COLORATION TECHNOLOGY
·
2024
·
IF 2
Na-won Baek,Shin-hee Lee
Enzymatic dyeing is an environmentally friendly and energy-efficient dyeing method conducted at low temperatures, making it an important option for sustainable dyeing processing technology. This study investigated the enzymatic dyeing of cotton and silk fabrics using six phenolic monomers (catechol, hydroquinone, 2-aminophenol, 4-aminophenol, 1,4-phenylenediamine and 2,5-diaminobenzenesulphonic acid) via oxidative polymerisation catalysed by horseradish peroxidase (HRP). The research explored the colouring mechanism, functional attributes and dyeability of the fabrics. The polymerisation mechanism of the polymer was elucidated through liquid chromatography–tandem mass spectrometry, while the functional and morphological characteristics of the dyed fabric were examined via Fourier transform–infrared spectroscopy, thermogravimetric analysis and scanning electron microscopy imaging. The dyed fabric underwent dyeability assessments, including colour depth analysis and various fastness tests. Under mild reaction conditions, nearly all the phenolic monomers successfully dyed both the silk and cotton fabrics using HRP. The dyed fabrics demonstrated enhanced thermal stability and dyeability. However, the cotton fabrics exhibited worse dyeability and fastness than the silk fabrics, with noticeable stains on their surfaces when dyed with certain phenols. These findings underscore the suitability of enzymatic oxidative dyeing for protein fibres over vegetable fibres, as well as the importance of tailoring enzymatic dyeing processes for vegetable fibres.
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JOURNAL OF SURFACTANTS AND DETERGENTS
·
2022
·Vol. 25
·期 4
·477-486
·
IF 1.972
Jiuxia Wang,Meihuan Yao,Guangyue Bai,Junling Liu,Yujie Wang
Surfactants have a considerable potential for inhibiting horseradish peroxidase (HRP) activity; yet, more research is needed to understand the inhibition mechanism to allow for choosing the suitable surfactant candidate as inhibitor. In this study, three traditional surfactants, sodium dodecyl sulfate (SDS), N -dodecyltrimethyl ammonium bromide (DTAB) and N -dodecyldimethyl (3-sulfopropyl) ammonium hydroxide (SB3-12), that share the same (C 12 ) hydrophobic tail but possess different charged head groups, were taken as model surfactant inhibitors, and the enzymatic activity of HRP was assessed in these surfactant solutions. The activity of HRP was inhibited by both anionic SDS and cationic DTAB at dilute concentration even below their critical micelle concentration (cmc), and the electrostatic interaction of the ionic surfactants with some amino residues of HRP was mainly responsible for the inhibition of activity. HRP in a dilute solution of SB3-12, with the latter's concentration being below its cmc, retained a high level of enzymatic activity; but, at concentrations above the cmc of SB3-12, HRP was inhibited owing to the synergetic interaction of the SB3-12 micelle with HRP. Results from circular dichroism (CD) and intrinsic fluorescence spectroscopic analyses of HRP showed the unfolding of the tertiary structure around HRP's heme active site played a critical role in the inhibition, whereas the changes of HRP in the secondary structure and the tertiary structure near its tryptophan residue (Trp117) induced by these surfactants were minor for the inhibition. Based on the experimental results, a relationship between conformation and activity for HRP was suggested.
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COLLOIDS AND SURFACES B-BIOINTERFACES
·
2012
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IF 3.456
Qijin Wan,Hongtu Song,Hao Shu,Zhaohao Wang,Jing Zou,Nianjun Yang
In order to construct a three-dimensional electrode, in situ electrochemical deposition of gold nanoparticles onto a gold electrode coated with a self-assembled monolayer of 3-mercaptopropionic acid (Au NP/MPA/Au) was conducted. Horseradish peroxidase (HRP) was then immobilized into this three-dimensional electrode, leading to the realization of direct electron transfer of HRP. Scanning electron microscopy and electrochemical impedance spectroscopy were applied to characterize the electrode before and after HRP immobilization. The apparent Michaelis-Menten constant for immobilized HRP on a Au NP/MPA/Au electrode is 0.78 mM, indicating high enzymatic activity of HRP. The HRP modified electrode was further utilized as a sensing platform for the electrocatalytic reduction and detection of hydrogen peroxide. For the detection of hydrogen peroxide on this electrode, the sensitivity is 311.72 μA mM −1 cm −2 , the detection limit is 0.16 μM, and the dynamic range is from 0.48 μM to 1.2 mM. Therefore this electrode is a promising device for sensitive and reproducible detection of H 2 O 2 .
