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IEEE TRANSACTIONS ON INSTRUMENTATION AND MEASUREMENT · 2024 · IF 5.6

Sensitive and Label-Free Optical Fiber Biosensor Based on ZIF-8/Lipase Composite Material and Its Application in Tributyrin Detection

Hongxin Zhang,Xuegang Li,Xue Zhou,Yanan Zhang,Yong Zhao

As a low-density lipoprotein, tributyrin plays a vital role in food safety and human health. In this work, we first proposed a novel high-performance tributyrin sensor made by supporting zeolitic imidazolate framework-8 (ZIF-8) and lipase onto the optic fiber sensor based on the surface plasmon resonance (SPR) principle. After adsorption of lipase within the ZIF-8 framework, through a rapid aqueous synthesis method, a thin and dense ZIF-8 film can be uniformly formed and stably and tightly bonded to the surface of the optical fiber sensor. ZIF-8 is one of the metal–organic frameworks (MOFs), which not only has the high porosity and specific surface area of MOFs, but also shows good affinity with lipase. The experimental results show that the proposed sensor can achieve the specific detection of tributyrin in the linear range of 0.1–3 mM, the sensitivity is 14.75 nm/mM, with a detection limit of 0.096 mM. The sensor proposed in this article for the first time using ZIF-8/lipase composite material to detect tributyrin has an accuracy of more than 83% in sample detection at the range of 0.1–3 mM. In addition, the stability test of the proposed sensor is as good as 0.47 nm, and the selectivity (in the presence of glycine, acetylcholine, glucose, and urea) of the sensor was analyzed. The sensor proposed in this article has the advantages of a low sample consumption of $100~\mu \text{L}$ , high sensitivity, simple structure, and label-free measurement. This method provides a new route for the rapid and reliable detection of tributyrin, which has potential applications in medical research and clinical diagnosis.

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CHEMICAL ENGINEERING JOURNAL · 2025 · IF 13.2

A wearable Kevlar-based glove biosensor integrating proline-modified UiO-66 and lipase for on-site detection of methyl parathion

Chenxi Liu,Xiao Wang,Xiangze Jia,Wanlin He,Shaobo Zhang,Hongsheng Liu

To meet the demand for nondestructive detection, we developed a truly human-wearable glove biosensor, which can be applied for in-situ analysis of pesticides on crop surfaces during the picking process. Herein, the Burkholderia cepacia (BCL)@UiO-66/Pro functionalized Kevlar-based laser-induced graphene (LIG) three-electrode glove sensing system was equipped with biocompatible semisolid electrolyte. In this system, Kevlar-based LIG electrodes showed the lowest sheet resistance of 28.26 Ω/sq. and I D /I G ratio value of 0.163 with optimal laser power of 9 %. Importantly, the BCL@UiO-66/Pro modified on Kevlar-based LIG electrode enhanced the catalytic efficiency of the BCL, the absolute value of the redox potential increases from the −0.412 V to −0.664 V due to an increase in the immobilization efficiency of BCL on UiO-66 after proline modification. In addition, the Kevlar-based wearable glove biosensor exhibited high repeatability, selective and sensitive electrochemical sensing of MP at concentrations ranging from 5 to 40 μM with a low detection limit of 0.84 μM. During the 10-day storage stability test, the fabricated Kevlar-based LIG biosensor demonstrated good reusability and excellent stability for MP detection with retention of more than 96 % of its initial response. Such wearable Kevlar-based glove biosensor could be a transformative approach for the in-situ analysis of pesticide residue on crops, which could also promote future precision agriculture development.

