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INDUSTRIAL CROPS AND PRODUCTS · 2025 · IF 6.2

Targeted regulation of hazardous substances from cigarette mainstream smoke based on the application of enzymes

Jie Hao,Xusong Wang,Liqun Li,Xuhui Huang,Na Wu,Tao Yu,Lu An,Lei Qin

The effect of exogenous enzyme treatment on hazardous substances and small-molecule compounds in smoke was investigated by treating Yunyan 87 tobacco with mesophilicα-amylase, pectinase, and lipase. The three enzymes could effectively diminish the total particulate matter (TPM) and nicotine-free dry particulate matter (NFDPM) content in smoke. Notably, mesophilicα-amylase demonstrated the most significant reduction, achieving a decrease of 8.15 % in TPM and 7.08 % in NFDPM content. The efficacy of these three enzymes in reducing phenol levels was remarkable, with a reduction exceeding 20 %. Pectinase and lipase exhibited superior performance in diminishing hydrogen cyanide (HCN) content, achieving a reduction of 13 %. The relative abundance of aroma-related and alkaloids compounds in smoke exhibited varying alterations after different enzyme treatments. The utilization of mesophilicα-amylase exhibited a favorable influence on the augmentation of aroma-related compounds, such as β-damascone and α-cyperone, whereas the effect of pectinase was opposite. The application of pectinase played a crucial role in the reduction of tobacco alkaloids and their related compounds. The occurrence of defects is unavoidable during the growth and curing process of tobacco leaves. Utilizing the characteristics of high efficiency and specificity of enzyme preparation for targeted modification of tobacco leaves is a viable method that can be tried to improve the quality of tobacco leaves.

研究领域: 生物学 · 医学 · 烟草科学
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2024 · IF 6

Metabolism and release of characteristic components and profiles of enzymatic activities during fermentation of Massa Medicata Fermentata

Luyu Shan,Jingjing Yang,Yaling Shi,Yalin Ye,Min Zhang,Ying Cui,Huijuan Yu,Yuefei Wang,Xin Chai

Various enzymes secreted by microorganisms during fermentation of Massa Medicata Fermentata (MMF) play a crucial role in conversion of the chemical substances for better clinical application. However, enzyme-driven transformation of chemical compounds during MMF fermentation has not been fully unveiled. Our findings revealed that MMF fermented with a mixture of wheat bran (WB)-flour (2:1) was observed with high enzymatic activities, alongside distinguished appearance. The activities of protease, ester bond hydrolase for cCGA and EF, and glycoside hydrolase all increased with the extended fermentation time of MMF, reaching 14.84×10 −8 ±0.3436×10 −8 , 0.05456×10 −8 ±0.0017×10 −8 , 0.5715×10 −8 ±0.1285×10 −8 , and 15.25×10 −8 ±0.01389×10 −8 Kat/g on the 8th day of fermentation. Moreover, protease has been proven to drive the conversion of WB proteins into amino acids by precolumn phenyl isothiocyanate derivatization. Besides, transformation patterns of ester bond hydrolase on substrate components were revealed, in which cryptochlorogenic acid was decomposed into caffeic acid and quinic acid, and ethyl ferulate was metabolized into ferulic acid. By glycoside hydrolase, amygdalin was transformed into prunasin and benzaldehyde. This study reveals the enzyme-mediated transformation patterns of the focused components during fermentation of MMF, laying foundation for further elucidation of its fermentation mechanism and elevation of quality control.

