ACS Materials Au
·
2026
·
IF 9.1
Yuhan Li,Zhuoyang Du,Yongheng Shi,Zeqing Liu,Lingmei Dai,Dehua Liu,Wei Du
Enzyme immobilization on solid supports enhances stability and reusability, yet nanoscale carriers such as metal–organic frameworks (MOFs) still face challenges in efficient recovery. While pyrolysis can magnetize Fe-MOFs, conventional methods often compromise either enzyme activity or structural integrity. This study presents a rational two-step oxidation–reduction (O–R) pyrolysis strategy to convert Meso-MIL-88A into a magnetically recyclable, mesoporous biocatalyst support (O-R500). Unlike one-step carbonization, which generates enzyme-incompatible Fe3O4, or carbonization-oxidation routes that collapse the framework, our approach first transforms the MOF into a robust α-Fe2O3 template while preserving its morphology. Citric acid then acts as a mild, slow-releasing reductant, selectively producing a γ-Fe2O3-rich phase without damaging the mesostructure. The resulting O-R500 exhibits well-defined mesopores (∼13 nm), sufficient magnetization (16 emu/g) for rapid separation, and a biocompatible surface that maintains the native conformation of immobilized Candida antarctica lipase B (CalB). In the synthesis of phosphatidyl EPA/DHA, CalB@O-R500 achieved 84.5% incorporation and retained 90.3% activity over five cycles, outperforming nonmagnetic counterparts. This work not only provides a high-performance magnetic biocatalyst but also establishes a generalizable design principle for converting Fe-MOFs into structured, biocompatible, and functionally integrated carriers.
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BIOCATALYSIS AND BIOTRANSFORMATION
·
2021
·
IF 2.181
Hongqian Dai,Yuan Lu,Hanbing Shi,Lan Tang,Xingyuan Sun,Zhimin Ou
Fe3O4 magnetic nanoparticles were prepared by chemical co-precipitation and modified with 3-aminopropyltriethoxysilane (APTES) and CS2 to form Fe3O4-APTES-CS2 magnetic carriers. Magnetically immobilized enzymes are attractive owing to their potential applications in many biological fields. When an alternating magnetic field is applied, the magnetic nanoparticles experience a force in the direction of the field, and the magnetic moments of the magnetic nanoparticles are apt to align in the direction of the field. Thus, magnetic nanoparticles behave like microscopic stirrers. The optimal reaction conditions of the acylation reaction using Fe3O4-APTES-CS2-lipase were 200 mmol/L 1-methyl-3-amphetamine, 100 mg immobilized lipase, 200 μL ethyl acetate, 12.6 × g rotating speed, 40 °C, and 5 days in the shaker. The conversion and enantiomeric excess of R-2a reached a maximum of 36.8% and 98.5%, respectively. 1-Methyl-3-phenylpropylamine was resolved using Fe3O4-APTES-CS2-lipase in an alternating magnetic field. The optimal magnetic field frequency and magnetic field intensity were determined to be 500 Hz and 12 Gs, respectively. The conversion and enantiomeric excess of R-2a reached a maximum of 40.3% and 98.5%, respectively. The results revealed that conversion under a magnetic field was significantly higher than that without a magnetic field. Highly optically active (R)-N-acetyl-1-methyl-3-amphetamine can be obtained via an efficient resolution of racemic 1-methyl-3-phenylpropylamine with immobilized lipase magnetic nanoparticles as a catalyst and ethyl acetate as an acyl donor in organic solvents in an alternating magnetic field.
