CHEMICAL ENGINEERING JOURNAL
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2025
·
IF 13.2
Qi Ao,Ziran Chen,Lin Jiang,Weiwei Jin
Triglycerides (TGA) are important clinical indicator for fatty liver, heart disease, hypertension and other endocrine disorders. Therefore, an accurate and stable TGA detector is crucial for a healthy diet. In this work, we developed a lipase-immobilized electrochemical biosensor with a novel conductive film for efficient detection of TGA. The lipase was embedded in sodium alginate (SA), cyclodextrin (CD) and graphene oxide (GO) film. Cyclodextrin had the effect of enhancing the pore structure of the films and had good binding ability with TGA, thus lipase@GO/SA/CD film showed good catalytic activity. The linear range of the TGA electrode was 0–7.5 mM. In addition, the detection limit was as low as 0.05 mM for the direct detection of TGA. The sensor was successfully recycled with average recovery values ranging from 90.6 % to 96.0 %. The lipase@GO/SA/CD film was suitable for TGA detection in dairy products detection, and provide a new sensing TGA platform.
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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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高影响因子
BIOPROCESS AND BIOSYSTEMS ENGINEERING
·
2026
·
IF 4.3
Shen Ji-Dong,Zhang Meng,Li Meng-Yang,Dong Yu-Qi,Liu Zhi-Qiang,Zheng Yu-Guo
Omega-3 polyunsaturated fatty acids (n-3 PUFAs) offer therapeutic benefits, including triglyceride reduction and management of cardiovascular and neurological disorders. This study investigates the use of fish oil processing by‑products, which consist mainly of fatty acid methyl and ethyl esters, as novel substrates for n‑3 PUFAs production. To overcome the low efficiency of conventional chemical methods and the vulnerability of free lipase to alcohol toxicity and poor reusability, we developed a stable immobilized lipase system. The target enzyme (CALB) was immobilized onto macroporous resin LXTE‑1000 via adsorption‑crosslinking, and optimal hydrolysis conditions were determined. The resulting immobilized enzyme (LXTE‑1000@CALB) showed markedly enhanced thermal and operational stability, retaining approximately 64.21% of its initial hydrolysis degree over ten consecutive batches. This work provides an efficient, green, and sustainable approach for valorizing fish oil by‑products and producing n‑3 PUFAs. Graphical abstract
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CHEMICAL ENGINEERING JOURNAL
·
2026
·
IF 12.5
Jing-Peng Li,Hui-Hang Zhang,Zeng-Hua He,Jun-Bo Tian,Ren-Chao Zheng,Xiao-Ling Tang,Yu-Guo Zheng
(2 S ,3 R )- p -methylsulfonylphenyl serine ethyl ester [(2 S ,3 R )- p -MPSE], a key chiral building block of the aryl β-hydroxy-α-amino ester family, serves as one of the critical intermediates for the synthesis of the veterinary antibiotic florfenicol. Kinetic resolution of rac - threo - p -MPSE by lipases represents a highly promising route. However, low catalytic efficiency of natural enzymes restricted its application. In this study, a lipase BSL from Bacillus subtilis was mined and rational design was performed to obtain a series of mutants. A robust Partial Least Squares (PLS) regression model, integrated with multi-dimensional encoding from the Amino Acid Index Database (AAindex) and Fast Fourier Transform (FFT)-based data processing technology, was constructed and trained. Using this machine learning (ML)-driven enzyme engineering approach, a mutant E115F/L67D/I421Q/P317I was successfully created, showing a 15.4-fold increase in catalytic efficiency ( k cat / K m ). Under the load of 1 M high substrate concentration, this mutant could achieve complete resolution of rac - threo - p -MPSE within 4 h, yielding optically pure (2 S ,3 R )- p -MPSE ( e.e. s > 99%) with a yield of 97.4% (based on the theoretical amount of single enantiomer). Additionally, the inactive isomer (2 R ,3 S )- p -methylsulfonylphenyl serine [(2 R ,3 S )- p -MPS] was recycled via chemical racemization based on a reversible retro-aldol cleavage mechanism and re-esterification, which facilitated the recycling of the substrate. This study not only breaks through the bottleneck of low catalytic efficiency of natural lipases through a machine learning-mediated precise enzyme engineering strategy, but also establishes a high-benefit chiral preparation process for (2 S ,3 R )- p -MPSE via an enzymatic resolution-chemical racemization coupling system.
