Food Bioscience
·
2025
·
IF 5.9
Zhe Xu,Jiale Chang,Zijin Qin,Hanxiong Liu,Xu Yan,Shuang Guan,Xiufang Dong,Jianping Wu,Tingting Li
The effective modulation of pancreatic lipase activities is critical in maintaining blood triglycerides and cholesterol levels within normal physiological ranges. This study investigated the inhibitory effect of peptides from sea cucumber collagen on pancreatic lipase activity through interaction with the Ca-binding sites on the enzyme. Among the five sea cucumber collagen digests (SCCD), the pepsin-digested 2h+trypsin-digested 3h digest (SDP2h+T3h) showed the strongest inhibitory effect on pancreatic lipase. A peptide RDDPEPSYK (RDD), with a sequence of Arg-Asp-Asp-Pro-Glu-Pro-Ser-Tyr-Lys from SDP2h+T3h, was found to target the Ca-binding site of pancreatic lipase, interacting with certain residues including Asp184, Glu187, Lys163, etc. Additionally, a cell study on 3T3-L1 preadipocytes indicated RDD's capability to inhibit adipocyte differentiation, as well as decrease intracellular triglycerides, total cholesterol, and lipid content. The results from this study suggest that RDD is a targeted pancreatic lipase inhibitor with potential applications for obesity control.
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高影响因子
Molecular Catalysis
·
2024
·
IF 3.9
Xiangsheng Zheng,Xiaohong Hao,Yan Wang,Siyu Gao,Dantong Wen,Jinchuan Wang
The development of novel biocatalysts is essential to promote the commercialization of biodiesel production by transesterification reaction. In this paper, Rhizopus oryzae lipase (ROL) was immobilized on an amino-functionalized zirconium-based metal organoskeleton by interfacial adsorption. The immobilization conditions were optimized and the enzymatic properties were tested, and the resulting novel biocatalysts exhibited higher stability and heat resistance. SEM, XRD and BET analyses were used to characterize the biocatalysts and carrier materials. The catalytic performance of ROL@UiO-66-NH 2 in the production of biodiesel by transesterification reaction was explored, and the production process was optimized by response surface method. The results showed that the conversion rate of FAEE reached 82.05% at molar ratio of ethanol/oil of 15.43:1, reaction temperature of 50.28°C, reaction time of 120.9 min, DES addition of 48.08 wt%, biocatalyst addition of 3 wt%, and ultrasonic power of 90 W. In addition, ROL@UiO-66-NH 2 demonstrated good recyclability, with the catalytic efficiency remaining at 71.87% after five cycles.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Yi-Ting Chen,Peng-Tai Long,Hai-Xia Xu,Wen-Jun Wang,Qing-Feng Zhang
Inhibition of pancreatic lipase (PL) is a strategy to prevent obesity. The inhibitory effects of Flos Sophorae Immaturus (FSI) extract and its main flavonoid components, rutin and quercetin, on PL were investigated. The contents of rutin and quercetin in FSI extract were 44.10 ± 1.33 % and 6.07 ± 1.62 %, respectively. The IC 50 values of FSI extract, rutin and quercetin on PL were 322, 258 and 71 μg/mL, respectively. Rutin and quercetin inhibited PL in a reversible and noncompetitive manner. The combination of rutin and quercetin exhibited synergistic inhibitory effects at low concentration. The binding of rutin/quercetin with PL caused the fluorescence quenching of protein. Fluorescence titration showed the binding affinity of quercetin with PL protein was stronger than that of rutin. Circular dichroism analysis showed the binding changed the secondary structure of PL with an increase in random coil and a decrease in α-Helix and β-Sheet. Molecular docking revealed that rutin and quercetin could interact with the amino acid residues around the catalytic site through multiple secondary interactions. In vivo studies showed that FSI extract can reduce fat absorption and promote fecal fat excretion through inhibition of PL activity, and the effects were mainly due to rutin and quercetin.