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FOOD HYDROCOLLOIDS
·
2022
·
IF 11.504
Na Zhang,Xue Han,Rumeng Yu,Xiaomin Tang,Bo Zhang,Yanyan Zhang,Xiaoyu Yin,Wenrui Ni,Mengze Wang,Bolin Zhang,Junfeng Fan
A bile salt (BS)-stabilized water/oil interface is a prerequisite for the pancreas lipase (PL) mediated hydrolyzation of triacylglycerol. Previous fat digestion research mainly focused on direct lipase inhibition by bioactive substances while ignoring the destructive role of these substances on BS-stabilized lipid emulsions . Here, we showed that polysaccharides (LP) weakly suppressed PL but destroyed BS-stabilized emulsions and thus inhibited free fatty acid (FFA) release. Physicochemical analysis showed that LP actions toward emulsion stability were mainly due to endogenous minerals (28%) in LP which affected aggregation and amphiphilic properties of BS-polysaccharide composites. This was evidenced by high wettability and low interfacial tension in demineralized polysaccharide and BS composites, with three phase contact angles which were identified as 80.4° and 95.6° as well as interfacial tensions as 9.26 and 9.37 mN/m, respectively. However, the low wettability, which was detected as 76.2° and 78.6° as well as high interfacial tension as 10.77 and 11.02 mN/m, respectively, was only observed in mineral-containing polysaccharides and BS composites. Further investigations showed that interactions with mineral-containing polysaccharides occupied hydrophobic sites in BS thereby elevating composite hydrophilicity. These findings provided novel insights into the effects of plant-sourced polysaccharides on fat digestion from an interface chemistry perspective, and in particular, they deepened our understanding of polysaccharide interactions with intestine-secreted lipid digestants.
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Gels
·
2022
·Vol. 8
·期 12
·812
·
IF 4.432
Ziheng Wang,Shumiao Lin,Qianqian Zhang,Jinlong Li,Sheng Yin
Efficient lipase catalysis requires sufficient oil–water interface engineered through structural design. Inspired by the architectural features of fabrics, a novel lipase-membrane catalytic system with interwoven polyacrylic acid (PAA) gel fibers and polyvinyl pyrrolidone (PVP) gel fibers was developed in this study by using double-needle electrospinning and gelation. It has been demonstrated that PAA/PVP hybrid gel fiber membranes (HGFMs) have a high swelling capacity for both water and oil phases, which created numerous discontinuous oil–water contact surface units in limited space of HGFMs, consequently forming effective interfacial catalytic systems. Volume competition between the water and oil phases suggests that balancing the proportions of these phases is very important for effective construction of oil–water interfaces and conditioning catalysis. Regulation of multiple factors of PAA/PVP HGFMs resulted in a catalytic efficiency of up to 2.1 times that of a macroscopic “oil-up/water-down” system (room temperature, pH = 7), and 2.9 times when three membranes are superimposed, as well as excellent pH and temperature stability. HGFMs were stacked to build a high-performing catalytic performance reactor. We expect that this study will be a beneficial exploration for expanding the lipase catalytic system.Keywords:lipase;interfacial catalysis;hybrid gel fiber membrane;double-needle electrospinning
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LWT-FOOD SCIENCE AND TECHNOLOGY
·
2022
·
IF 6.056
Geling Kuang,Yingjie Du,Shihai Lu,Zichen Wang,Zhijin Zhang,Xianwei Fan,Muhammad Bilal,Jiandong Cui,Shiru Jia
Enzymatic hydrolysis of vegetable oils is crucial for its potential application in foods and drugs. However, the poor activity of free lipase hinders the reaction. Herein, inspired by lipase interface activation, a novel [email protected] hybrid biocatalyst with a superior catalytic activity for hydrolysis of vegetable oils was developed though the sol-gel biosilicification approach in the oleic acid/water two-phase system. The resultant [email protected] hybrid biocatalyst exhibited 13.5-fold higher activity than free lipase, and excellent storage stability. After 100 days of storage, the free lipase absolutely loss hydrolytic activity whereas the [email protected] hybrid biocatalyst still retained 197.4% of its initial activity. In particular, hydrolysis yield of soybean oil by the hybrid biocatalyst reached 98.8% within only 4 h, which is the fastest value recorded in the current literature. After 5 consecutive cycles, hydrolysis yield still retained up to 63%. Therefore, this strategy provides a facile and efficient method for preparing lipase hybrid biocatalysts with high hydrolysis activity.
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MICROPOROUS AND MESOPOROUS MATERIALS
·
2021
·
IF 5.455
Jingjing Zhu,Huaqiang Chen,Lan Wang,Engang Fu,Jianping Wu,Qilei Zhang,Lirong Yang,Gang Xu
A composite hollow mesoporous MIL-101@Pd@ZIF-8-30min (HM-MIL@Pd@ZIF-30min) nanocatalyst with hollow core and stable shell was developed in this study. Hollow mesoporous MIL-101(HM-MIL) was hydrothermally synthesized and employed as the supports of Pd nanoparticles by adopting a facile HM-MIL-template strategy to make ZIF-8 crystals uniformly overgrew on HM-MIL-101@Pd microcrystal cores. The obtained core-shell catalyst possessed hollow mesoporous structure, and the shell layer of ZIF-8 had additional advantages of abundant Lewis basic sites for heterogeneous racemization reaction. Compared with unmodified HM-MIL@Pd and solid MIL-101(Cr)@Pd@ZIF-8 (S-MIL@Pd@ZIF-8), HM-MIL@Pd@ZIF-8-30min had higher racemic chemical activity (conv. 99%) and selectivity (sel. R-amide 94%) in one-pot dynamic kinetic resolution (DKR) reaction system of rac -1-phenethylamine. The catalyst showed excellent stability, and the conversion and selectivity reached 95% and 93% respectively after ten catalytic cycles.