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高影响因子
Engineering
·
2022
·
IF 12.834
Xue Cai,Jiang-Wei Shen,Yu Qiang,Jing Hua,Zhang-Qi Ma,Zhi-Qiang Liu,Yu-Guo Zheng
Lipase-catalyzed stereoselective resolution of cis -(±)-dimethyl 1-acetylpiperidine-2,3-dicarboxylate ( cis -(±)-1) is an attractive route for the synthesis of ( S,S )-2,8-diazobicyclo[4.3.0]nonane, an important chiral intermediate of the fluoroquinolone antibiotic, moxifloxacin. In our previous study, a lipase from Sporisorium reilianum (SRL) was identified to possess excellent thermostability and pH stability. However, the low enzymatic activity of the SRL is a challenge that must be addressed. A rational design was initially employed for SRL tailoring according to the engineered Candida antarctica lipase B (CALB), resulting in a beneficial variant called SRL-I194N/V195L. Subsequently, two key amino acid residues in loop 6, L145 and L154, which might modulate the lid conformation between open and closed, were identified. A tetra-site variant, SRL-I194N/V195L/L145V/L154G (V13), with a significantly enhanced activity of 87.8 U∙mg −1 was obtained; this value was 2195-fold higher than that of wild-type SRL. Variant V13 was used to prepare optically pure (2 S ,3 R )-dimethyl 1-acetylpiperidine-2,3-dicarboxylate ((2 S ,3 R )-1), resolving 1 mol∙L −1 cis -(±)-1 with a conversion of 49.9% in 2 h and absolute stereoselectivity ( E > 200). Excellent stability with a half-life of 92.5 h was also observed at 50 °C. Overall, the study findings reveal a lipase with high activity toward cis -(±)-1 at an industrial level and may offer a general strategy for enhancing the enzyme activity of other lipases and other classes of enzymes with a lid moiety.
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JOURNAL OF FOOD SCIENCE
·
2022
·Vol. 87
·期 2
·651-663
·
IF 3.693
Hao-Xiang Gao,Heng-Yu Liang,Nan Chen,Bi Shi,Wei-Cai Zeng
Ligustrum robustum (Rxob.) Blume is traditionally served as a functional tea in China. In this work, the antioxidant activities of L. robustum (Rxob.) Blume extract (LRE) were evaluated and its inhibitory effect and mechanism on pancreatic lipase were further investigated. With the high contents of phenols (139.70 ± 1.41 mg gallic acid equivalent/g extract) and flavonoids (326.46 ± 7.36 mg rutin equivalent/g extract), LRE showed significant antioxidant activities ( p < 0.05) for scavenging free radicals and hydrogen peroxide, inhibiting lipid peroxidation and providing strong reducing power. Meanwhile, LRE displayed remarkable inhibitory activity on pancreatic lipase with a low half-effective inhibitory concentration (IC 50 ) of 2.469 ± 0.005 mg/ml which was further determined as non-competitive inhibition. The spectroscopic results showed that LRE inhibited the activity of pancreatic lipase by modifying the tertiary and secondary structures of lipase. Moreover, four phenolic compounds (acteoside, lipedoside A, oleuropein and ligurobustoside C) were identified from LRE by the high performance liquid chromatography-quadrupole- time of flight-mass spectrometry. In addition, according to molecular docking analysis, the four phenols could interact with pancreatic lipase by hydrogen bonds, so as to change the spatial structure of pancreatic lipase and inhibit its catalytic activity. The present results suggest that LRE not only exhibits strong antioxidant capacity but possesses effectively inhibitory activity on pancreatic lipase, which might have the potential to be developed as functional food and nutraceuticals for the prevention of metabolic diseases. Practical Application Ligustrum robustum (Rxob.) Blume extract has been confirmed to possess antioxidant activity and lipase inhibitory activity, which indicates that the L. robustum extract has the potential to prevent oxidative stress and regulate fat metabolism. This work suggests that L. robustum extract can be served as a novel resource to prepare nutraceuticals and functional food in food industries.