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PubMed
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2025
·
IF 6.2
Qiong Wang,Mei Zhao,Hossain M. Zabed,Xinrui Tang,Jiaojiao Chen,Jiayin Wang,Haoyang Li,Xianghui Qi
The discovery of novel heat-resistant lipases has the potential to broaden their applications in the food industry and other fields. This study identified a novel heat-resistant lipase PFHL from Pseudomonas fluorescens HK44 based on data-driven mining, which was subsequently expressed in Escherichia coli for its molecular insights into substrate specificity. The purified PFHL demonstrated optimal activity at 60 °C and pH 7.0 with a half-life of 2.52 h and retained 48.23% of its relative activity at 90 °C. The enzyme exhibited a substrate preference for medium-chain fatty acid esters, displaying a catalytic efficiency kcat/Km of 134.31 mM–1·min–1 toward 4-nitrophenyl laurate (pNPC12), 1.45-fold higher than that for 4-nitrophenyl palmitate (pNPC16). Additionally, molecular docking and molecular dynamics simulations were performed to elucidate the mechanism underlying its substrate specificity and catalytic efficiency. The results revealed that pNPC12 fit the catalytic pocket better than pNPC16, and the complex exhibited greater stability during the simulation. Up to seven hydrogen bonds were formed, and the substrate was able to rapidly reach and position itself within the catalytic pocket. These findings offer valuable insights into PFHL’s substrate preferences, laying the groundwork for its rational design and further optimization to enhance its suitability for industrial applications in the future.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2025
·
IF 8.5
Jun Zhang,Jiachi Lei,Kuntai Li,Siran Feng,Shucheng Liu,Jingliang Xu,Zhongming Wang
A hollow macroporous chitin carrier (HMCC) was developed as a high-efficiency platform for lipase immobilization, offering superior specific surface area, biocompatibility, and protein affinity. Using a NaOH/urea/water treatment system, chitin was dissolved and processed into HMCC, leveraging its amphiphilic properties to achieve remarkable interfacial performance. Compared to the conventional chitin carrier (~0.34 mg/g), HMCC-OA exhibited a highest 3.39-fold increase in protein loading capacity. Immobilization of Geobacillus thermocatenulatus lipase 2 (GTL2) on HMCC-OA yielded a hydrolytic activity of 145.95 U/mg, surpassing free GTL2 by 1.14-fold. In addition, the HMCC demonstrated exceptional versatility by supporting various commercial lipases while showcasing optimal hydrolytic efficiency with GTL2. Notably, GTL2 bioreactor mitigated thermal inactivation at elevated temperatures (up to 90 °C), retained high activity across short- to medium-chain fatty acids (C 4 , C 8 , C 10 ), and maintained significant residual activity (51.79 U/mg) after 10 recycling cycles. These results highlight the innovative design and robust performance of HMCC as a sustainable carrier for lipase bioreactor, enabling enhanced biocatalytic performance demanding thermal stability and interfacial activity.
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高影响因子
ACS Food Science & Technology
·
2022
·
IF 0
Huaqing Hou,Huijuan Shangguan,Shan Zhang,Lan Wang,Qianchun Deng,Jie Shi,Lei Zheng
Lutein exhibits remarkable physiological activities such as retinal protection, antioxidant, anti-cancer, and other functions, although it decomposes easily under light or heat. Enzymatic esterification of lutein is vital for its stability and bioavailability in lipophilic foods. Therefore, efficient and green esterification preparation methods are greatly needed. In this work, which prepared graphene-like mesoporous carbons (GMCs) as a matrix, a new biocatalyst emerged to immobilize Candida antarctica lipase B (CALB) and to catalyze the esterification of lutein and succinic anhydride to generate lutein diester. It was characterized by TEM, XRD, TGA, XPS, and BET to verify the successful preparation. The biocatalyst displayed up to 93.32% esterification rate at 45 °C after 72 h, which was 1.56 times higher than that of the free enzyme, and also retained more than 70% of its initial activity after 8 times reuse. To the best of our knowledge, this is the highest esterification rate of lutein diester synthesis, which provides a further idea for the green preparation of lutein esters.
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JOURNAL OF COLLOID AND INTERFACE SCIENCE
·
2021
·
IF 8.128
Le Zhong,Yuxiao Feng,Hongtong Hu,Jiabao Xu,Ziyuan Wang,Yingjie Du,Jiandong Cui,Shiru Jia
Inspired by the interfacial catalysis of lipase , Herein, the hydrophobic ZIF-L coated with polydimethylsiloxane (PDMS) were prepared by chemical vapor deposition (CVD) and used to immobilize lipase from Aspergillus oryzae (AOL) for biodiesel production. The results showed that the PDMS coating enhanced the stability of ZIF-8 and ZIF-L in PBS. Immobilization efficiency of AOL on PDMS-modified ZIF-L was 96% under optimized conditions. The resultant immobilized lipase ( [email protected] ) exhibited higher activity recovery (430%) than [email protected] Meanwhile, compared with free lipase, the [email protected] exhibited better storage stability and thermal stability. After 150 days of storage, the free lipase retained only 20% of its original activity of hydrolyzing p-NPP, while the [email protected] still retained 90% of its original activity. The biodiesel yield catalyzed from soybean oil by free lipase was only 69%, However, the biodiesel yield by [email protected] reached 94%, and could still be maintained at 85% even after 5 consecutive cycles. It is believed that this convenient and versatile strategy has great promise in the important fields of immobilized lipase on MOF for biodiesel production.
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PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2022
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IF 6.056
Ruiguo Cui,Xinyi Che,Lilang Li,Dongxiao Sun-Waterhouse,Jia Wang,Yonghua Wang
Lipase MAJ1 from Janibacter sp. is an sn-1,3 specific lipase for preparing long-medium-long (LML) type structured triacylglycerols (TAGs), but low optimum reaction temperature limited its application. Based on the structure built with Alphafold2 and MD simulation, we performed mutagenesis on the lid domain. The mutants L171A, A182P and P192C-T100C increased the optimum temperatures by 5 °C, 5 °C and 10 °C, respectively. The combination of three mutations (MAJ1 M4) increased the optimum temperature by 10 °C and a 5.5-fold increase in activity on tricaprylin. The residual activity of MAJ1 M4 was 70% after 60 min incubation at 45 °C, compared to no residual activity determined for MAJ1 wild-type in the same condition. The production of LML with the immobilized lipase MAJ1 M4-catalyzed interesterification was 57.1 mol% in 24 h compared with 44.3 mol% produced by MAJ1 wild-type. Moreover, the immobilized MAJ1 M4 retained 93% productivity after 13 cycles of synthesis. This mutagenesis design would pave the way for the application of MAJ1 in the food industry.