研究领域: 药理学 · 微生物学 · 生物化学 · 中医药
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TENSIDE SURFACTANTS DETERGENTS · 2020 ·Vol. 57 ·期 3 ·222-229 · IF 1.089

Washing Performance of Detergent Formulations with Sodium Oxalate as Builder in Presence of Different Enzymes

Chen Li,Hong Xu,Jinxiang Dong

In this work, we have investigated the washing performance of sodium oxalate-based detergents containing different enzymes (protease, lipase and cellulase). The results show that sodium oxalate-based detergents with enzymes have a better washing performance than formulations containing the conventional builder STPP and zeolite 4A. For sodium oxalate-based with protease, the amount of sodium oxalate and protease have a significant effect on the detergency. Lipase can improve detergency of sodium oxalate-based detergents after “first washing” in the presence of different anionic surfactant (LAS, MES and AES). For cellulase, only sodium oxalate in the presence of LAS has a detergency increase.

研究领域: 化学工程 · 生物技术
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ACS Nano · 2024 · IF 15.8

Surface Au–H Species as Self-Generated Prosthetic Groups of a Formate Dehydrogenase-like Au Nanozyme to Engineer Multienzymatic Activities

Xu Li,Wenlong Tan,Jinsong Fan,Kun Li

Although the past decade has witnessed a rapid development of oxidoreductase-mimicking nanozymes, the mimicry of cofactors that play key roles in mediating electron and proton transfer remains limited. This study explores how surface Au–H species conjugated to Au nanoparticles (NPs) that imitate formate dehydrogenase (FDH) can serve as cofactors, analogous to NADH in natural enzymes, offering diverse possibilities for FDH-mimicking Au nanozymes to mimic various enzymes. Once O2 is present, Au–H species assist Au NPs to complete the on-demand H2O2 generation for cascade reactions. Alternatively, when oxidizing organic molecules are introduced as substrates, Au–H species confer nitro reductase- and aldehyde reductase-like activities on Au NPs under anaerobic conditions. Furthermore, similar to the dehydrogenase–NADH complex, Au NPs possessing Au–H species are gifted with esterase-like activity for ester hydrolysis. By revealing that Au–H species are prosthetic groups for FDH-mimicking Au nanozymes, this work may inspire explorations into future self-generated cofactor mimics for nanozymes, thereby circumventing the need for exogenous cofactors.

CAS / MDL: 68-04-2
研究领域: 催化 · 生物化学 · 纳米技术 · 酶学
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SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY · 2024 · IF 4.3

Copper-based biomimetic nanozymes with multi-enzyme activity for phosphate detection

Zhendong Fu,TongJia Zhang,Cong Chen,Xiaoyu Wang,Liping Wang

Nanozymes are nanoparticles with enzymatic activity, which are widely used in environmental and antibacterial research. Herein, we designed and synthesized novel amorphous nanozyme Cu-Im NPs with multiple enzyme-mimicking activities. Cu-Im NPs have the same active sites as natural laccase. In addition, the active center is similar to that of carbonic hydrolase, replacing the zinc ions with copper ions. Meanwhile, Cu-Im NPs also possess peroxidase-like activity. We reveal the multi-enzyme catalytic mechanisms of Cu-Im NPs. Notably, phosphate inhibits the laccase-like and peroxidase-like activities of Cu-Im NPs while activating their hydrolase activity. Based on these findings, we have developed a sensitive and selective method for detecting phosphate anions.

研究领域: 生物化学 · 环境科学 · 纳米医学
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BIORESOURCE TECHNOLOGY · 2014 · IF 5.039

Synergism of cellulase, xylanase, and pectinase on hydrolyzing sugarcane bagasse resulting from different pretreatment technologies

Jingbo Li,Pengfei Zhou,Hongmei Liu,Chunjiang Xiong,Jianghai Lin,Wenjuan Xiao,Yingxue Gong,Zehuan Liu

