BIOPROCESS AND BIOSYSTEMS ENGINEERING
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2018
·Vol. 41
·期 5
·739-748
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IF 2.139
Jiaojiao Xia,Bin Zou,Gangbin Zhu,Ping Wei,Zhenjiang Liu
To promote the activity and stability of immobilized porcine pancreatic lipase (PPL), novel carrier was combined with special immobilization method. Enzymatic activity was enhanced after immobilized onto ionic liquid modified magnetic Fe 3 O 4 by electrostatic adsorption. Activity of immobilized enzyme (PPL-IM/BF 4 -Fe 3 O 4 @CA) reached 596 U/g PPL. Through the combination of electrostatic adsorption and embedding immobilization methods, we improve binding force between the carrier and enzyme, and further enhance the efficiency and stability of immobilized enzyme. The activity of PPL-IM/BF 4 -Fe 3 O 4 @CA after repeated third use was 78%. After storage at room temperature for 5 days, the residual activity was 89%. Enzymatic properties and catalytic kinetics of immobilized enzymes were studied, and the effect mechanism of ionic liquid modified Fe 3 O 4 on PPL was revealed. The effect of ionic liquid on the carrier structure was investigated by characterization of XRD, FT-IR, SEM and TG. The mechanism and enzymatic properties of immobilized PPL via electrostatic adsorption and embedding were analyzed. A novel and efficient immobilized PPL was developed.
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RSC Advances
·
2018
·Vol. 8
·期 29
·16088-16094
·
IF 2.936
Jianyun Yu,Chenhui Wang,Anming Wang,Ningning Li,Xinxin Chen,Xiaolin Pei,Pengfei Zhang,Stephen Gang Wu
To achieve dual-reuse of both enzyme and support in enzyme immobilization, hybrid nanoflowers (hNFs) were synthesized and crystallized in aqueous solution using calcium phosphate as inorganic component and enzyme as organic component. When hNFs lost their catalytic activity after reuse for times, they underwent dissolution and recrystallization to achieve the dual-cycle of enzyme and support. Six enzymes including papain, bromelain, trypsin, Lipase from Porcine Pancreas (PPL), Lipase from Thermomyces lanuginosus (TLL) and Lipase B from Candida antarctica (CALB) were chose as model enzymes and the obtained hNFs all presented high catalytic activity and thermal stability. The highest catalytic efficiency (Kcat/Km) of TLL-hNFs was 38.52 mM−1 s−1, 21.7 folds than that of free enzyme. Moreover, after heating for 6 h at 70 °C, the residual activities of TLL-hNFs, PPL-hNFs, and CALB-hNFs, were 78.3%, 72.9% and 84.3%, which were 4.57, 2.61 2.35 folds of that of their corresponding free one. Furthermore, the recovery rate of Ca3(PO4)2 were above 95% by recrystallizing the calcium phosphate with fresh enzymes after dissolving the used hNFs and removing the denatured enzyme. The recrystallized hNFs using the recovered phosphate salts and fresh enzymes all gave the consistent catalytic activities. This sustainable dual-cycle method depending on calcium phosphate crystallization, dissolution and recrystallization, was facile and efficient and can also be applied to other enzymes immobilization for industrial biocatalysis.
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APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
·
2017
·Vol. 185
·期 3
·606-618
·
IF 1.751
Zou Bin,Chu Yanhong,Xia Jiaojiao,Chen Xueshan,Huo Shuhao
Porcine pancreatic lipase (PPL) was immobilized onto functionalized ionic liquid-modified silica carrier using gelatinization and physical adsorption. The immobilized lipase was characterized with N 2 adsorption–desorption, X-ray diffraction (XRD), scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FT-IR) before and after modification and immobilization. The results showed that the modification of the ionic liquid and the introduction of lipase had been successfully approved. The rate of enzymatic reaction and its influencing factors was primarily studied by enzymatic reaction kinetics. K
m values of PPL-SiO 2 @CA and PPL-IM/BF 4 -SiO 2 @CA were 4.9 and 3.7 mg/ml, respectively. It indicated that the modification of the functionalized ionic liquid enhanced the affinity between the immobilized enzyme and the substrate. The immobilization efficiency, specific activity, optimum temperature, optimum pH, thermal stability, reusability, and storage stability of the immobilized enzyme were investigated. We found that the stability of the immobilized enzyme was significantly higher than that of the unmodified immobilized enzyme. Specially, PPL-IM/BF 4 -SiO 2 @CA maintained good thermal stability and retained more than 92% of its activity at 65 °C after preheating 3 h.
