ENZYME AND MICROBIAL TECHNOLOGY
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2017
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IF 2.502
Shuguang Wang,Debing Zheng,Lingyu Yin,Fei Wang
Cross-linked enzyme aggregates (CLEAs) have emerged as an interesting biocatalyst design for enzyme immobilization. However, the commercialization of CLEAs is often hampered by their shortcomings, such as poor-controlled particle size, low activity and sticky characteristic. In order to overcome these drawbacks, five nanoparticles (NPs) (nano-TiO 2 , nano-MgO, nano-Ni, nano-Cu and nano-Fe 3 O 4 ) were used to improve CLEAs activity and structure in this study. Results showed that moderate dosage of nano-TiO 2 addition increased CLEAs activity, and the most increment was 15.2% relative to CLEAs without NPs. This was possibly due to more channels and smaller size particle of CLEAs after nano-TiO 2 addition. Moreover, nano-TiO 2 addition not only decreased fluorescence intensity but also caused the red shift in tryptophan (Trp) and tyrosine (Typ) residues. Nano-TiO 2 addition decreased K m and increased V max of CLEAs. These changes were benefit to the activity and structure of CLEAs. However, addition of other four NPs (nano-MgO, nano-Ni, nano-Cu and nano-Fe 3 O 4 ) did not increase CLEAs activity and even decrease CLEAs activity due to less amorphous cavities and larger or discrete particle size than CLEAs without NPs. In addition, FT-IR results showed that NPs addition increases the content of regular structure of CLEAs, and causes a partial transformation of β-turn into β-sheet. This study showed that it was potential to improve CLEAs performance by nano-TiO 2 addition.
研究领域:
生物化学
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酶工程
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产品关联
DOI
PubMed
高影响因子
Scientific Reports
·
2015
·Vol. 5
·期 1
·1-13
·
IF 5.578
Cui Jiandong,Jia Shiru,Liang Longhao,Zhao Yamin,Feng Yuxiao
A novel enzyme immobilization approach was used to generate mesoporous enzymes-silica composite microparticles by co-entrapping gelatinized starch and cross-linked phenylalanine ammonia lyase (PAL) aggregates (CLEAs) containing gelatinized starch into biomemitic silica and subsequently removing the starch by α-amylase treatment. During the preparation process, the gelatinzed starch served as a pore-forming agent to create pores in CLEAs and biomimetic silica. The resulting mesoporous CLEAs-silica composite microparticles exhibited higher activity and stability than native PAL, conventional CLEAs and PAL encapsulated in biomimetic silica. Furthermore, the mesoporous CLEAs-silica composite microparticles displayed good reusability due to its suitable size and mechanical properties and had excellent stability for storage. The superior catalytic performances were attributed to the combinational unique structure from the intra-cross-linking among enzyme aggregates and hard mesoporous silica shell, which not only decreased the enzyme-support negative interaction and mass-transfer limitations, but also improved the mechanical properties and monodispersity. This approach will be highly beneficial for preparing various bioactive mesoporous composites with excellent catalytic performance.
研究领域:
生物化学
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材料科学
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DOI
PubMed
高影响因子
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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2015
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IF 2.128
Wei-Wei Zhang,Xian-Ling Yang,Jun-Qi Jia,Na Wang,Cheng-Li Hu,Xiao-Qi Yu
Novel surfactant-activated magnetic cross-linked enzyme aggregates of Thermomyces lanuginosus lipase (TLL-magnetic-CLEAs) were developed and provided an efficient approach to improve the activity and stability of lipase for biodiesel production. In the methanolysis of Jatropha oil for biodiesel synthesis, the maximum yield in isopropyl ether was 88% after 48 h at 40 °C, representing 3.5-fold and 2.5-fold higher activity than that exhibited by free TLL and TLL CLEAs, respectively. Moreover, Tween 80-activated TLL-magnetic-CLEAs retained their activity during storage at 4 °C for 11 weeks and 10 cycles of repeated 48 h biodiesel reactions at 40 °C (over 30 days). Additionally, the surface morphology, particle size and loading of lipase aggregates were confirmed by Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM). The combination of interfacial activation, high specific enzyme activity, improved stability and easy recovery of magnetic CLEAs presents an attractive process for lipase immobilization and provides a promising catalyst for biodiesel production.
研究领域:
生物化学
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可再生能源
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酶工程
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产品关联
DOI
高影响因子
CHEMICAL ENGINEERING JOURNAL
·
2025
·
IF 13.2
Danqing Shen,Qian Du,Pan Wang,Yongquan Zhou,Jianming Pan
The continuous phase films in high internal phase emulsions (HIPEs), which seems to be a microchannel-like space, are benefit for confined synthesis of ultrafine adsorbent. Herein, switchable and microchannel-like space in the continuous phase of oil-in-water HIPEs is developed for fabricating ultrafine ZrO 2 anchoring cross-linked enzyme aggregates (CLEAs-ZrO 2 ), and then as-prepared composites were applied as defluoridation adsorbent. Bis(3-aminopropyl)tetramethyldisiloxane oleic acid surfactant (BTOA) can realize reversible emulsification and demulsification in response to CO 2 /N 2 switch, endowing with simple collection of products and continuous preparation. This confinement effect is expected of resulting in a 28 % increase in adsorption capacity and 33 % reduction in synthesis time. In addition, the adsorption capacity of CLEAs-ZrO 2 is nearly 4.2 times higher than that of commercially available defluoridants. In fluorine-containing industrial wastewater, the removal efficiency of fluoride ion (F - ) reaches 93 %, and the corresponding partition coefficients ( K d ) achieves the value of 31.1 L g −1 . By analyzing with XPS spectra and in-situ FT-IR spectroscopy, a strong Zr-F bonding interaction between CLEAs-ZrO 2 and F - in the solution boosts this specific adsorption. This work presents a novel method for constructing switchable confinement system, but also offers a promising defluoridation adsorbent for industrial effluents.