Sugarcane bagasse (SCB) resulting from different pretreatments was hydrolyzed by enzyme cocktails based on replacement of cellulase (Celluclast 1.5 L:Novozym 188   =   1   FPU:4   pNPGU) by xylanase or pectinase at different proportions. Lignin content of NaOH pretreated SCB and hemicellulose content of H 2 SO 4 pretreated SCB were the lowest. NaOH pretreatment showed the best for monosaccharide production among the four pretreatments. Synergism was apparently observed between cellulase and xylanase for monosaccharide production from steam exploded SCB (SESB), NaOH, and H 2 O 2 pretreated SCB. No synergism was observed between cellulase and pectinase for producing glucose. Additionally, no synergism was present when H 2 SO 4 pretreated SCB was used. Replacement of 20% of the cellulase by xylanase enhanced the glucose yield by 6.6%, 8.8%, and 9.5% from SESB, NaOH, and H 2 O 2 pretreated SCB, respectively. Degree of synergism between cellulase and xylanase had positive relationship with xylan content and was affected by hydrolysis time.

研究领域: 生物化学 · 可再生能源 · 酶工程
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COLLOIDS AND SURFACES B-BIOINTERFACES · 2019 · IF 3.973

Controlled formation of porous CuCo2O4 nanorods with enhanced oxidase and catalase catalytic activities using bimetal-organic frameworks as templates

Dan Song,Ting Li,Yun-Yun Wei,Zhang-Run Xu

Porous structures with highly dispersed and active catalytic sites are vital to improve the catalytic activity and stability of artificial enzyme-related catalytic reactions. Herein, a novel nanorod-like bimetal-organic framework serving as porous support and supplier of Co 2+ and Cu 2+ was used to prepare a beneficial porous metal oxide. By optimizing the calcination temperature, the composition of calcined product can be controlled and the nanorods with isolated and highly active CuCo 2 O 4 nanoparticles were obtained. The porous CuCo 2 O 4 nanorods exhibit a pH-dependent catalytic property, that is, they behave as oxidase in acid conditions and catalase in alkaline conditions. The CuCo 2 O 4 nanorods perform dual-enzyme catalytic activity superior to monometallic oxides. What’s more, compared with the reported Co 3 O 4 nanoparticles, Co 3 O 4 /CuO hollow nanocage hybrids and NiCo 2 O 4 mesoporous spheres, the porous CuCo 2 O 4 nanorods show higher affinity to 3,3′,5,5′-tetramethylbenzidine with a lower K m value. The superior dual-enzyme catalytic activities of CuCo 2 O 4 nanorods benefit from the high catalytic activity of binary metal oxides and structural stability. After incubating in a wide range of pHs, temperatures and ionic strengths, the catalytic activity of CuCo 2 O 4 nanorods can be maintained. The oxidase activity of CuCo 2 O 4 nanorods can be inhibited in the presence of ascorbic acid, which can be applied in effective detection of ascorbic acid. This study opens a new path to prepare stable and highly active porous artificial enzymes.

CAS / MDL: 7722-84-1 54827-17-7
研究领域: 材料科学 · 生物催化 · 纳米技术
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ChemSusChem · 2025 · IF 6.6

Enzymatic Cleanup of Formaldehyde in Aqueous Solutions

Zhenyu Zhai,Yunjie Li,Zhilei Li,Jingting Wang,Yuan Li,Yi-Heng P. Job Zhang

Graphical Formaldehyde poses a significant threat to human health. We developed an enzymatic technique for the cleanup of formaldehyde in aqueous solutions. This technique utilized an enzyme cocktail, which catalyzed the reaction of formaldehyde and ambient dioxygen into carbon dioxide and water, with degradation ratios of up to 100 %. Numerous methods have been developed to address gaseous formaldehyde pollution, but most of them cannot be applied directly to eliminate the pollution of formaldehyde in aqueous solutions. Formaldehyde in aqueous solutions can be leached from formaldehyde-containing solid materials (e. g., food, wood, clothes, resins) and absorbed from gaseous formaldehyde by water. Here we developed an enzymatic cleanup technique — the reconstitution of an enzyme cocktail consisting of three coenzyme-free oxidoreductases (i. e., formaldehyde dismutase, methanol oxidase, and formate oxidase) and catalase for the complete oxidation of formaldehyde. This enzyme cocktail catalyzed the reaction of formaldehyde and ambient dioxygen into carbon dioxide (CO 2 ) and water, which was demonstrated by the stable isotope tracer technique. Significant levels of formaldehyde were detected from aqueous solutions leached from the squid, pomfret, fabric, and curtain in the market. When this enzyme cocktail was applied to treat the leachates of contaminated samples above, formaldehyde was eliminated with degradation ratios of up to 100 %. This enzymatic cleanup technique, featuring excellent biosafety (for example, degradable catalysts and non-immunogenicity), independence from light, high degradation ratios, and no special equipment required, could be widely used to treat contaminated food, drinking water, and formaldehyde-containing leachate.

