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2014
·Vol. 25
·期 9
·1704-1711
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IF 1.253
Tan Zhongqin,Fang Miaoli,Du Huan,Song Lelian,Ren Dahai,Tang Xiujuan,Han Xiaoxiang,Liang Xinle
The synthesis between palmitic acid and methanol was carried out in a w/o reverse microemulsion prepared from the mixture of dodecylbenzenesulfonic acid (DBSA)/isooctane/water. Box-Behnken design was adopted to evaluate the effect of significant factors on the methyl palmitate yield and response surface methodology (RSM), which was employed to optimize the process parameters in the esterification. The conditions that showed optimal results for methyl palmitate preparation were: 3.33 w0 ([H2O]/[surfactant]), 4.2 h reaction time, 5:1 methanol/acid molar ratio, and 130 mg g-1 lipase ([lipase]/[acid]) concentration. The following verification experiment obtained a result of 97% in almost total agreement with the expected value (98%). The kinetic constants of the model were determined by experiments at 40 °C with initial concentrations of 0.025-0.25 mol L-1 palmitic acid and 0.025-0.3 mol L-1 methanol in the microemulsion system. The kinetic studies showed that the reaction obeyed the Ping-Pong bi-bi mechanism with inhibition by methanol.
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APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
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2014
·Vol. 172
·期 6
·3287-3296
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IF 1.687
Yu Tingting,Cao Xuejun
Chaotropes could significantly enhance lipase activity recovery in reverse micellar back extraction. However, the mechanism of chaotropes promoting the release of enzyme from reverse micelles was not clear. In this study, chaotropes were added in the process of lipase reverse micellar extraction, and back extraction recovery was improved. In back extraction, at 0.6 M urea in stripping solution, 94.60 % total extraction recovery was obtained. Meanwhile at 0.3 M guanidine hydrochloride, nearly 65 % lipases were released into the stripping solution. DLS and Karl Fischer method results showed that the presence of urea in stripping solution could weaken the electrostatic interaction between lipase and cetyltrimethylammonium bromide molecules, promoting lipase release from reverse micelles, and guanidine hydrochloride could stimulate lipase and free water molecules enwrapped in reverse micelle release into the stripping solution. These experimental results provide a clue for understanding the mechanism of chaotropes influencing on protein recovery in reverse micelle back extraction.
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JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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2014
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IF 2.745
Yang Zhang,Na Wang,Zong-Bo Xie,Long-Hua Zhou,Xiao-Qi Yu
PPL (lipase from porcine pancreas) was found to catalyze asymmetric cross aldol reactions of aromatic and heteroaromatic aldehydes with various ketones in ionic liquid ([BMIM][PF 6 ]) for the first time. Interestingly, PPL exhibited high catalytic activity and excellent stereoselectivity in this efficient and recyclable room temperature ionic liquid in the presence of moderate water, similar to the results obtained in organic solvents. High yields of up to 99%, excellent enantioselectivities of up to 90% ee, and good diastereoselectivities of up to >99:1 dr were achieved.
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JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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2014
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IF 2.745
Long-Hua Zhou,Na Wang,Guan-Nan Chen,Qi Yang,Sheng-Yong Yang,Wei Zhang,Yang Zhang,Xiao-Qi Yu
Lipase-catalyzed direct vinylogous Michael addition reactions of electron-deficient vinyl malononitriles to nitroalkenes are reported for the first time. A series of nitroalkenes reacting with vinyl malononitriles generate the corresponding products with moderate to high yields in the presence of Lipozyme ® (immobilized lipase from Mucor miehei ) with excellent diastereoselectivities in all reactions under optimized conditions. Docking studies were performed to further elucidate the differences between the various enzymes and substrates. Furthermore, we demonstrated the synthetic potential of the multi-functional products by performing reactions that employed the electron-deficient alkylidene double bond.
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INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
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2015
·Vol. 16
·期 4
·7273-7288
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IF 2.862
Dongming Lan,Qian Wang,Jinxin Xu,Pengfei Zhou,Bo Yang,Yonghua Wang
Thermostability and substrate specificity are important characteristics of enzymes for industrial application, which can be improved by protein engineering. SMG1 lipase fromMalassezia globosais a mono- and diacylglycerol lipase (MDL) that shows activity toward mono- and diacylglycerols, but no activity toward triacylglycerols. SMG1 lipase is considered a potential biocatalyst applied in oil/fat modification and its crystal structure revealed that an interesting residue-Asn277 may contribute to stabilize loop 273–278 and the 3104 helix which are important to enzyme characterization. In this study, to explore its role in affecting the stability and catalytic activity, mutagenesis of N277 with Asp (D), Val (V), Leu (L) and Phe (F) was conducted. Circular dichroism (CD) spectral analysis and half-life measurement showed that the N277D mutant has better thermostability. The melting temperature and half-life of the N277D mutant were 56.6 °C and 187 min, respectively, while that was 54.6 °C and 121 min for SMG1 wild type (WT). Biochemical characterization of SMG1 mutants were carried out to test whether catalytic properties were affected by mutagenesis. N277D had similar enzymatic properties as SMG1 WT, but N277F showed a different substrate selectivity profile as compared to other SMG1 mutants. Analysis of the SMG1 3D model suggested that N277D formed a salt bridge via its negative charged carboxyl group with a positively charged guanidino group of R227, which might contribute to confer N277D higher temperature stability. These findings not only provide some clues to understand the molecular basis of the lipase structure/function relationship but also lay the framework for engineering suitable MDL lipases for industrial applications.Keywords:mono- and diacylglycerol lipase;thermostability;substrate selectivity;site-directed mutagenesis
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2025
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IF 8.5
Le Zhong,Yuxiao Feng,Zichen Wang,Tian Tian,Yali Bi,Jiandong Cui
Enzymatic synthesis of flavor esters is crucial for applications in food, beverage, and cosmetics industries. However, the poor activity and stability of free lipase hinder these reaction. Inspired by the concept of lipase interface activation, MIL-53(Al)-NH 2 was modified with alkyl acid anhydrides of varying chain lengths to tailor its hydrophobicity, and Candida Rugosa lipase (CRL) was subsequently immobilized on this surface to achieve efficient interface activation. The resulting CRL@MIL-53(Al)-AM11 exhibited 3.5 times higher activity than the unmodified CRL@MIL-53(Al)-NH 2 . Moreover, CRL@MIL-53(Al)-AM11 enabled one-step purification of crude CRL via selective adsorption. It also showed enhanced storage and thermal stability as well as higher resistance to protease degradation and denaturants than free CRL. CRL@MIL-53(Al)-AM11 retained 75 % of its initial activity after 30 min treatment at 55 °C, whereas the free CRL retained only 41 %. After 11 days of storage, CRL@MIL-53(Al)-AM11 maintained 70 % of its initial activity, in contrast to 36 % for the free lipase. Notably, CRL@MIL-53(Al)-AM11 achieved a 97 % conversion rate in the esterification synthesis of the flavoring substance (butyl butyrate) within 24 h and retained over 40 % conversion after five consecutive cycles. Therefore, this strategy offers a feasible approach for constructing high-performance immobilized lipases for flavor ester synthesis.