Above, the immobilized lipase maintained more than 92% of its initial activity after incubating at 65 °C for 3 h.
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CHEMISTRY-A EUROPEAN JOURNAL
·
2017
·Vol. 23
·期 58
·14614-14622
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IF 5.317
Jing Du,Mei-Da Cao,Shu-Li Feng,Fang Su,Xiao-Jing Sang,Lan-Cui Zhang,Wan-Sheng You,Mei Yang,Zai-Ming Zhu
Graphical Pinning down catalysts : Two new Preyssler-type polyoxometalate-based coordination polymers were synthesized and applied to immobilize horseradish peroxidase (HRP). These polymers exhibited higher enzyme loading, required a shorter loading time, and exhibited excellent reusability (see figure). Enzyme immobilization is of increasing importance for biocatalysis, for which good supports are critical. Herein, two new Preyssler-type polyoxometalate (POM)-based coordination polymers, namely, {[Cu(H 2 biim) 2 ][{Cu(H 2 biim) 2 (μ-H 2 O)} 2 Cu(H 2 biim)(H 2 O) 2 ]H[({Cu(H 2 biim)(H 2 O) 2 } 0.5 ) 2 ((μ-C 3 HN 2 Cl 2 ){Cu(H 2 biim)} 2 ){Z(H 2 O)P 5 W 30 O 110 }] ⋅ x H 2 O} n ( 1 : Z=Na, x= 9; 2 : Z=Ag, x= 10; H 2 biim=2,2′-biimidazole) were designed and synthesized. Compounds 1 and 2 exhibit the same skeletons, which contain multiple Cu II complex fragments and penta-supported {ZP 5 W 30 } (Z=Na, Ag) clusters. They were first employed to immobilize horseradish peroxidase (HRP). Results show that compounds 1 and 2 are good supports for HRP immobilization, and exhibit higher enzyme loading, lower loading times, and excellent reusability. The immobilized HRP (HRP/ 1 or HRP/ 2 ) was further applied to detect H 2 O 2 , and good sensitivity, wide linear range, low detection limit, and fast response were achieved. This work shows that POM-based hybrid materials are a new kind of promising support for enzyme immobilization.
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PROCESS BIOCHEMISTRY
·
2017
·
IF 2.497
Zhen Gao,Jianlin Chu,Tianyue Jiang,Tingting Xu,Bin Wu,Bingfang He
According to the purification characteristics of lipase from Burkholderia ambifaria YCJ01, mesoporous TiO 2 was functionalized by phenylaminopropyl trimethoxysilane (Ph-TiO 2 ) for lipase immobilization. This support permitted one step immobilization and purification of lipase YCJ01 via hydrophobic interactions from crude fermentation supernatant. The activity of immobilized lipase was 6119.2 U/g support with 12.8 mg/g support of enzyme loading. The ratio of the activity of immobilized lipase to decrease activity in the supernatant after immobilization reached 2.2, which indicated that the immobilized lipase molecules exhibited a dramatic hyperactivation. In comparison with free lipase, immobilized lipase showed significantly improved pH stability and thermalstability. The Ph-TiO 2 /YCJ01 biocomposite was analyzed by scanning electron microscopy, Fourier transform infrared spectroscopy and thermogravimetric analysis . The result indicated lipase was efficiently immobilized on Ph-TiO 2 surface. Finally, the research about cinnamyl acetate synthesis suggested that Ph-TiO 2 /YCJ01 had enhanced catalytic efficiency compared with free lipase. In solvent free medium, the yield of 96.9% was obtained after one operation, and maintained more than 80% of yield after ten reaction cycles.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2023
·
IF 8.2
Lixi Cai,Yanqi Gao,Yunmeng Chu,Yuanqing Lin,Lixing Liu,Guangya Zhang
Tailoring magnetic nanocarriers with tunable properties is of great significance for the development of multifunctional candidate materials in numerous fields. Herein, we report a one-pot biomimetic silicification-based method for the synthesis of silica-coated magnetic nanoparticles. The synthesis process was mild, low cost, and highly efficient, which took only about 21 min compared with 4.5–120 h in other literature. Then, the carriers had been characterized by VSM, SEM, TEM , XRD, FT-IR, and EDS to confirm their function. To evaluate the usefulness of the carriers, they were adopted to couple the purification and immobilization of β-1,3-xylanase from the cell lysate in a single step with high immobilization yield (92.8 %) and high activity recovery (82.4 %). The immobilized enzyme also retained 58.4 % of the initial activity after 10 cycles and displayed good storage properties, and improved thermal stability , which would be promising in algae biomass bioconversion as well as other diverse applications.