CAS / MDL: 3228-27-1 9001-05-2
研究领域: 环境科学 · 生物化学 · 食品科学
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BIORESOURCE TECHNOLOGY · 2024 · IF 9.7

Investigating enhancement of protease and lysozyme combination pretreatment on hydrolysis of sludge organics under humic acid inhibition

Xiang Zou,Junguo He,Xinlei Pan,Qiupeng Cai,Shengye Duan,Yijie Zhong,Xinxin Cui,Jie Zhang

This study investigated the impact of humic acid (HA) on enzymatic pretreatment efficiency, focusing on sludge properties and HA molecular structure. The results showed that enzymatic pretreatment alleviates HA inhibition, improving hydrolysis efficiency. In the presence of HA, soluble proteins and polysaccharides in the enzyme-cocktail group reached 27.7 mg/L and 23.9 mg/L, 1.4 and 1.3 times higher than the blank group, respectively. The enzyme-cocktail group also had the highest soluble DNA concentration (19.4 mg/L) and the lowest viable cell proportion (69.3 %), indicating effective cell lysis. Enzyme-cocktail pretreatment reduced electrostatic repulsion, enhancing the mobility of extracellular organics. Enzyme interactions with HA released internal hydrolases and decreased amide groups on the HA surface, increasing the availability of biodegradable substrates. Overall, enzymatic pretreatment proves effective in mitigating HA-induced inhibition, thereby improving sludge biodegradation and enhancing carbon recovery in anaerobic fermentation.

CAS / MDL: 1415-93-6 9001-92-7
研究领域: 环境生物学 · 生物化学
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ACS Biomaterials Science & Engineering · 2019 · IF 4.511

Fe(III)-Tannic Acid Complex Derived Fe3C Decorated Carbon Nanofibers for Triple-Enzyme Mimetic Activity and Their Biosensing Application

Sihui Chen,Yixian Wang,Mengxiao Zhong,Dahai Yu,Ce Wang,Xiaofeng Lu

In the past decade, nanomaterials-based artificial enzymes have emerged as a hot spot in the field of catalysis. However, it is a significant challenge to fabricate functional nanomaterials for multiple-enzyme mimetic activity. In this work, we have presented an efficient catalytic platform to mimic peroxidase, oxidase, and catalase-like activity by Fe3C decorated carbon nanofibers (Fe3C/C NFs). First, polyacrylonitrile nanofibers (PAN NFs) are prepared via an electrospinning technique. Next, an Fe(III)-tannic acid (TA) complex is formed on the surface of PAN NFs through a wet chemical reaction. Finally, Fe3C/C NFs are obtained from the carbonization of the PAN/Fe(III)-TA complex nanofibers. The prepared Fe3C/C NFs show an excellent triple-enzyme mimetic property including peroxidase-like, oxidase-like, and catalase-like activity, which is investigated thoroughly by the colorimetric experiment of the 3,3′,5,5′-tetramethyl benzidine oxidation and the degradation of H2O2. Thanks to the superior catalytic performance of Fe3C/C NFs for oxidase mimicking, a facile and colorimetric way to determine glutathione with a high sensitivity and favorable selectivity has been achieved. This work provides an efficient platform for multiple-enzyme mimicking, which may expand their promising applications in biosensing, biomedicine, and environmental technology.