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Foods · 2021 ·Vol. 10 ·期 11 ·2529 · IF 4.35

Lipase Addition Promoted the Growth of Proteus and the Formation of Volatile Compounds in Suanzhayu, a Traditional Fermented Fish Product

Cuicui Jiang,Mengyang Liu,Xu Yan,Ruiqi Bao,Aoxue Liu,Wenqing Wang,Zuoli Zhang,Huipeng Liang,Chaofan Ji,Sufang Zhang,Xinping Lin

This work investigated the effect of lipase addition on a Chinese traditional fermented fish product,Suanzhayu. The accumulation of lactic acid and the decrease of pH during the fermentation were mainly caused by the metabolism ofLactobacillus. The addition of lipase had little effect on pH and the bacterial community structure but promoted the growth ofProteus. The addition of lipase promotes the formation of volatile compounds, especially aldehydes and esters. The formation of volatile compounds is mainly divided into three stages, and lipase had accelerated the fermentation process.Lactobacillus,EnterococcusandProteusplayed an important role not only in inhibition of the growth ofEscherichia-Shigella, but also in the formation of flavor. This study provides a rapid fermentation method for theSuanzhayuprocess.Keywords:fermented fish;Proteus;lipase;volatile compounds;aldehydes;esters

✓ 已验证 DOI PubMed 高影响因子
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Frontiers in Bioengineering and Biotechnology · 2020 · IF 3.644

Highly Efficient Regioselective Decanoylation of Hyperoside Using Nanobiocatalyst of Fe3O4@PDA-Thermomyces lanuginosus Lipase: Insights of Kinetics and Stability Evaluation

Bi Yanhong,Wang Zhaoyu,Tian Yaoqi,Fan Haoran,Huang Shuo,Lu Yihui,Jin Zhengyu

The immobilization of Thermomyces lanuginosus lipase on polydopamine-functionalized Fe3O4 magnetic nanoparticles (Fe3O4@PDA-TLL) as a nanobiocatalyst was successfully performed for the first time, and the Fe3O4@PDA-TLL was used for regioselective acylation of natural hyperoside with vinyl decanoate. The effects of several crucial factors, such as the reaction solvent, substrate molar ratio, temperature, and immobilized enzyme dosage, were investigated. Under optimum conditions, the reaction rate, 6″-regioselectivity, and maximum substrate conversion were as high as 12.6 mM/h, 100%, and 100%, respectively. An operational stability study demonstrated that the immobilized enzyme could maintain 90.1% of its initial maximum conversion even after reusing it five times. In addition, further investigations on the kinetic parameters, like Vmax, Km, Vmax/Km, and Ea, also revealed that the biocompatible Fe3O4@PDA could act as an alternative carrier for the immobilization of different enzymes.

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3 Biotech · 2019 ·Vol. 9 ·期 7 ·1-9 · IF 1.786

Surfactant-modified Aspergillus oryzae lipase as a highly active and enantioselective catalyst for the kinetic resolution of (RS)-1-phenylethanol

Yan Hong De,Guo Bing Han,Wang Zhao,Qian Jun Qing

The lipase from Aspergillus oryzae was modified with a surfactant and then observed to exhibit high catalytic efficiency and enantioselectivity for the kinetic resolution of ( RS )-1-phenylethanol. The influential factors of the modified-lipase preparation were investigated, including the surfactant source, the organic cosolvent, and the buffer pH. The optimum modification conditions were found with a surfactant of polyoxyethylene sorbitan monopalmitate, an organic cosolvent of tetrahydrofuran and a phosphate buffer of pH 7.0. In the transesterification of ( RS )-1-phenylethanol with vinyl acetate, the surfactant-modified lipase showed excellent enantioselectivity for the R -isomer ( E  > 200), giving an enantiomeric excess of higher than 99% for ( R )-1-phenylethyl acetate at 46.8% conversion with the reaction time of 2 h at 30 °C. The enzymatic activity had barely altered after 30 days even at 50 °C when it was saved in a powdered state. The results indicated that the modification strategy was useful and highly efficient, and that modified A. oryzae lipase was a promising biocatalyst in the kinetic resolution of ( RS )-1-phenylethanol.