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FOOD CHEMISTRY
·
2022
·
IF 9.231
Ruimin Wang,Lu Wang,Lin Zhang,Sitong Wan,Congfa Li,Sixin Liu
This study focused on the relationship between content levels of phytochemicals and the biological activities of noni ( Morinda Citrifolia L.) fruit extracts (NFEs) prepared with traditional solvents and deep eutectic solvents (DESs). The results indicated the total phenolic content in Bet-Gly (Betaine: Glycerol) extracts (11.89 mg GAE/g DW) and total iridoid content in 70% ethanol extracts (26.38 mg CE/g DW) were the highest. A total of 17 compounds were identified and quantified in NFEs. Traditional solvent extracts, except ethyl acetate, exhibited higher antioxidant activities than DESs. Three DES extracts showed higher activities against pancreatic lipase than traditional solvent extracts. Multivariate analysis revealed that the type of extraction solvent exerts a significant influence on the phytochemical compositions and biological activities of NFEs. This study provided valuable information on the efficient extraction of phytochemicals from noni fruits and DESs are promising green solvent for the extraction of bioactive compounds from noni fruits.
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ACS Sustainable Chemistry & Engineering
·
2020
·
IF 7.632
Teng Sun,Zhe Dong,Jing Wang,Feng-Hong Huang,Ming-Ming Zheng
Lipase immobilization processes have the potential to drive large-scale industrial applications through cost savings. Among them, the Pickering emulsion system has recently emerged as an ecofriendly technique for enhanced enzymatic activity. In this study, a novel and facile immobilization of lipase in an ultrasound-assisted Pickering emulsion system was developed. The lipase loading amount and yield was 177.3 mg/g and 41.3%, respectively. In the enzymatic synthesis of four sterol lipoates, the immobilized lipase (UIP-HMSS@CRL) achieved the highest catalytic efficiency (CE) of 6.4 mmol/g·h among the reported methods, which was 9.1-fold higher than that of free lipase and 32.0-fold higher than that of previous methods. UIP-HMSS@CRL performed with much higher Vm and lower Km, indicating the excellent catalytic rate and stronger affinity. Moreover, UIP-HMSS@CRL displayed satisfying thermal stability and recyclability, retaining 88.6% of enzyme activity after 10 cycles. The lipase lid was opened at the oil–water interface by both ultrasound and interfacial synergistic activation effect, which provided easier access to an active site and thus achieved excellent catalytic performance. This ultrasound-assisted interface immobilization would open new opportunities for preparation of high-performance and sustainable biocatalysts.
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Frontiers of Chemical Science and Engineering
·
2020
·Vol. 14
·期 5
·868-879
·
IF 3.552
Shen Jiang-Wei,Cai Xue,Dou Bao-Juan,Qi Feng-Yu,Zhang Xiao-Jian,Liu Zhi-Qiang,Zheng Yu-Guo
A lipase from Sporisorium reilianum SRZ2 (SRL) with 73% amino acid sequence identity to Candida antarctica lipase B (CALB) was cloned and overexpressed in Pichia pastoris . The recombinant SRL showed a preference for short-chain p -nitrophenyl esters. It achieved maximum activity at pH 8.0 and 65°C for p -nitrophenyl hexanoate (C6) with K m and k cat / K m values of 0.14 mmol·L −1 and 1712 min −1 · mmol · L −1 at 30°C, respectively. SRL displayed excellent thermostability and pH stability, retaining more than 79% of its initial activity after incubation at 60°C for 72 h and 75% at pH 3 to 11 for 72 h. It also maintained most of its activity in the presence of inhibitors and detergents except sodium dodecyl sulfate, and it tolerated organic solvents. SRL was covalently immobilized and successfully used for ethyl hexanoate synthesis in cyclohexane or in a solvent-free system with a high conversion yield (> 95%). Furthermore, high conversion yield was also achieved for the synthesis of various short-chain flavor esters when high substrate concentrations of 2 mol · L −1 were applied. This study indicated that a CALB-type lipase from S. reilianum SRZ2 showed great potential in organic ester synthesis.