CAS / MDL: 67-68-5 100-21-0
研究领域: 材料科学 · 生物医学 · 环境科学
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APPLIED MICROBIOLOGY AND BIOTECHNOLOGY · 2019 ·Vol. 103 ·期 15 ·6333-6344 · IF 3.67

The substrate specificity of aniline dioxygenase is mainly determined by two of its components: glutamine synthetase-like enzyme and oxygenase

Ji Junbin,Zhang Ji,Liu Yongchuang,Zhang Yanting,Liu Yuanxin,Yan Xin

The residues of aniline and its derivatives are serious environment pollutants. Aniline dioxygenase (AD) derived from aerobic bacteria catalyzes the conversion of aniline to catechol, which has potential use in the bioremediation of aromatic amines and biorefining process. AD contains four components: a glutamine synthetase (GS)-like enzyme, a glutamine amidotransferase (GAT)-like enzyme, oxygenase, and reductase. ADs from diverse hosts exhibit different substrate specificities against aniline derivatives. However, what component of AD determines AD’s substrate specificity is still unknown which limits the effects of extending AD’s substrate spectrum through mutagenesis. Here, each component of two ADs (AtdA1A2A3A4A5 and AdoQTA1A2B) which have different substrate ranges was heterologously expressed and purified. The activity of both ADs was successfully constructed in vitro using the purified components. To identify the component that affects the substrate specificity of the ADs, the substrate specificity of each component was studied. The inability of AtdA1A2A3A4A5 to catalyze 4-methylaniline was determined with GS-like enzyme AtdA1; its inability to convert 2-isopropylaniline was caused by the oxygenase component, and its inability to convert 4-isopropylaniline was caused by both GS-like enzyme AtdA1 and oxygenase components. The inability of AdoQTA1A2B to catalyze 2-methylaniline was determined by GS-like enzyme AdoQ; its inability to convert 2-isopropylaniline was caused by both GS-like enzyme AdoQ and oxygenase components. Together, these results show that GS-like enzyme and oxygenase but not GAT-like enzyme or reductase play dominant roles in the substrate specificity of AD, and this finding will facilitate the engineering of AD to expand its substrate range.

研究领域: 环境科学 · 微生物学 · 分子生物学
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WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY · 2024 ·Vol. 41 ·期 1 ·1-12 · IF 4

Cloning, expression, and characterization of a heparinase III coupled with heparinase I for enzymatic depolymerization of heparin

Li Yang-Nan,Zhu Chen-Yuan,Xu Chen-Lu,Yu Shen,Huan Tong,Zhang Ye-Wang

A heparinase III ( Ns Hep-III) from Niabella sp . was identified, cloned, and expressed as soluble form in E. coli BL21 (DE3). With heparin as substrate, the maximum activity of Ns Hep-III of 90.0 U·mg − 1 was achieved at pH 7.1 Tris-HCl (containing 15 mM Mg 2+ ) and 30 o C. The half-life of Ns Hep-III was determined to be 5 h at 30 o C. The interactions between Ns Hep-III and substrates were studied by molecular docking. The combination of Ns Hep-III and a heparinase I from Bacteroides eggthii ( Be Hep-I) was employed to cleave heparin. Analysis of the enzymatic products of Ns Hep-III by SAX-HPLC showed seven different modified disaccharides, indicating that Ns Hep-III has a wide range of substrate specificity. The results of GPC analysis demonstrated that the average molecular weight of the product of heparin cleavage by the combination of Ns Hep-III/ Be Hep-I was reduced to 3969 Da, which accounted for 90% of all the components, and complied with the requirements of the European Pharmacopoeia. Ns Hep-III has notable activity and efficiency in cleaving heparin, which is potentially useful for the industrial production of low molecular weight heparin.

研究领域: 生物化学 · 药学
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