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高影响因子
APPLIED CATALYSIS A-GENERAL
·
2021
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IF 5.706
Qian Wang,Meiling Ge,Xuan Guo,Zhijun Li,Agen Huang,Fu Yang,Rong Guo
The mesoporous supports of alkylated poly(ionic liquid)s (PILs) are got through free radical copolymerization . With an immobilization yield of 99% for Candida antarctica lipase B (CalB), the biocatalyst showed high advantage for biodiesel production under mild conditions. Typical catalyst CalB 0.2 @PIL-C8 was capable of effectively converting soybean oil into biodiesel with a yield of 68.2%, which is higher than Novozym 435 for 57.5%. The biodiesel yield was almost 1.5 folds compared to that of free CalB under the same conditions. And the catalyst remained about 80% activity in a seven-run recovery test with no CalB leaching in the whole process. The hydrophobic PILs not only provide a suitable reaction micro-environment but also can help CalB keep an open conformation in immobilizing with its flexible hydrophobic alkyl chains. This research offered a green and effective strategy for regulating the hydrophobicity and surface potential of support to enhance the performance of immobilized lipase.
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APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
·
2020
·Vol. 193
·期 3
·717-729
·
IF 2.277
Zhang Jun,Tian Miao,Chen Xiaoyan,Lv Pengmei,Luo Wen,Wang Zhiyuan,Xu Jingliang,Wang Zhongming
Biodiesel biosynthesis with enzymatic transesterification is considered green, sustainable, and environmentally friendly method. Lipase from Burkholderia cepacia G63 has excellent catalytic properties in biodiesel production. Lipase chaperones promote secretion and folding of enzymes, thereby enhancing enzymatic activity. In the current study, heterologous co-expression of lipase (lipA) and chaperone (lipB) was achieved in Escherichia coli through codon optimization. The enzymatic activity of purified and renatured lipAB was 2080.23 ± 19.18 U/g at 50 °C and pH 8.0. Moreover, lipAB showed increased resistance to pH and temperature changes, and lipAB retained stable catalytic properties after treatment with metal ions, organic solvents, and surfactants, namely Mg 2+ , methanol, and Triton-100X. Besides, using recombinant lipase lipAB as catalysts, biodiesel was synthesized using rapeseed oil under 50 °C for 72 h with a yield of 90.23%. Thus, the current study confirmed that co-expression of lipase and its chaperone is an effective strategy to enhance enzyme activity and improve the biochemical profile, meanwhile, showing that lipAB is a promising biocatalyst for biodiesel production.
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高影响因子
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2023
·
IF 4.1
Guangzheng Ma,Zihan Zhang,Mei Chen,Yifei Zhang,Binbin Nian,Yi Hu
BACKGROUND The relative low stability, reusability and activity of enzymes made the industrial production of vitamin E succinate (VES) can only be performed with complex processes and high cost using chemical methods. To address these issues, in the present study, an ionic liquids (ILs) modification strategy was developed to improve the activity and stability of lipases in VES synthesis. RESULTS The results showed that the [1-butyl-3-methyl imidazole] [ N -acetyl- l -proline] ILs modified Candida rugosa lipase (CRL) has the highest modification degree (48.28%), activity (774 U g −1 ), thermostability and solvent tolerance in three selected modifiers. Additionally, after reaction condition optimization, the highest yield of VES can be improved to 95.18% at 45 °C for 15 h, which was significantly improved compared to some previous studies. CONCLUSION In the present study, a high-efficiency VES synthesis strategy was successfully developed via modification of lipase. Moreover, the mechanism by which ILs modification can enhance the activity and stability of lipase was investigated via both experimental and computational-aided methods. Molecular dynamics simulation suggested that ILs modification changed the geometry of Phe344 from flat to upright, which significantly reshaped and enhanced the size of substrate binding pocket of CRL. It is also agreement with our circular dichroism and fluorescence spectroscopy results, which suggested that the modification changed the secondary structure of CRL to a certain extent. The larger pocket also endowed the suitable binding pose of succinate, which made the hydrogen bonds between succinate and active site Ser209 become stronger, and thus improving the yield of VES. © 2023 Society of Chemical Industry.