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Plasma Processes and Polymers
·
2023
·Vol. 20
·期 5
·2200228
·
IF 3.5
Siyuan Sui,Hongmei Sun,Guohua Ni,Yafeng Liu,Huan Zheng,Tao Sun,Ling Kong,Zhongyang Ma,Fangli Yuan
The surface of polytetrafluoroethylene (PTFE) is activated by argon (Ar), Ar mixed with water vapor (Ar-H 2 O), and a mixture of Ar, water vapor, and ammonia (Ar-H 2 O-NH 3 ) plasmas and then grafted onto polymerized dopamine/ethylene imine and immobilized heparin. Oxygen-containing functional groups are all introduced onto the PTFE surface treated by three types of plasma. The amount of oxygen grafted is the highest in samples treated with Ar-H 2 O-NH 3 plasma compared to that treated with Ar-H 2 O plasma. An increase in the content of oxygen grafted onto PTFE contributes to an increase in the thickness and cross-linking bond of the polymeric interlayer and then raises the density of the heparin coating. The thickness of the polydopamine/polyethylenimide intermediate layer on the surface of PTFE treated with Ar-H 2 O-NH 3 plasma is 4.8 ± 0.3 μm, and the density of the immobilized heparin coating was 95 μg/cm 2 .
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JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY
·
2022
·Vol. 98
·期 4
·919-931
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IF 3.709
Bixiu Song,Dajun Ren,Zhaobo Wang,Yongwei Huang,Xiaoqing Zhang,Shuqin Zhang,Xiangyi Gong,Wangsheng Chen
As a result of the poor mechanical properties of most metal–organic frameworks (MOFs), they are liable to dissociate in water and thus cannot maintain immobilized enzyme activity. In this paper, a magnetic porous carbon material (Fe-Cu-MPC) with good stability was prepared by high temperature carbonization using a bimetallic Fe-Cu-MOF precursor, and used to immobilize laccase by a simple and rapid adsorption-crosslinking method. Optimized by the response surface method, optimal conditions for the immobilization of laccase on Fe-Cu-MPC were obtained as follows: enzyme concentration 1.275 mg mL −1 , immobilization time 32 min, and pH 4.7. Under the optimal preparation conditions, the activity of the immobilized laccase obtained was 0.63 U mg −1 , with activity recovery of 63.13%. The enzyme loading was 189.03 mg g −1 and the immobilization yield was 74.13%. Compared with free laccase, Fe-Cu-MPC@Lac showed stronger tolerance to temperature and pH, and had better thermal stability and storage stability. The removal of BPA by immobilized laccase was studied, showing that the removal effect of Fe-Cu-MPC@Lac on BPA was much higher than that of free laccase. Within 5 h, the BPA removal amount of Fe-Cu-MPC@Lac (0.34 mmol g −1 ) was two-fold that of free laccase (0.14 mmol g −1 ), and the BPA removal rate reached 41.35% after ten cycles. Finally, based on the intermediates identified by gas chromatography–mass spectrometry, two possible degradation pathways of BPA were proposed. Studies have shown that Fe-Cu-MPC is an excellent carrier and Fe-Cu-MPC@Lac has great potential in the treatment of BPA containing wastewater. © 2022 Society of Chemical Industry (SCI).
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ACS Sustainable Chemistry & Engineering
·
2023
·
IF 8.4
Guanjia Yang,Jialing Wang,Wenming Shao,Shimeng Wang,Bin Wu,Bingbing Gao,Bingfang He
Conventional enzyme immobilization approaches can only immobilize certain specific enzymes with poor generality. Attempts to improve the universality of enzyme types tend to impart them with more enzymatic catalysis applications. Here, inspired by mussel adhesive proteins, we present a novel eco-friendly surface carrier that was 3D printed and modified by electro-oxidation for enzyme immobilization. The carrier was fabricated through 3D printing by transforming acrylonitrile butadiene styrene (ABS) material into a suitable structure (3DABS). Then, electro-oxidative modification was performed on the surface to form a polydopamine (PDA) coating (3DABS-PDA). The desired structures for the enzyme immobilization carriers were obtained through 3D printing technology, while electro-oxidation modification of the surface provided numerous and firmly covalent binding sites. Based on these features, we have demonstrated that 3D printed and electro-oxidation-modified carriers could be applied to immobilize different types of enzymes. The loading capacity of all immobilized enzymes (galV, EG5C-1, XynLK9, and kdcA) exceeded 25 mg·g–1 (37.7 mg·g–1 for galV), and after 10 reuse cycles, the substrate conversion rate of 3DABS-PDA@galV was still over 85%. The carriers can be reused after simple processing. These results indicate that 3DABS-PDA provides an efficient, sustainable, and versatile approach for enzyme immobilization and exhibits excellent value in various enzymatic catalysis applications.
