INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2024
·
IF 7.7
Xiong Li,Chuyi Li,Wanzi Yao,Jian Mao
Carrageenan oligosaccharides have attracted significant attention due to their excellent biological activities, and they can be produced by carrageenases. In this study, a novel marine bacterium, Shewanella sp. LE8, was used to enzymatically degrade carrageenan, and the κ-, ι-, and λ-carrageenases produced by the bacterium were characterized. The crude enzyme derived from media exhibited κ-carrageenase activity, indicating its natural secretion during growth and proliferation. According to the results of molecular weight distribution from HPGPC, λ-carrageenan could be degraded by Shewanella sp. LE8 cells in both 20 mM Tris-HCl buffer and PBS, while ι-carrageenan can only be hydrolyzed in PBS environment, indicating the activation of ι-carrageenase in Shewanella sp. LE8 was dependent on the presence of Na + ions. The components of carrageenan hydrolysates were determined by ESIMS, and results revealed that κ-carrageenan hydrolysates were primarily consisted of G4S-DA, [G4S-DA] 2 and [G4S-DA] 3 , while ι-carrageenan hydrolysates were predominantly composed of [G4S-DA2S] 2 . Moreover, the fragment ions of λ-carrageenan revealed that the hydrolytic process not only encompasses enzymatic cleavage of glycosidic bonds but also involves the participation of sulfatase. The precise structure was further elucidated through NMR analysis, confirming that the end-products of ι-carrageenase were neoι-carratetraose. The results highlight the potential of Shewanella sp. LE8 for industrial applications in the production of ι-carrageenan oligosaccharides.
研究领域:
海洋生物学
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酶学
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生物化学
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DOI
PubMed
高影响因子
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES
·
2024
·
IF 2.8
Jun Zhang,Ze-hua Liu,Ke-meng Zhao,Zhi Dang,Yun Liu,Yu Liu
This work for the first time reported the complete transformation of 17β-estradiol (E2) to estrone (E1) by unknown wild-type enzyme present in the widely used commercial arylsulfatase derived from Helix pomatia . It was found that acetate could effectively inhibit the unknown enzyme with a half inhibitory concentration (IC 50 ) of 140.9 μM, while phosphate and citrate showed no inhibition. Since the buffer solutions with phosphate and citrate have been used in the enzymatic hydrolysis of natural estrogen conjugates for decades, the transformation of E2 to E1 likely occurred during such procedure, inevitably leading to overestimated E1, but underestimated E2. It was further suggested that acetate should be used to prevent this undesirable transformation during the enzymatic hydrolysis of natural estrogen conjugates.
研究领域:
生物化学
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环境科学
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医学
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DOI
PubMed
高影响因子
CHEMICAL RESEARCH IN TOXICOLOGY
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2019
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IF 3.274
Ruihong Li,Wei Li,Yutong You,Xiucai Guo,Ying Peng,Jiang Zheng
Aloe-emodin (AE) is a major anthraquinone ingredient of numerous traditional Chinese medicines with a variety of beneficial biological activities in vitro. Previous studies suggested that AE possessed cytotoxicity and genotoxicity. Nevertheless, the mechanisms of the toxic action of AE have not yet been fully clarified. The present study aimed at characterization of metabolic pathways of AE to better understand the mechanisms of AE-induced cytotoxicity. An AE-derived glutathione conjugate (AE-GSH) was observed in rat liver cytosol incubations containing AE and GSH, along with 3′-phosphoadenosine-5′-phosphosulfate (PAPS). Similar incubation fortified with N-acetylcysteine (NAC) in place of GSH offered an AE-NAC conjugate corresponding to the GSH conjugate. The formation of the two conjugates was found to require PAPS. The two conjugates were respectively detected in bile and urine of rats given AE. Sulfotransferase (SULT) inhibitor pentachlorophenol (PCP) suppressed the production of the observed AE-GSH/NAC conjugates in vivo, which suggested that SULTs participated in the process of the metabolic activation of AE. The presence of PCP attenuated cell susceptibility to AE-induced cytotoxicity. The present study illustrated potential association of sulfation-mediated bioactivation of AE with its cytotoxicity.