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INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
·
2019
·Vol. 54
·期 6
·2084-2093
·
IF 2.281
Mohamed Abdin,Yahya Saud Hamed,Hafiz Muhammad Saleem Akhtar,Dan Chen,Shanza Mukhtar,Peng Wan,Asad Riaz,Xiaoxiong Zeng
Summary The objectives of this study were to determine the optimal extraction conditions of polyphenols from Syzygium cumini seeds by response surface methodology and investigate their antioxidant activity and inhibition on α-amylase and pancreatic lipase. As results, the optimal extraction conditions in the ultrasonic extraction process which maximised total polyphenols content, minimised the IC 50 values of α-amylase and pancreatic lipase were determined as follows: extraction time 60 min, ethanol concentration 63% and solvent/solid ratio 44 mL g −1 . The main phenolic compounds in partially purified fraction of Syzygium cumini seeds were catechin, epicatechin, kaempferol, gallic, 5-caffeoylquinic, caffeic and ferulic acids. In addition, the partially purified fraction inhibited 87.66 ± 5.55 and 86.61 ± 3.15% of α-amylase and pancreatic lipase, respectively. The results suggested that Syzygium cumini seeds could be explored as a natural antioxidant and could be used as a source of highly antidiabetic and anti-obesity bioactive compounds.
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高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2019
·
IF 3.714
Xin Huang,Xingran Kou,Li Wang,Ruya Ji,Chaoyang Ma,Hongxin Wang
Tangeretin (TAN) is a biologically functional polymethoxylated flavonoid , extracted from the Citrus Peel (Chenpi). Although 5-demethyltangeretin (5-DT) generated through hydrolysis using a TAN precursor has superior biological function to TAN, its traditional preparation methods are difficult due to environmental hazard and low efficiency processes. In this study, the phosphoric acid (a kind of edible acids) was screened as catalysts of TAN hydrolysis conversion to 5-DT. The main conversion-influencing factors of reaction (material/liquid ratio, temperature and time) were investigated and the antioxidant activity of the modified products was determined by measuring DPPH (Diphenylpicrylbenzoquinone) free radical scavenging capacity and total reducing power. The phosphoric acid/ethanol (v/v) ratio of 7:3, material/liquid (g/L) ratio of 2:1, conversion temperature of 175 °C and conversion time of 2 h were attained as optimal conditions with a 93.71% conversion rate. Further, in vitro antioxidant and anti-lipase experiments confirmed that 5-DT was superior to TAN in total reducing power, scavenging capacity of DPPH free radicals (p < 0.01) and inhibition of lipase activities. Therefore, phosphoric acid is proposed as an alternative catalyst for the modification of TAN. Further, it provided technical support for the industrial production of 5DT and its application in functional foods.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2018
·
IF 3.909
Yue Li,Nanjing Zhong,Ling-Zhi Cheong,Jianrong Huang,Hongxiao Chen,Shaoyan Lin
In this study, SBA-15 was modified by a series of silane coupling reagents and later used to immobilize Candida antartica lipase B (CALB). The enzymatic properties of the immobilized CALB samples were studied. In addition, the catalytic performance in glycerolysis of soybean oil for diacylglycerols (DAG) production was also investigated. The highest enzymatic activity up to 6100.00 ± 246.41 U/g was observed from the propyl methacrylate group modified SBA-15 supported CALB. No loss of activity was observed from the propyl methacrylate group modified SBA-15 supported CALB, but a higher-than-initial activity was notably found from 3-aminopropyl group and n -octyl group modified SBA-15 supported CALB after a 4-h incubation in air at 70 °C. 1-isocyanatopropane group modified SBA-15 supported CALB exhibited selectivity for DAG production. DAG content up to 61.90 ± 2.38 wt% and a DAG/MAG ratio at 3.11 ± 0.08 was obtained after a 24-h reaction at 60 °C in a solvent-free system.
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高影响因子
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