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Scientific Reports
·
2017
·Vol. 7
·期 1
·1-5
·
IF 4.259
Wang Xu-Ping,Zhou Peng-Fei,Li Zhi-Gang,Yang Bo,Hollmann Frank,Wang Yong-Hua
A Ser105Ala mutant of the lipase B from Candida antarctica enables ‘perhydrolase-only’ reactions. At the example of the chemoenzymatic Baeyer-Villiger oxidation of cyclohexanone, we demonstrate that with this mutant selective oxidation can be achieved in deep eutectic solvent while essentially eliminating the undesired hydrolysis reaction of the product.
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BIOCHEMICAL ENGINEERING JOURNAL
·
2023
·
IF 3.9
Balaji Panchal,Jinxi Wang,Yuzhuang Sun,Kai Bian,Cunliang Zhao,Qiaojing Zhao,Bangjun Liu
Lipase from Burkholderia species immobilized onto novel mesoporous polymeric ionic liquids (MO(Poly)C n –BLE) could be utilized as a low–cost biocatalyst for the lipase-catalyzed synthesis of free fatty acid esters from dried municipal sewage sludge. To assess this, this investigation has focused on three main parts of this process: (i) the development of a series of large surface polymer synthesis; (ii) mesoporous polymeric biocatalyst preparation using lipase from Burkholderia sp. immobilization onto MO(Poly)C n , and supports for this alongside Mesoporous polymer ionic liquid–1–bromooctane–lipase from Burkholderia sp. enzyme (MO(Poly)C 18 –BLE) were characterized using FT-IR, SEM, XPS , N 2 , and TGA ; (iii) Response surface methodology was used to determine the optimal conditions for ester production from municipal sewage sludge lipids using a central composite design. Four process variables were assessed at three levels; a total of 13 experiments were performed to study the effects of the lipids: ethanol molar ratio, catalyst concentration, reaction time, and temperature on the ester’s yield. A 91.25% ester yield was obtained under optimal conditions: a 1:12 molar ratio of municipal sewage sludge lipid to ethanol, 225 wt% MO(Poly)C 18 –BLE, 5 h reaction time, 45 ℃ reaction temperature, and a constant 150 rpm agitation. This novel biocatalyst synthesis method and ester production process from municipal sewage sludge lipids may provide ecological and economic support for industrial biodiesel production in the future.
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CHINESE CHEMICAL LETTERS
·
2016
·
IF 1.947
Dong-Hang Yin,Wei Liu,Zhi-Xiang Wang,Xin Huang,Jing Zhang,De-Chun Huang
The direct three-component aza-Diels–Alder reaction was conducted with lipase as a catalyst for the first time. Under the optimized conditions, the aza-Diels–Alder reaction catalyzed by lipase from Candida sp. 99–125 provided the products in moderate to excellent yields. Meanwhile, the endo / exo ratio reached up to 88:12.
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CHINESE JOURNAL OF CHEMICAL ENGINEERING
·
2023
·
IF 3.8
Yong-Yi Zeng,Xin-Yi Xu,Jin-Xuan Xie,Wen-Li Chen,Lan Liu,Xin-Jian Yin,Bi-Shuang Chen
Alkane-based biodiesel is considered the next generation of biodiesel owing to its potential environmental benefits and the fact that it exhibits much higher specific caloric values than traditional biodiesel. However, the formidable obstacle impeding the commercialization of this cutting-edge fuel alternative lies in the cost associated with its production. In this study, an engineered strain Escherichia coli ( E. coli ) showcasing harmonized coexpression of a lipase (from Thermomyces lanuginosus , TL L) and a fatty acid photodecarboxylase (from Chlorella variabilis , Cv FAP) was first constructed to transform triglycerides into alkanes. The potential of E. coli BL21 (DE3)/pRSFDuet-1- TL L- Cv FAP for alkane synthesis was evaluated with tripalmitin as a model substrate under various process conditions. Following a comprehensive examination of the reaction parameters, the scope of the biotransformation was expanded to ‘real’ substrates (vegetable oils). The results showed that bioderived oils can be transformed into alkanes with high yields (0.80–10.20 mmol·L –1 ) under mild conditions (35 °C, pH 8.0 and 36 h) and blue light illumination. The selected processes were performed on an increased lab scale (up to 100 ml) with up to 24.77 mmol·L –1 tripalmitin, leading to a yield of 18.89 mmol·L –1 pentadecane. With the employment of a method for efficiently producing alkanes under mild conditions alongside a simple procedure to isolate alkanes from the reaction system, the utilization of sustainable biomass as a fundamental feedstock emerges as the primary solution to lower the cost of alkane-based biodiesel. Thus, this study proposes a readily implementable and highly effective approach for alkane-based biodiesel production.
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