研究领域:
药理学
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毒理学
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生物化学
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DOI
PubMed
高影响因子
WATER ENVIRONMENT RESEARCH
·
2022
·Vol. 94
·期 4
·e10704
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IF 3.306
Ke-meng Zhao,Shu-shu Zhong,Jun Zhang,Cun-sheng Zhang,Zhi Dang,Ze-hua Liu
Arylsulfatase and β-glucuronidase are two important enzymes in wastewater and surface water, which play important roles on cleavage of sulfate/glucuronide estrogens. In this work, a high-performance liquid chromatography (HPLC)-based new method was firstly established for arylsulfatase/β-glucuronidase with determination of p-nitrophenyl sulfate ( p NPS)/p-nitrophenyl-β-D-glucuronide ( p NPG). The limits of detections (LODs) of the developed method for pNPS and pNPG were 0.164 and 0.098 μM, respectively. Intraday and interday reproducibility expressed as relative standard deviation (RSD) values of retention times and peak areas was 0.39%–3.68% and 0.23%–4.74%, respectively. The respective recovery efficiencies of this HPLC-based method spiking at three different concentrations for p-nitrophenol ( p NP), p NPS, and p NPG in activated sludge were 76.5%–88.1%, 79.2%–93.1%, and 84.2%–96.1%, with RSD below 3.9%. The HPLC-based method was finally applied to estimate the enzyme activity of arylsulfatase/β-glucuronidase in one activated sludge system and along which the classical spectrophotometric method was also evaluated. Compared with the classic spectrophotometric analytical method, the HPLC-based new method could simultaneously measure arylsulfatase/β-glucuronidase one time, which was convenient and time-saving. Moreover, the developed method could effectively avoid possible underestimation that the spectrophotometric method might encounter. Practitioner points A new HPLC-based method for activity estimation of arylsulfatase and β-glucuronidase was developed. The HPLC-based method can simultaneously estimate enzyme activity of both arylsulfatase and β-glucuronidase. The HPLC-based method can avoid possible underestimation that spectrophotometric method may encounter.
研究领域:
环境生物学
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生物化学
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分析化学
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DOI
PubMed
高影响因子
ENVIRONMENTAL SCIENCE AND POLLUTION RESEARCH
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2022
·Vol. 29
·期 42
·64244-64251
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IF 5.19
Zhao Ke-meng,Liu Ze-hua,Zhang Jun,Zhong Shu-shu,Dang Zhi
Arylsulfatase and β-glucuronidase are the two substantial enzymes having a significant role in the cleavage of conjugated natural estrogens (C-NEs). The present study reports that arylsulfatase and β-glucuronidase have been abundantly found in the digestive tracts of Cipangopaludina chinensis ; in which, their corresponding activities were 60 and 5 U/g wet waste, respectively. The arylsulfatase from Cipangopaludina chinensi s could show high activity at low temperatures. Hence, its activity still remained at 53.2% of maximal activity even at an extremely low temperature of 4 ℃; while the corresponding activities of arylsulfatase from Helix pomatia or activated sludge were less than 20% and 10%, respectively. The arylsulfatase and β-glucuronidase from Cipangopaludina chinensis could efficiently cleave C-NEs suggesting that they could be alternative enzymes derived from Helix pomatia that are used for cleavage of conjugated compounds in environmental or biological sample analysis. Meanwhile, they might also be used to enhance the cleavage of C-NEs in municipal wastewater.
研究领域:
环境生物学
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生物化学
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DOI
PubMed
高影响因子
ACS Omega
·
2025
·
IF 4.3
Songzhi Li,Yang Guo,Hong Jiang,Huan Zhang,Jiayu Li,Yanli Chen,Jie Li,Xiangzhao Mao,Minxiao Wang
Arylsulfatase catalyzes the cleavage of sulfate ester bonds and plays a role in agar desulfation, thereby enhancing agar gel strength and quality. While studying the desulfurization pathway in Pseudoalteromonassp. SR43-6, a sequence encoding a potential arylsulfatase─Pseudoalteromonas Ars (Ps-Ars)─was found. The enzyme, with p-nitrophenyl sulfate as a substrate, exhibited optimal activity at 35 °C and pH 8.0. Its relative activity (206 U/mg) exceeded that of the recently identified arylsulfatases. Four hundred units of the enzyme removed 86.4% of sulfate groups from Gelidium amansii agar in 4 h, whereas 800 U of the enzyme removed 71.3% of sulfate groups from Gracilaria lemaneiformis agar in 8 h. After enzymatic treatment, G. amansii agar gel strength was enhanced by 32%, and a similar improvement was observed in G. lemaneiformis agar gel strength. Enzymatic agar desulfurization offers mild, quality-retaining, and environmentally friendly advantages, augmenting industrial application prospects.