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RSC Advances
·
2020
·Vol. 10
·期 15
·8949-8957
·
IF 3.119
Huijuan Shangguan,Shan Zhang,Xin Li,Qi Zhou,Jie Shi,Qianchun Deng,Fenghong Huang
Lutein scavenges free radicals and inhibits vision damage caused by photo oxidation, while decomposing easily with light and heat. Its stability and bioavailability can be tremendously improved by lutein ester synthesis. However, green and efficient esterification preparation methods are urgently needed. In this study, which used functionalized graphitic carbon nitride nanosheets (g-C3N4-Ns) as the immobilized carrier, a novel biocatalyst was designed and prepared to accommodate Candida antarctica lipase B (CALB), considerably enhancing the performance. It was characterized by TEM, XRD, FTIR, XPS, TGA, and BET to demonstrate successful preparation and then applied to catalyze esterification between lutein and succinate anhydride in dimethyl formamide (DMF) solvent resulting in a conversion rate up to 92% at 50 °C in 60 h, 34% more than free CALB under the same conditions. We believe this is the highest esterification rate in lutein esters synthesis and it has great potential to facilitate eco-friendly and efficient preparation.
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JOURNAL OF INDUSTRIAL AND ENGINEERING CHEMISTRY
·
2020
·
IF 5.278
Anming Wang,Xinxin Chen,Jianyun Yu,Ningning Li,Huimin Li,Youcheng Yin,Tian Xie,Stephen Gang Wu
To prepare enzyme@Ca 3 (PO 4 ) 2 for environmentally friendly biocatalysis, Ca 2+ and (PO 4 ) 3− were extracted from bone waste by acidification. In the nearly neutralized filtrate, the Ca 2+ and (PO 4 ) 3− formed a Ca 3 (PO 4 ) 2 sediment that crystallized on a template of Thermomyces lanuginosus lipase (TLL) at 4 ℃ for 24 h, producing enzyme@Ca 3 (PO 4 ) 2 -Bone hybrid nanoflowers (hNFs). Clindamycin palmitate was efficiently synthesized by transfer of a palmityl moiety from vinyl palmitate to clindamycin free base using these hNFs as a biocatalyst. At 30 ℃ in petroleum ether (PE) as the solvent, the yield of the TLL hNF-catalyzed reaction was as high as 70.0%. Even at a high temperature (80 ℃), the yield in the hNF-catalyzed reaction was still 52.6%, but no product was detected when using free lipase as the catalyst. Moreover, the hNFs retained 90% of their initial activity after 10 cycles (120 h, 12 h per cycle). This green and sustainable method that utilizes bone waste from food production as the raw source of the inorganic component was facile and efficient, and the system may also be applicable for preparing other enzyme@Ca 3 (PO 4 ) 2 hNFs for industrial applications.
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JOURNAL OF SEPARATION SCIENCE
·
2019
·Vol. 43
·期 5
·1003-1010
·
IF 2.516
Yixia Tang,Wang Li,Yuying Wang,Yuefen Zhang,Yibing Ji
An on-line system for preliminary screening lipase inhibitors from natural products with an immobilized lipase microreactor coupled to capillary electrophoresis was established. In this research, the lipase was anchored on the amino activated capillary inner wall using glutaraldehyde as a homobifunctional linker through Schiff base reaction. The immobilized lipase activity was evaluated by measuring the peak area of the hydrolyzate of p-nitrophenyl acetate. In order to maintain the enzymatic activity of immobilized lipase, the acetonitrile content and the pH of the reaction solution were also optimized. Under the optimized reaction conditions, the Michaelis–Menten constant of the immobilized lipase and the half maximal inhibitory concentration for orlistat were studied, which were consistent with previous literature data. Furthermore, the developed method was applied to screen lipase inhibition activity from ten natural products. As a result, we found that six natural products have inhibitory effect on the activity of lipase, among which the inhibitory effect of Rhizoma atractylodis extract has never been reported before.
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危险品化学品经营许可证（带存储）