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高影响因子
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
·
2014
·
IF 2.745
Teng Zhang,Xiao-Ling Xu,Yi-Ning Jin,Jian Wu,Zhi-Kang Xu
Carbon nanotubes are widely applied in electronics, which offers great potential for enhancing the activity of redox enzyme. In this work, polyimide (PI) was blended with multiwalled carbon nanotubes (MWCNTs) and then electrospun into nanofibers for the immobilization of horseradish peroxidase (HRP), a redox enzyme. SEM and TEM were used to characterize the surface morphology of the PI/MWCNTs nanofibers and to analyze the protruding parts induced by the blending of MWCNT. The results indicate that, compared to the virgin PI nanofibers, the blending of MWCNTs increases the retention activity of immobilized HRP from 2.38% to 12.50%. Circular dichroism and UV–vis molecular absorption spectrometry were used to explore the interactions between HRP and MWCNTs . It seems that MWCNTs increase the enzyme activity by the facilitation of electron transfer among the catalytic intermediates “HRP I”, “HRP II” and MWCNTs.
研究领域:
生物化学
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纳米生物技术
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酶工程
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生物材料
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分析化学
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Biochar
·
2026
·Vol. 8
·期 1
·2
·
IF 13.5
Zhang Xueyan,Lv Shiyu,Yuan Tian,Fu Kerong,Yang Pu,Yao Yanpo,Liang Junfeng,Gao Tongguo,Wang Feng
Secretion and long-term accumulation of phenolic acid allelopathic substances are critical factors decreasing yield in continuous capsicum cropping systems. However, there are limited effective technologies and methods for removing these substances. In this study, biochar (BC) with ultrahigh specific surface area and pore volume was prepared via K 2 CO 3 etching, called carbonate-modified biochar (CBC). Then, it was loaded with horseradish peroxidase (HRP) under glutaraldehyde crosslinking conditions to form HRP–CBC. The maximum loading capacity of HRP reached 311.46 U g −1 . Under various factors, the degradation efficiency of allelopathic substances such as ferulic acid followed the order HRP–CBC > HRP–BC > HRP, indicating that the combination of alkaline etching and enzyme immobilization enhances ferulic acid degradation. At a HRP–CBC dose of 2 U mL −1 and pH 7, the degradation of 20 mg L −1 ferulic acid was achieved within 6 h. Furthermore, this method demonstrated excellent degradation performance against multiple phenolic acid compounds responsible for yield reduction in continuous chili pepper cropping systems. HRP–CBC exhibited superior stability, enhanced stress resistance, and broad application potential. The inhibitory effect of ferulic acid on chili seed germination disappeared after degradation by immobilized HRP. Liquid chromatography–mass spectrometry and ecotoxicity analyses confirmed that HRP–CBC degraded ferulic acid into less toxic small organic molecules through a free radical-mediated mechanism. Therefore, a modified biochar immobilized with HRP offers a promising strategy for removing phenolic acid allelopathic substances from continuous cropping systems. Graphical
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ChemSusChem
·
2023
·Vol. 16
·期 9
·e202202212
·
IF 8.4
Jianqiao Liu,Jin Qin,Shiquan Li,Kai Yan,Jingdong Zhang
Graphical See a little light : A biophotoelectrocatalytic system is designed to remove 4-nitrophenol (4-NP). The developed system is constructed with a Ag 3 PO 4 /BiVO 4 photoanode and a horseradish peroxidase (HRP)-loaded carbon cloth (CC) cathode. The Z-scheme Ag 3 PO 4 /BiVO 4 heterojunction enhances the separation efficiency of photogenerated carriers, which promotes the degradation of 4-NP under visible light irradiation. Photoelectrocatalysis (PEC) is regarded as a promising and sustainable process for removal of organic contaminants from wastewater. Meanwhile, enzymatic catalysis also provides an effective way to carry out polluted environment remediation under mild conditions. In this study, a biophotoelectrocatalytic (BPEC) system is designed to remove 4-nitrophenol (4-NP) based on a combination of PEC and enzymatic catalysis. The developed BPEC system is constructed with a Ag 3 PO 4 /BiVO 4 photoanode and a horseradish peroxidase (HRP)-loaded carbon cloth (CC) cathode. On the photoanode, the construction of a direct Z-scheme Ag 3 PO 4 /BiVO 4 heterojunction enhanced the separation efficiency of photogenerated carriers, which promoted the PEC degradation of 4-NP under visible light irradiation. After HRP was immobilized on the cathode, the degradation efficiency of 4-NP reached 97.1 % after 60 min PEC treatment. The result could be ascribed to the HRP-catalyzed oxidation reaction via in situ-generated H 2 O 2 from the CC cathode during the PEC process. Moreover, the possible degradation pathways of 4-NP in such a BPEC system are also discussed.
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Journal of Analytical Science and Technology
·
2021
·Vol. 12
·期 1
·1-9
·
IF 2.769
Dong Bin,Fan Qian,Li Ming,Huan Yanfu,Feng Guodong,Shan Hongyan,Fei Qiang
In this study, N-(4-aminobutyl)-N-ethylisoluminol (ABEI) was used as an energy donor, while sodium fluorescein was used as an enhancer and energy acceptor, which resulted in it producing resonance energy transfer and greatly increasing the strength of chemiluminiscence (CL). When horseradish peroxidase (HRP) is added, hydrogen peroxide (H2O2) will quickly separate into hydroxyl radicals (·OH) and superoxide ions (O2·−). If tyrosine (Tyr) is present in the system, the hydroxyl group on the benzene ring of Tyr robs ·OH and O2·− in the CL system, thereby reducing the intensity of CL. Based on this phenomenon, a luminescence system of ABEI and sodium fluorescein system was established to detect Tyr for the first time. This method has an ultra-low detection limit and a wide linear range, and is cheap and easy to operate. Under various optimal conditions, the linear range is from 3.0×10−8 to 3.0×10−5 mol/L, and the limit of detection is 2.4×10−8 mol/L. It has been successfully used in the detection of dairy products with satisfactory results.
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CHINESE JOURNAL OF ANALYTICAL CHEMISTRY
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2020
·
IF 0.936
Xing-Yu HOU,Yu-Kui TONG,Fu-Gui ZHU,Qin-Fei XIA,Miao-Miao TIAN
Graphene oxide (GO) is a two-dimensional atom-thick sheet generated from an oxidation of graphene. GO possesses a range of reactive oxygen functional groups on the basal planes and edges, which makes it a good candidate in the field of separation and enrichment through chemical functionalization. In this work, GO-based Fe 3 O 4 magnetic nanoparticles were prepared, and boronic acid groups were introduced by 3-aminophenylboronic acid (APBA) at the same time to improve the enrichment efficiency. Herein, the GO-based magnetic boronate-affinity adsorbent (Fe 3 O 4 @GO@APBA) was developed focusing on the specific capture of low abundance of glycoprotein. The composites gathered excellent characters of large specific surface area and biocompatibility of GO, strong magnetic responsiveness, and enhanced affinity properties of boronic acid. The proposed system showed better specificity for glycoprotein even in the presence of non-glycoproteins. As a result, the prepared Fe 3 O 4 @GO@APBA not only exhibited high selectivity for horseradish peroxidase (HRP), and an outstanding tolerance for interference, but also showed excellent rebinding rate for an extraction application. Furthermore, this method provided a reliable way to improve conventional magnetic adsorbent, and showed great potential in analysis of low-abundant glycoprotein from even complex samples.
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Biointerphases
·
2023
·Vol. 18
·期 4
·
IF 2.1
Wang Qi,Fu Hao,Qi Xiaoyu,Zhang Lei,Ma Hongyan
Horseradish peroxidase (HRP) is a hemoglobin composed of a single peptide chain that catalyzes the oxidation of various substrates such as phenol and aniline in the presence of hydrogen peroxide via its iron-porphyrin catalytic center. This enzyme is widely used in industrial phenol removal, food additives, biomedicine, and clinical test reagents due to its rapid reaction rate and obvious reaction outcomes. However, the large-scale use of HRP in industrial applications still faces numerous challenges, including activity, stability, and sustainability. This study demonstrates that when peroxidase is immobilized in zwitterionic polymer hydrogels, polycarboxybetaine (PCB) and polysulfobetaine (PSB), the properties of the enzyme are improved. PCB and PSB-embedded HRP exhibit a 6.11 and 1.53 times increase in Kcat/Km value, respectively, compared to the free enzyme. The immobilized enzyme also experiences increased activity over a range of temperatures and better tolerance to extreme p H and organic solvents, including formaldehyde. In addition, immobilized HRP exhibits excellent performance in storage and reproducibility. Remarkably, PCB-HRP still retains 80% of the initial activity after a 6-week storage period and can still attain the initial catalytic level of the free enzyme after six repeated cycles. It also removes 90% of phenol within 12 min, surpassing the current pharmacy on the market. These experimental results indicated that we have successfully designed a set of stable and efficient support substrates for horseradish peroxidase, which enhances its suitability for deployment in industrial applications.