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INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
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2024
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IF 2.6
Hai-Xia Xu,Qiao-Ting Xu,Zhong-Ping Yin,Ji-Guang Chen,Qing-Feng Zhang
Summary Obesity is becoming a top global health problem. Inhibition of digestive enzymes is an effective approach in weight management due to the reduction of energy absorption. In this study, the inhibitory effects of luteolin on α-glucosidase and pancreatic lipase were investigated in vitro and in vivo via enzyme kinetics, fluorescence quenching, molecular docking and rat experiments. The results showed that luteolin inhibited α-glucosidase and pancreatic lipase in a mixed-type and uncompetitive manner with IC 50 values of 29.31 and 42.74 μg mL −1 respectively. The binding of luteolin with the two enzymes caused the quenching of intrinsic fluorescence of protein. Molecular docking simulation revealed that luteolin could be located in the active pocket of α-glucosidase and interact with the key amino acid residues. Moreover, a hydrophobic interaction and a van der Waals force were formed between luteolin and the key amino acid residues of pancreatic lipase (His264 and Ser153). In vivo studies further confirmed that luteolin could significantly decrease the absorption of glucose and triacylglyceride in rats by inhibiting α-glucosidase and pancreatic lipase.
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LANGMUIR
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2024
·
IF 3.7
Frank Peprah Addai,Jiacong Wu,Feng Lin,Xinnan Ma,Juan Han,Yuelin Liu,Yang Zhou,Yun Wang
In this work, a trimetallic (Ni/Co/Zn) organic framework (tMOF), synthesized by a solvothermal method, was calcinated at 400 and 600 °C and the final products were used as a support for lipase immobilization. The material annealed at 400 °C (Ni-Co-Zn@400) had an improved surface area (66.01 m2/g) and pore volume (0.194 cm3/g), which showed the highest enzyme loading capacity (301 mg/g) with a specific activity of 0.196 U/mg, and could protect the enzyme against thermal denaturation at 65 °C. The optimal pH and temperature for the lipase were 8.0 and 45 °C but could tolerate pH levels 7.0–8.0 and temperatures 40–60 °C. Moreover, the immobilized enzyme (Ni-Co-Zn@Lipase, Ni-Co-Zn@400@Lipase, or Ni-Co-Zn@600@Lipase) could be recovered and reused for over seven cycles maintaining 80, 90, and 11% of its original activity and maintained a residual activity >90% after 40 storage days. The remarkable thermostability and storage stability of the immobilized lipase suggest that the rigid structure of the support acted as a protective shield against denaturation, while the improved pH tolerance toward the alkaline range indicates a shift in the ionization state attributed to unequal partitioning of hydroxyl and hydrogen ions within the microenvironment of the active site, suggesting that acidic residues may have been involved in forming an enzyme–support bond. The high enzyme loading capacity, specific activity, encouraging stability, and high recoverability of the tMOF@Lipase indicate that a multimetallic MOF could be a better platform for efficient enzyme immobilization.
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FOOD CHEMISTRY
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2024
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IF 8.5
Liang Wang,Zheng Zhou,Ji Wang,Xu-Song Wang,Da-Yong Zhou,Lei Qin,Xu-Hui Huang
The regulation of reaction rate differentiation, catalytic precursor differentiation, and end-product differentiation during enzyme-mediated reactions within complex lipid systems is a key area of research in flavor regulation. A multilayer lipid oxidation model, utilizing Plaice bone oil (PBO), lipase, and lipoxygenase, was employed to investigate oxidation differences between various lipids and corresponding flavor formation patterns. Lipase treatment resulted in higher levels of non‑oxygenated volatile compounds and saturated aldehydes, whereas lipoxygenase treatment increased oxygenated compounds, particularly (E)-2-hexenal, 1-penten-3-one, and 2-pentylfuran. The hydrolysis of triglycerides by lipase significantly raised the concentration of monounsaturated fatty acids. Lipoxygenase catalyzed the formation of position-specific oxidation products at the ω-6 carbon position of PUFAs, such as 15-hydroperoxy-EPA and 17-hydroperoxy-DHA. These enzymatic treatments altered the lipid profile, leading to distinct flavor formation patterns. This study provides valuable insights into the mechanisms underlying enzyme-mediated volatile substance variations in food.
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