✓ 已验证 DOI PubMed 高影响因子
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JOURNAL OF FOOD SCIENCE · 2022 ·Vol. 87 ·期 12 ·5276-5288 · IF 3.693

Promoting lipid oxidation and release of volatiles of pork fat pulp by lipase, blue light with riboflavin in liquor immersion

Shiya Liang,Fengjiao Zhang,Songgui He,Weigang Li,Zhenqiang Wu

The deeply oxidized pork fat (PF) is the key in the production of Chi-aroma Baijiu, a Chinese distilled spirit. Previous studies have not proposed an integrated method to promote lipid oxidation of PF, and the formation of volatiles has not been studied. In this work, an efficient method was established to promote lipid oxidation and release of volatiles of pork fat pulp (PFP) in an integrated treatment for the production of Chi-aroma Baijiu. The results showed that the acid value of PFP by lipase pretreatment (T1) was significantly elevated ( p < 0.05), compared to the control (T0). Lipase-blue light-riboflavin-25°C (T2), lipase-open vial-dark-25°C (T3), and lipase-dark-40°C (T4) further promoted lipid oxidation and reached the oxidation level of PFP by F0, while T2 show the best results. The peroxide value of PFP by T2, T3, and T4 was 41.96-, 16.70- and 14.20-fold higher, and the para-anisidine value was 27.13-, 6.94- and 6.70 fold higher than that in T1. The flavor and volatile analyses showed that PFP by T2 had higher response values than T0 at six electronic nose sensors. T2–T4 promoted the release of volatiles and T2 showed the best result. T2 potentially facilitated lipid oxidation, esterification, and substance exchange of PFP, resulting in a higher type (78.57%) and content (114.50%) of volatiles than T0. The integrated treatment with lipase hydrolysis, blue light with riboflavin could promote lipid oxidation and volatiles release to improve production efficiency of deeply oxidized PF. The results would be viably applied to the production of Chi-aroma Baijiu. Practical Application Deeply oxidized pork fat was the key to the production of Chi-aroma Baijiu, while it took a long time (at least 4 months) to prepare. The integrated treatment with lipase hydrolysis, blue light with riboflavin could promote lipid oxidation and volatiles release to improve the production efficiency of deeply oxidized pork fat. The results would be viably applied to the production of Chi-aroma Baijiu.

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eFood · 2023 ·Vol. 5 ·期 1 ·e123 · IF 0

Potential hypoglycemic and hypolipidemic bioactive constituents in Cyclocarya paliurus leaves explored by affinity ultrafiltration with α-glucosidase and pancreatic lipase

Mengjia Xu,Huixia Feng,Mingquan Guo

Cyclocarya paliurus has been widely applied for therapeutic feeding as a traditional Chinese medicine homologous food with high nutritional and medical value. Nevertheless, the specific bioactive compounds liable for hypoglycemic and hypolipidemic properties and underlying mechanisms remain unexplored. In the present study, the in vitro hypoglycemic and hypolipidemic effects of C. paliurus were assessed by α-glucosidase and pancreatic lipase inhibition assays, and the results indicated that 70% ethanol extract exhibited remarkable α-glucosidase and pancreatic lipase inhibitory activity with the IC 50 value of 3.14 μg/mL and 0.98 μg/mL, respectively. A total of 18 and 15 potential ligand candidates were screened, and the chemical structures were characterized. Furthermore, the docking result showed that chlorogenic acid, quercetin, kaempferol 3- O -rhamnoside, and pterocaryoside A contributed to the underlying hypoglycemic and hypolipidemic effects of C. paliurus , further strengthened the bindings of the enzyme-ligand complex and suppressed the enzyme's activity with the binding energies ranged from −4.00 to −6.31 kcal/mol. The interrelations between the specific bioactive constituents, α-glucosidase or lipase, and hypoglycemic or hypolipidemic activities were also carified. The present study reveals substantial prospects of C. paliurus to be developed as a natural dietotherapy, disease-prevention, and healthcare for diabetes and obesity in the near future.

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Molecular Catalysis · 2021 · IF 5.062

Engineering actively magnetic crosslinked inclusion bodies of Candida antarctica lipase B: An efficient and stable biocatalyst for enzyme-catalyzed reactions