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BIOTECHNOLOGY AND BIOENGINEERING
·
2022
·Vol. 120
·期 2
·352-398
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IF 4.395
Shalu Aggarwal,Saiqa Ikram
Immobilization depicts a propitious route to optimize the catalytic performances, efficient recovery, minimizing autocatalysis, and also augment the stabilities of enzymes, particularly in unnatural environments. In this opinion, supramolecules and multimolecular frameworks have captivated immense attention to achieve profound controllable interactions between enzyme molecules and well-defined natural or synthetic architectures to yield protein bioconjugates with high accessibility for substrate binding and enhanced enantioselectivities. This scholastic review emphasizes the possibilities of associating multimolecular complexes with biological entities via several types of interactions, namely covalent interactions, host–guest complexation, π − π ${\rm{\pi }}-{\rm{\pi }}$ interactions, intra/inter hydrogen bondings, electrostatic interactions, and so forth offers remarkable applications for the modulations of enzymes. The potential synergies between artificial supramolecular structures and biological systems are the primary concern of this pedagogical review. The majority of the research primarily focused on the dynamic biomolecule-responsive supramolecular assemblages and multimolecular architectures as ideal platforms for the recognition and modulation of proteins and cells. Embracing sustainable green demeanors of enzyme immobilizations in a quest to reinforce site-selectivity, catalytic efficiency, and structural integrality of enzymes are the contemporary requirements of the biotechnological sectors that instigate the development of novel biocatalytic systems.
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LANGMUIR
·
2022
·
IF 4.331
Liang Sun,Haoya Han,Zhiyong Liu,Zhinan Fu,Chen Hua,Enguang Ma,Jiangtao Guo,Jichang Liu,Li Li,Bo Fang,Xuhong Guo
Nanosized gold nanoparticles (AuNPs) are of great interest in areas such as catalysts or imaging but are easy to aggregate due to high surface activity. To stabilize AuNPs, two approaches were employed to immobilize AuNPs in spherical polymer brushes (SPBs), namely, the in situ preparation of AuNPs within the brush layer of SPBs and external addition of preprepared citrate-capped AuNPs. The distribution and stability of AuNPs in SPBs were studied by small-angle X-ray scattering (SAXS). SAXS results demonstrated that the in situ-prepared AuNPs were mainly located on the inner layer and their amount decreased from inside to outside. In the case of external addition of preprepared AuNPs, the cationic SPB showed obvious immobilization, while almost no AuNPs were immobilized in the anionic SPB. The stable immobilization of the AuNPs in SPBs was the result of multiple interactions including complexation and electrostatic interaction. SAXS was validated to be a distinctive and powerful characterization method to provide theoretical guidance for the stable immobilization of AuNPs.
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Journal of Oleo Science
·
2022
·
IF 1.628
Wenyi Chen,Maomao Kou,Lin Li,Bing Li,Jianrong Huang,Shudong Fan,Li Xu,Nanjing Zhong
In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase® Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition of phospholipids in the gum, of the immobilized LU samples, were carefully studied. Hydrolysis activities over 1800 U/g were obtained from all the immobilized LU samples. The highest activity of up to 4554.17 U/g was observed from the 3-ureidopropyl group-modified SBA-15-supported LU. Most of the immobilized LU samples removed the phospholipids effectively from crude soybean oil (initial phosphorous content 314.23 mg/kg), with a residual phosphorus content of less than 10 mg/kg. The reusability of the immobilized LU samples in the degumming process was evaluated. No loss of activity was observed from the methyl and N-(2-aminoethyl)-3-aminopropyl group-modified SBA-15-supported LU samples after five cycles of reuse. In addition, 3-aminopropyl and 3-glycidyloxypropyl group-modified SBA-15-supported LU samples retained over 90% of their initial activity; N-phenylaminomethyl and 1-isocyanatopropane group-functionalized SBA-15-supported LU samples retained approximately 80% of their initial activity. The phospholipids in the gum were analyzed. The n-octadecyl and N-(2-aminoethyl)-3-aminopropyl group-functionalized SBA-15-supported LU samples were selective for lysophosphatidylethanolamine (LPE) preparation, and LPE percentages up to 37.14 and 38.80% were obtained, respectively. The N-phenylaminomethyl group-modified SBA-15-supported LU showed selectivity toward lysophosphatidylcholine (LPC) production, with an LPC percentage of up to 38.5%.
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