研究领域:
生物化学
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海洋微生物学
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食品科学
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DOI
PubMed
高影响因子
SCIENCE OF THE TOTAL ENVIRONMENT
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2019
·
IF 5.589
Jun Zhang,Ze-hua Liu,Shu-shu Zhong,Hao Wang,Bamu Caidan,Hua Yin,Zhi Dang
Arylsulfatase and β-glucuronidase are two important enzymes that are responsible for deconjugation of estrogen conjugates. It is important to keep estrogen conjugates intact during sample collection and storage, while the effective inhibition conditions for arylsulfatase and β-glucuronidase remain unknown. To elucidate these conditions, inhibition experiments were performed by adding several inhibitors or by introducing extreme pH conditions. This work confirms that arylsulfatase and β-glucuronidase can tolerate some extremes, including high concentrations of mercury dichloride , ethanol, and EDTA, while low pH (<3) or high pH (>11) can effectively inhibit their activities. The high tolerance of arylsulfatase and β-glucuronidase for mercury dichloride explains why estrogen conjugates in wastewater samples were deconjugated, even in the extremely unfavorable condition with a high concentration of mercury dichloride. Although low pH (<3) can effectively inhibit arylsulfatase/β-glucuronidase, deconjugation of sulfate conjugates by acid hydrolysis readily occurs; thus, a high pH of 11 is an appropriate storage condition for the effective inhibition of arylsulfatase/β-glucuronidase. This appropriate storage condition was confirmed and validated with diluted and sterilized activated sludge samples in which arylsulfatase/β-glucuronidase inhibition was effective for 48 h at room temperature and with a high pH of 11. The developed appropriate storage condition for effective inhibition of arylsulfatase/β-glucuronidase has wide application potential not only for estrogen conjugates but also for all conjugates of other organic micropollutants .
研究领域:
环境科学
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生物化学
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DOI
高影响因子
ENVIRONMENTAL SCIENCE AND POLLUTION RESEARCH
·
2022
·Vol. 29
·期 13
·19913-19917
·
IF 5.19
Zhang Jun,Zhong Shu-shu,Zhao Ke-meng,Liu Ze-hua,Dang Zhi,Liu Yu
Steroid arylsulfatase is an important enzyme in human, which plays an important role in dynamic equilibrium of natural estrogens. On the other hand, sulfite can be endogenously produced as a consequence of human body’s metabolism of sulfur-containing amino acids, while its main sources to human are mainly derived from food as it is a widely used additive. Sulfite-sensitivity is a well-known phenomenon to a small proportion of populations. However, its potential adverse effects on healthy individuals have been hardly reported. It was for the first time reported in this study that sulfite could effectively inhibit arylsulfatase, and its IC50 values for the snail- and human urine–derived arylsulfatase were determined to be 71.9 and 142.8 µM, which were lower than the concentration of sulfite in some healthy population. Consequently, it appears that sulfite might disrupt estrogen homeostasis in human, and this deserves further investigation.
研究领域:
生物化学
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毒理学
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内分泌学
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DOI
PubMed
高影响因子
ACS Sensors
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2019
·
IF 6.944
Hao-Hua Deng,Hua-Ping Peng,Kai-Yuan Huang,Shao-Bin He,Qiao-Feng Yuan,Zhen Lin,Rui-Ting Chen,Xing-Hua Xia,Wei Chen
In this study, on the basis of the biomineralization capability of urease, a facile, one-step, and green synthetic method has been proposed for the fabrication of gold nanoclusters (AuNCs). The prepared urease-encapsulated AuNCs (U-AuNCs) exhibited strong red fluorescence emission (λem = 630 nm) with a quantum yield as high as 17%. