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JOURNAL OF APPLIED POLYMER SCIENCE · 2013 ·Vol. 130 ·期 3 ·1498-1502 · IF 1.395

Enhancing the stability of immobilized catalase on activated carbon with gelatin encapsulation

Yulin Wang,Yuepeng Guan,Yin Yang,Peng Yu,Yaqin Huang

Gelatin (Gel) encapsulation onto activated carbon (AC) with catalase (CAT) was developed as an alternative method for CAT immobilization in this study. The immobilized CAT with AC encapsulated by Gel as the supporter accounted for 65.69% of the native enzyme activity. Furthermore, the properties of the immobilized CATs were characterized by Fourier transform infrared spectroscopy and scanning electron microscopy. Among free CAT and the two immobilized CATs, the immobilized CAT with AC encapsulated by Gel as the supporter showed the highest relative enzymatic activity and a high stability in a broad range of pH values and temperatures, and its residual activity was 80% after 15 uses, whereas the immobilized CAT with AC as the supporter was retained at a level of only 50% under the same conditions. © 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 130: 1498–1502, 2013

CAS / MDL: 9001-05-2
研究领域: 生物化学 · 材料科学
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Foods · 2021 ·Vol. 10 ·期 11 ·2797 · IF 4.35

Preparation of Antarctic Krill Oil Emulsion and Its Stability under Catalase Treatment

Zhenxiao Zheng,Kai Zhu,Zhiyuan Dai

Making Antarctic krill oil into emulsion is a good way to utilize Antarctic krill, but proliferation of microorganisms cannot be ignored. H2O2is widely used in the sterilization of liquid food since its decomposition products are environmentally friendly, although residual H2O2should be removed for food safety. Adding catalase (CAT) is an effective means to do this. However, the enzyme activity center of CAT is the iron porphyrin group, which has the risk of accelerating lipid oxidation in the oil emulsion. Therefore, we hypothesized that CAT might not be suitable for the removal of H2O2in Antarctic krill oil emulsion. In this paper, Antarctic krill oil emulsion was prepared, and then the effect of CAT on the emulsion was studied through visual observation, microscopic morphology observation, turbidity and stability, particle size, and ζ-potential; finally, the mechanism of CAT destroying the emulsion was explored from the perspective of lipid oxidation. The results showed that a stable Antarctic krill emulsion was prepared using Tween-80 as the emulsifier, with the oil concentration of 1% (v/v) and the ratio of surfactant to oil phase of 1:5 (v/v). The emulsion treated with CAT had undergone demulsification, stratification, and coagulation after 2 days of incubation, while the emulsion treated with superoxide dismutase (SOD) and bovine serum albumin (BSA) changed little. In addition, the thiobarbituric acid reactive substances (TBARS) value and the content of hydroxyl radicals in the CAT group increased significantly. The preliminary research results indicated that the effect of CAT on the emulsion related to the lipid oxidation caused by the iron porphyrin group at the center of the enzyme activity. All these results indicated that CAT was not suitable for the removal of residual H2O2in Antarctic krill oil emulsion. Moreover, it is helpful to avoid the contact of Antarctic krill oil emulsion and CAT during the processing of the krill.Keywords:Antarctic krill emulsion;catalase;iron porphyrin;lipid oxidation

研究领域: 食品科学 · 生物化学
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BIOTECHNOLOGY AND BIOPROCESS ENGINEERING · 2022 ·Vol. 27 ·期 1 ·135-144 · IF 3.386

Efficient Immobilization of Enzymes on Amino Functionalized MIL-125-NH2 Metal Organic Framework

Wang Zichen,Liu Yang,Li Jinhong,Meng Guoqing,Zhu Daoyu,Cui Jiandong,Jia Shiru

As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH 2 is very low due to small pore size and few amino groups on the surface of the MIL-125-NH 2 . In this work, catalase (CAT) was immobilized on the MIL-125-NH 2 and amino functionalized MIL-125-NH 2 by adsorption (CAT@MIL-125-NH 2 ) and covalent binding (CAT@Amino MIL-125-NH 2 ), respectively. Compared with the CAT@MIL-125-NH 2 and free CAT, the CAT@Amino MIL-125-NH 2 displayed high activity recovery, good pH stability, stability against denaturants, and thermostability. Furthermore, activity recovery of CAT@Amino MIL-125-NH 2 was 56% higher than CAT@MIL-125-NH 2 . The CAT@Amino MIL-125-NH 2 still retained 50% residual activity for 14 days at room temperature, whereas free CAT lost activity after storage for 1 day at the same storage conditions. Furthermore, the CAT@Amino MIL-125-NH 2 maintained 62% of its initial activity after 4 consecutive uses, showing good reusability. The results showed that the amino functionalized MIL-125-NH 2 is an excellent carrier of enzyme immobilization.

研究领域: 生物化学 · 材料科学
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SCIENCE OF THE TOTAL ENVIRONMENT · 2021 · IF 7.963

ABTS as an electron shuttle to accelerate the degradation of diclofenac with horseradish peroxidase-catalyzed hydrogen peroxide oxidation

Yixin Huang,Jinbin Lin,Jing Zou,Jiaxin Xu,Mengyun Wang,Huahua Cai,Baoling Yuan,Jun Ma

Horseradish peroxidase (HRP)-catalyzed hydrogen peroxide (H 2 O 2 ) oxidation could degrade a variety of organic pollutants, but the intrinsic drawback of slow degradation rate limited its widespread application. In this study, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) was introduced into HRP/H 2 O 2 system as an electron shuttle to enhance diclofenac degradation under neutral pH conditions. The green-colored ABTS radical (ABTS •+ ), generated by the oxidation of ABTS with HRP-catalyzed H 2 O 2 oxidation, was proved to be the main reactive species for the rapid degradation of diclofenac in HRP/H 2 O 2 /ABTS system. There was no destruction of ABTS/ABTS •+ in HRP/H 2 O 2 /ABTS system, and ABTS was verified as an ideal electron shuttle. The reaction conditions including solution pH (4.5–10.5), HRP concentration (0–8 units mL −1 ) and H 2 O 2 concentration (0–500 μM) would impact the formation of ABTS •+ , and affect the degradation of diclofenac in HRP/H 2 O 2 /ABTS system. Moreover, compared with Fenton and hydroxylamine/Fenton systems, HRP/H 2 O 2 /ABTS system had better diclofenac degradation efficiency, higher H 2 O 2 utilization efficiency and stronger anti-interference capacity in actual waters. Overall, the present study provided a meaningful and promising way to enhance the degradation of organic pollutants in water with HRP-catalyzed H 2 O 2 oxidation.

研究领域: 环境科学 · 生物化学
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ENVIRONMENTAL SCIENCE AND POLLUTION RESEARCH · 2019 ·Vol. 27 ·期 20 ·24686-24691 · IF 2.914

Effects of carbendazim on catalase activity and related mechanism

Lu Guangqiu,Tan Wei,Li Guizhen,Yang Min,Wang Hongbin

The different techniques like spectroscopy and fluorescence quenching were used to study the interactive effect of carbendazim (CARB) and catalase (CAT) at the molecular level. The results showed that conditions were beneficial to the quenching mechanism at 25.0 °C, pH 7.0, while the binding constant k was 1.92 × 10 5 L mol −1 and the number of binding site was 1.0385. The thermodynamic parameters indicated that CARB could interact spontaneously with CAT to form a complex mainly by van der Waals’ interactions and hydrogen bonds. The interaction mechanism between CARB and CAT was that the effects of CARB on CAT in soil were activated and then restore stability. However, the effects of CARB on simple CAT were activated and then inhibited.

CAS / MDL: 9001-05-2
研究领域: 生物化学 · 环境科学
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Marine Drugs · 2017 ·Vol. 15 ·期 9 ·284 · IF 3.503

Construction of a Fluorescent H2O2 Biosensor with Chitosan 6-OH Immobilized β-Cyclodextrin Derivatives

Wenbo Dong,Weiping Li,Yu Chen,Yanchun Ye,Shaohua Jin

In the present work, a fluorescent H2O2biosensor was constructed by encapsulating fluorescent probe Rhodamine B (RhmB) in the hydrophobic cavity of the cyclodextrin (β-CD) and immobilizing catalase (CAT) on the 2-NH2of chitosan (CTS) in a chitosan 6-OH immobilized β-cyclodextrin derivative (CTS-6-CD). The inclusion complex of CTS-6-CD to RhmB (CTS-6-CD-RhmB) was prepared by a solution method. Its structure and inclusion efficiency were determined by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), and fluorescence spectroscopy (FL). CAT was immobilized on CTS-6-CD-RhmB to eventually form the functional membrane, CTS-6-CD-RhmB-CAT, via glutaraldehyde crosslinking, which was further characterized by FTIR and FL, and used as a H2O2biosensor. The functional membrane was used to simultaneously oxidize and detect H2O2. The detection condition was optimized as pH 8, a reaction temperature of 25 °C, and an immobilized enzyme concentration of 2 × 10−4mol/L. The fluorescence response of the biosensor exhibited a good linear relationship with the concentration of H2O2in the range of 20 mΜ–300 μM and the detection limit of 10−8mol/L.Keywords:chitosan;catalase;β-cyclodextrin;Rhodamine B;fluorescent biosensor

CAS / MDL: 9001-05-2
研究领域: 生物化学 · 分析化学
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LUMINESCENCE · 2022 ·Vol. 37 ·期 9 ·1547-1556 · IF 2.613

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Like Zhou,Hui Zhou,Huilong Xiao,Zihang Zhang,Ziyun Xiong,Xun Tuo,Hui Guo

Nifedipine (NDP), a dihydropyridine calcium antagonist, is widely used for the treatment of hypertension and angina pectoris. Catalase is a key antioxidant enzyme that is closely relevant to the level of reactive oxygen specie in vivo . Here, the research explored the effects of NDP on the conformation and catalytic function of bovine liver catalase (BLC) through enzymatic reaction kinetic techniques, multispectroscopic analysis, and computer simulation methods. Kinetic studies clarified that the NDP reduced the activity of BLC using a noncompetitive inhibition mechanism. Based on trial data, a static quenching mechanism functioned in quenching the intrinsic fluorescence of BLC. The binding constant value was (4.486 ± 0.008) × 10 4 M −1 (298 K) and BLC had one binding site for NDP. Tyr was prone to be exposed more to a hydrophilic environment in wake of a shift in fluorescence value. The binding reaction of BLC to NDP caused a conformational change in BLC, which in turn led to increase in the α-helix content and a decline in the β-sheet content. Furthermore, several amino acids residues interacted with NDP by means of van der Waals forces, whereas Gln397, Asn368, Gln371, Asn384, and Pro377 formed several hydrogen bonds with NDP.

CAS / MDL: 9001-05-2 21829-25-4
研究领域: 生物化学 · 药物学
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CATALYSIS COMMUNICATIONS · 2012 · IF 2.986

A facile method to prepare chemically crosslinked and efficient polyvinyl alcohol/chitosan beads for catalase immobilization

Jinjin Zang,Shaoyi Jia,Yong Liu,Songhai Wu,Yinbao Zhang

In this paper, polyvinyl alcohol (PVA) was modified with 3-aminopropyl triethoxysilane (APTES) and formed chemically crosslinked beads with chitosan. FTIR and SEM were used to characterize the support and immobilized catalase. Compared with control group, the activity of modified group increased about 1400   U/g support . The optimal temperature and optimal pH of immobilized catalase were 45   °C and pH 7.0. The thermal stability of catalase also enhanced after immobilization. Moreover, the immobilized catalase retained more than 90% of its original activity after using it for 9 times.

CAS / MDL: 919-30-2
研究领域: 生物化学 · 生物工程
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MATERIALS RESEARCH BULLETIN · 2014 · IF 1.968

Comprehensive studies on the nature of interaction between catalase and SiO2 nanoparticle

Yanqing Wang,Hongmei Zhang

The effect of SiO 2 nanoparticle on the conformation and activity of catalase were studied and observed by UV–vis, circular dichroism, fluorescence spectroscopy and molecular modeling methods. All the experimental data showed that the spectral changes of catalase were induced by SiO 2 nanoparticle exposure. SiO 2 nanoparticle could bind to catalase by electrostatic, hydrogen bonding and hydrophobic forces. These interactions decreased the α-helices content of catalase, which had more unfolded and more flexible structure. These structural changes did not obviously affect the solvent polarity of environment around both Trp and Tyr residues on catalase. Moreover, the activity assay indicated that SiO 2 nanoparticle was an activator for catalase activity. In a word, the biomolecular structure changes revealed by spectra provided a better understanding of the nanotoxicity and potential health effects of SiO 2 NP exposure.

CAS / MDL: 9001-05-2
研究领域: 生物化学 · 纳米毒理学 · 分子生物学
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SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY · 2025 · IF 4.6

Enhanced binding of triclocarban to catalase induced by coexisting nanoplastics

Qi Lou,Rongguang Shi,Rui Guan,Jing Lan,Yaoyao Wang,Yaru Li,Wansong Zong,Zongshan Zhao