研究领域:
环境科学
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材料科学
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产品关联
DOI
高影响因子
JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY
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2016
·Vol. 92
·期 7
·1785-1793
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IF 2.738
Jiandong Cui,Tao Lin,Yuxiao Feng,Zhilei Tan,Shiru Jia
BACKGROUND Cross-linking enzyme aggregates (CLEAs) seem to be a promising immobilization method due to mild processing conditions and short preparation time. However, the CLEAs prepared in aqueous solution exhibit amorphous large clusters that cause significant mass-transfer limitations, leading to low catalytic efficiency. In this work, novel spherical CLEAs of lipase from bovine pancreas (spherical CLEAs) were prepared within droplets dispersed in a water-in-hydrophobic ionic liquid microemulsion rather than a conventional aqueous solution. The properties of the spherical CLEAs were determined. RESULTS The resultant CLEAs exhibited spherical structure with good monodispersity instead of the amorphous clusters of conventional CLEAs, and showed higher activity recovery (84.6%) than that of conventional CLEAs (52.8%). The high activity recovery of spherical CLEAs could be attributed to both interfacial activation of the microemulsion system and the well-defined structure of the spherical CLEAs, which not only activated lipases in an active form, but also decreased mass-transfer limitations. Moreover, the thermostability, storage stability, tolerance against hydrophilic solvents, and mechanical stability of the spherical CLEAs were enhanced significantly. The spherical CLEAs evidenced excellent reusability in comparison with conventional CLEAs. CONCLUSIONS The novel strategy in this study might open an attractive way towards effectively improving the catalytic properties of traditional CLEAs. © 2016 Society of Chemical Industry
研究领域:
生物化学
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酶工程
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材料科学
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产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2025
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IF 8.5
Xiang Zhou,Jiahao Xu,Jiayao Sun,Hao Chen,Dechun Huang,Wei Chen,Hongliang Qian
1,3-Dioleoyl-2-palmitoylglycerol (OPO) is crucial for infant nutrition; however, conventional immobilized lipase requires high-purity enzymes, which increases costs and limits industrial scalability. Herein, Rhizomucor miehei lipase (RML) was immobilized on surface-modified magnetic nanoparticles using cross-linked enzyme aggregates (CLEAs) technology to produce Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs. This approach combines the separation and immobilization of enzymes, allowing for the use of lower-purity lipase, which enhances its suitability for industrial-scale processes. The optimized Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs exhibited excellent thermal, pH, and storage stability. The performance of Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs was evaluated by catalyzing the synthesis of OPO through the enzymatic hydrolysis of glycerol tripalmitate (PPP) and oleic acid (OA). Under optimal conditions, the OPO content in products reached 63.33 ± 0.30%, highlighting the high efficiency of the enzymatic process. After eight reuse cycles, the Fe 3 O 4 @SiO 2 @TPOAC@RML CLEAs retained around 75% of their relative activity. Therefore, this strategy of lipase immobilization using CLEA technology, coupled with magnetic nanoparticles, offers a promising approach for OPO synthesis.
研究领域:
生物催化
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纳米技术
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酶固定化
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食品化学
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工业生物技术
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
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2026
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IF 10.4
Tong Sun,Wenyue Sun,Shutong Lin,Yan Liu,Lili Lu
α-Galactosidases with high activity and stability are crucial for industrial applications, such as the hydrolysis of raffinose family oligosaccharides (RFOs) in soymilk. In this study, four novel cross-linkers, including dimethyl pimelimidate (DMP), dimethyl suberimidate (DMS), bis(sulfosuccinimidyl)suberate (BS 3 ), and bis- N -succinimidyl-(pentaethylene glycol) ester [BS(PEG) 5 ], were first applied to directly cross-link active α-galactosidase inclusion bodies. This simple approach generated stable and recyclable cross-linked enzyme aggregates (CLEAs) without precipitation or the need for carrier matrices. The resulting CLEAs showed 95–100% activity recovery, far exceeding that of glutaraldehyde (45%). All CLEAs exhibited broad pH and thermal stability, holding over 94% of their initial activity after 10 batches for RFOs hydrolysis in soymilk. Specifically, DMS-CLEAs maintained nearly 100% hydrolysis efficiency throughout 10 cycles. CLEAs prepared with the short-arm cross-linkers demonstrated superior enzyme activity recovery compared to those formed with the long-arm ones. These findings highlight the potential of α-galactosidase CLEAs for legume-based food processing.
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DOI
PubMed
高影响因子
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