Yu Han,Xinying Zhang,Liangyu Zheng

In our previous study, the soluble expression of recombinant Candida antarctica lipase B ( r CalB) in E. coli is achieved through fusion with polyamino acid tails. The present study showed that even in the form of inclusion bodies ( r CalB-IBs), r CalB-IBs were still active towards enzyme-catalyzed reactions. r CalB-IBs could be directly crosslinked by the oxidized dextran in the presence of Fe 3 O 4 nanoparticles to obtain magnetic aggregates ( r CalB-mclIBs), and an activity recovery of 113.9 % ± 2.2 % could be achieved under optimized conditions. The obtained r CalB-mclIBs exhibited excellent thermal and storage stabilities, and a good tolerance in changing pH environmental. r CalB-mclIBs could be effectively recycled and could retain 85.4 % ± 2.5 % of its initial activity, and an e.e. p of 84.4 % ± 2.2 % in ( R , S )-NEMPA-ME hydrolysis was observed after the 10th cycle. After the application of r CalB-mclIBs into a promiscuous carbon–carbon bond-forming reaction, the MBH and the Aldol products could be obtained simultaneously. This study provides a simple and inexpensive strategy to highlight the application potential of r CalB-IBs as a biocatalyst.

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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2025 · IF 8.5

Co-immolization of lipase and bimetallic Cu/Mn aminoclay nanozyme onto montmorillonite for spatially synergistic conversion of p-nitrophenyl esters

Ke Wang,Yuqing Huang,Shiyong Sun,Haoming Tang,Lin Gong,Dongdong Wang,Xueyan Zhang,Sen Lin

The detoxification and valorization of toxic p-nitrophenol (p-NP) and its ester derivatives into high-value p-aminophenol (p-AP) present a significant challenge in green chemistry. This work addresses this challenge by developing a hybrid catalyst through the co-immobilization of lipase and a novel bimetallic Cu/Mn aminoclay nanozyme (CMAC) onto montmorillonite (Mt). The key innovation lies in the multifunctional design of CMAC, which serves not only as a highly active laccase-mimicking nanozyme but also as an intrinsic immobilization matrix for lipase, while the Mt support simultaneously prevents nanozyme aggregation and enhances structural stability. This integrated lipase-CMAC@Mt. platform enables efficient substrate channeling, whereby the p-NP intermediate generated from lipase-catalyzed hydrolysis of p-NPP is directly reduced by adjacent CMAC to p-AP, minimizing intermediate accumulation and overcoming diffusion limitations. As a result, the hybrid catalyst achieves efficient one-pot conversion of p-NPP to p-AP, without requiring harsh reagents or intermediate separation. Remarkably, it exhibits exceptional reusability (76.8 % activity retention after 10 cycles) and storage stability (82.4 % activity retained over 30 days), substantially outperforming conventional free enzyme systems. This study demonstrates a strategic bio-nano synergy that combines the specificity of enzymes with the robustness of nanozymes, offering a scalable and economically viable platform for simultaneous toxic waste elimination and resource recovery.

CAS / MDL: 16940-66-2
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JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE · 2025 ·Vol. 105 ·期 7 ·3931-3941 · IF 3.5

Selective synthesis of triacylglycerols by the ADS-17-supported Candida antarctica lipase B through esterification of oleic acid and glycerol

Jiawei Zheng,Qiangyue Zhang,Nanjing Zhong

BACKGROUND Immobilized enzyme possessing both high activity and good selectivity is important in practice. In this study, Candida antarctica lipase B (CALB) was immobilized onto the macroporous resin ADS-17 for triacylglycerol (TAG) synthesis through esterification of oleic acid and glycerol. The reaction conditions were optimized by single-factor study and orthogonal test, and the reusability of the immobilized CALB (CALB@ADS-17) was evaluated. In addition, the mechanism of lipase immobilization was studied and the catalytic mechanism of CALB@ADS-17 was investigated. RESULTS Oleic acid conversion up to 99.20% and TAG content at 91.58 wt% could be obtained under optimal conditions. In addition, the CALB@ADS-17 retained 84.28% of its initial activity after 11 cycles of reuse. The mechanism of lipase immobilization was through hydrophobic adsorption. The relationship between temperature and oleic acid conversion was ln V 0 = 6.3316 − 4.3321/ T , and the activation energy ( E a ) was 36.02 kJ mol −1 . CALB@ADS-17 did not exhibit an obvious interfacial activation phenomenon. Its kinetic behavior can be described by the Michaelis–Menten model, whose kinetic parameters of v max , k cat , K m , K i , and k ca t /K m were 0.01265 μmol L −1 s −1 , 9310.72 s −1 , 0.4907 mmol L −1 , 3.997 mmol L −1 , and 1.90 × 10 4 L mmol −1 s −1 , respectively. CONCLUSION CALB@ADS-17 showed good esterification performance and exhibited good selectivity towards TAG generation. In addition, CALB@ADS-17 exhibited good reusability in esterification reactions and has potential in practical applications. © 2025 Society of Chemical Industry.

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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2026 · IF 6.7

Highly Stereoselective Synthesis of the Chiral Fungicide’s Intermediate (R)-N-(2,6-Dimethylphenyl) Aminopropionic Acid Methyl Ester via an Esterase-Lipase Cascade

Xinjun Yu,Zhaoxia Qian,Zhichao Tu,Mingpeng Zhou,Yuxiang Sun,Xin Liu,Zhao Wang,Yinjun Zhang

(R)-N-(2,6-dimethylphenyl) aminopropionic acid methyl ester ((R)-DMPM) is a key chiral intermediate for the fungicide N-(2,6-Dimethylphenyl)-N-(methoxyacetyl)-alanine methyl ester ((R)-Metalaxyl). The biological function of the (R)-Metalaxyl is heavily dependent on its R-configuration, however, conventional chemical or single-esterase esterification for (R)-DMPM production induces severe racemization, dramatically compromising the optical purity and the efficacy of (R)-metalaxyl. In this study, a novel dual-enzyme cascade immobilized on polystyrene resin, combining the esterase PAE from Pseudochrobactrum asaccharolyticum WZZ003 for stereoselective hydrolysis of the substate (R,S)-(DMPM) to produce (S)-DMPM and (R)-MAP-acid, and the Novozym 435 for transmethylation of (R)-MAP-acid to produce (R)-DMPM, was applied. After a systematic optimization of dual-enzyme catalysis, the highest optical purity of (R)-DMPM ever reported with an e.e.p of 99.1% and an E value of 900 was obtained under the 49.2% conversion of (R,S)-DMPM and 96.2% of esterification yield conditions. The results overcome the limitations of racemization and provides a green, high-yield route for the industrial production of (R)-DMPM.

CAS / MDL: 681-84-5 9002-98-6
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FOOD CHEMISTRY · 2026 · IF 10.4

Plant small molecules steer lipase selectivity and free fatty acid profiles in enzyme-modified cheese revealed by machine learning–guided analysis

Xiao Tan,Huijin Liu,Qingqing Liu,Dan Hu,Junling Cui,Wushuang Bai,Martin Gand,Binglin Li

Mint and cumin extracts regulate lipase activity in enzyme-modified cheese. • Epicatechin and 7-hydroxycoumarin promote medium-chain FFAs, suppress long-chains. • Molecular simulations reveal selective inhibition of long-chain triglyceride binding. • Sensory analysis confirms enhanced aroma, reduced off-flavors in modified cheeses. • Plant-derived compounds offer a novel approach to optimizing cheese flavor. In enzyme-modified cheese (EMC), controlling the release of specific free fatty acids (FFAs) by lipases remains challenging. Eight plant extracts were screened, and Mentha haplocalyx and Cuminum cyminum showed pronounced regulatory effects on lipolysis. These extracts were further fractionated, purified, and identified. This study demonstrates that epicatechin and 7-hydroxycoumarin can selectively modulate lipase-mediated fatty acid release, promoting the accumulation of aroma-active medium-chain free fatty acids while suppressing long-chain fatty acid release during EMC production. The results revealed a concentration-dependent, bidirectional “pendulum effect,” where changing additive levels shifted lipase selectivity and apparent activity, enabling tunable FFA profiles. Sensory evaluation confirmed the chemical data, identifying one desirable-aroma EMC and two low off-flavor EMCs. Integrated AlphaFold3 modelling, molecular dynamics, docking, machine-learning analyses, and kinetic experiments firstly provided molecular-level insights into the mechanisms underlying the promotion of medium-chain fatty acid release and the suppression of long-chain fatty acid liberation during EMC production. Download: Download high-res image (183KB) Download: Download full-size image

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