Triclocarban (TCC), as an emerging environmental contaminant, can induce changes of catalase (CAT) activities and the oxidative stress. Nanoplastics have also been found to readily bind to functional proteins and affect their physiological expressions. However, their combined toxicities are still not clearly illustrated at molecule level. Here, we explored the impact of polystyrene nanoplastics (PSNPs) on the binding of TCC to CAT, using a combination of spectroscopy, enzyme activity assays, dynamic light scattering analysis and molecular docking. The results show that CAT activity was overactivated and increased to 131 % and 138 % (TCC = 6 μM) by TCC alone and NPs-TCC exposure, respectively. Dynamic light scattering analysis demonstrate that CAT was adsorbed on the surface of PSNPs and formed a protein corona. Fluorescence, UV–visible and circular dichroism spectra analyses reveal that loosening of the CAT backbone and the reduction in α-helix content induced by TCC was further exacerbated by PSNPs. This structural perturbation may enhance the binding affinity of TCC to CAT. The coexistence of PSNPs and TCC could further increase CAT activity compared to individual TCC, probably being attributed to protein corona formation and enhanced conformational changes of CAT induced by PSNPs. These findings will contribute to the understanding of the oxidative damage in the co-existence of TCC and PSNPs, and provide new insights into the toxic effects in coexisting scenarios.

CAS / MDL: 101-20-2
研究领域: 环境科学 · 生物化学
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Nanomaterials · 2025 ·Vol. 15 ·期 10 ·752 · IF 4.3

Preparation of g-C3N4/Co3O4/NS-CQDs Composite Materials and Their Application in the Detection of Hydrogen Peroxide and Glucose

Chang Feng,Yufeng Chen,Weie Wang,Yanan Niu,Xi Cao,Yuguang Lv

g-C3N4, a biocompatible material, has prominent applications in biology and is ideal for nano-enzyme studies. Though reported as a peroxidase mimic, its activity remains low. This group combined N,S-doped carbon quantum dots (NS-CQDs) with g-C3N4(7NSC-g), verifying its peroxidase-like activity. Based on this, a ternary composite of Co3O4in different forms and 7NSC-g was developed to enhance peroxidase activity, to design a g-C3N4-based composite enzyme. Characterizations determined the composition and morphology. Colorimetry evaluated peroxidase activity, where the simulated enzyme catalyzes blue product formation from the TMB substrate in the presence of H2O2. UV-Vis spectrophotometry measured absorbance changes to determine target concentrations. The results show Co3O4doping improves catalytic activity, with larger specific surface area providing more activation sites. The highest activity of g-C3N4/NS-CQDs/Co3O4was at 5% floral Co3O4, being efficient due to Co3O4’s electron-transfer acceleration and hydroxyl-radical mechanism. Under optimal conditions, the composite detected H2O2(10.0–230.0 μM, detection limit of 0.031 μM) and glucose (10.0–650.0 μM, detection limit of 1.024 μM).

研究领域: 生物化学 · 材料科学 · 医学检测
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ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY · 2021 ·Vol. 108 ·期 2 ·e21835 · IF 1.698

Molecular characterization of a catalase gene from the green peach aphid (Myzus persicae)

Mao-Ye Li,Yun Wang,Xiao Lei,Chuan-Tao Xu,Dong-Dong Wang,Su Liu,Shi-Guang Li

The green peach aphid, Myzus persicae (Sulzer), is a serious agricultural pest with a worldwide distribution. Catalase (CAT), which is encoded by the catalase ( Cat ) gene, is an extremely important antioxidant enzyme that plays a pivotal role in protecting cells against the toxic effects of hydrogen peroxide. The Cat gene has not been characterized in M. persicae ; therefore, this study describes the identification of the Cat ( MpCat ) gene from M. persicae . MpCat contains an open reading frame of 1515 bp and encodes a MpCAT protein consisting of 504 amino-acid residues. MpCAT possesses features typical of other insect catalases, including 7 conserved amino acids involved in binding heme and 15 involved in binding nicotinamide adenine dinucleotide phosphate. Phylogenetic analysis showed that MpCAT was closely related to orthologs from other aphid species. MpCat consisted of nine exons and eight introns, and the number and insertion sites of introns are consistent with those of Cat genes from Acyrthosiphon pisum (Harris) and Aphis gossypii Glover. The mRNA transcripts of MpCat were detected at all tested developmental stages, with the highest mRNA level in alate adults. The expression of MpCat was significantly upregulated when M. persicae was exposed to low and high temperatures, ultraviolet radiation, Beauveria bassiana , and permethrin. The transcription of MpCat and the activity of catalase were suppressed by RNA interference, and knockdown of MpCat significantly reduced the survival rate in M. persicae under heat stress. The results provide valuable information for further study on the physiological functions of MpCat . Research Highlights A catalase gene ( MpCat ) was characterized in Myzus persicae . Transcription of MpCat was responsive to various environmental stresses. Knockdown of MpCat increased mortality in M. persicae under heat stress.

CAS / MDL: 52645-53-1
研究领域: 昆虫学 · 分子生物学 · 遗传学
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