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CHINESE CHEMICAL LETTERS
·
2017
·
IF 1.932
Meng Li,Xiang-Rong Huang,Yi Guo,Ya-Zhuo Shang,Hong-Lai Liu
The traditional surfactant sodium dodecyl sulfate (SDS) and ionic liquid 1-ethyl-3-methylimidazolium tetrafluoroborate ([Emim][BF 4 ]) have been combined to create a novel efficient medium for chromogenic catalysis of 3,3′,5,5′-tetramethylbenzidine with horseradish peroxidase in presence of H 2 O 2 . The results have shown the [Emim][BF 4 ] in the mediums can promote the rate of formation of the blue chromogen, the SDS is responsible for the stabilization of the blue chromogen due to the electrostatic attraction between positively charged blue chromogen and the negatively charged surfactant. The SDS/[Emim][BF 4 ] combination not only enhance catalytic activity of HRP remarkably but also stabilize the blue chromogen formed in the HRP oxidation of the substrate TMB compared to the conventional medium. Based on the superior combination of SDS and [Emim][BF 4 ], the colorimetric assay for detecting HRP activity and H 2 O 2 concentration was established. This work demonstrates a novel efficient medium for chromogenic catalysis with potential applications in biosensors and clinical diagnosis.
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CLEAN-Soil Air Water
·
2016
·Vol. 45
·期 2
·1600077
·
IF 1.716
Yong-Ming Lu,Qiao-Yue Yang,Li-Ming Wang,Ming-Zhu Zhang,Wen-Qiang Guo,Zheng-Nan Cai,Dan-Dan Wang,Wei-Wei Yang,Yan Chen
Nowadays it is still of great demand to find a feasible, inexpensive and green material for industrial enzyme immobilization for wastewater treatment. In this work, horseradish peroxidase (HRP) was successfully immobilized on glutaraldehyde activated carbon nanospheres. Compared with free HRP, the immobilized one showed better tolerance of temperature and pH. Meanwhile the storability and reusability were also greatly improved after immobilization. The immobilized HRP could be used for removal of several phenolic compounds from an aqueous solution and exhibited excellent removal efficiency, especially for chlorophenols, 4-methoxyphenol, and bisphenol A. The immobilization could also make the enzyme more tolerant of ions and preserve its bioactivity. Moreover, by the introduction of support-enzyme interaction a remarkably enhanced biodegradation was observed. The biodegradation of phenols with electron-donor groups were found to be doubled after immobilization on active carbon nanospheres. These findings might be useful for further construction of immobilized enzymes for industrial applications, which exhibit excellent stability together with high activity.
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FOOD CHEMISTRY
·
2017
·
IF 4.529
Bei Wang,Yanyan Zhang,Chandrasekar Venkitasamy,Bengang Wu,Zhongli Pan,Haile Ma
The objective of this research was to investigate the effects of pulsed light on the activity and structure of horseradish peroxidase in buffer solution. Enzyme residual activities were measured. Surface topography, secondary, and tertiary structures of horseradish peroxidase were determined using atomic force microscopy (AFM), Raman spectroscopy, and fluorescence spectroscopy, respectively. Results showed that a complete inactivation of horseradish peroxidase was achieved by application of 10 pulses of pulsed light treatment at an intensity of 500 J/pulse. The AFM analysis revealed that the aggregation of enzyme protein increased and surface roughness decreased with the increase in the treatment time. Fluorescence and Raman spectroscopy analysis exhibited that pulsed light destroyed the tertiary and secondary protein structures. The β-sheet composition was decreased while β-turn and random coils were increased. Pulsed light could effectively inactivate horseradish peroxidase by destroying the secondary and tertiary structures of protein in the active center of the enzyme.
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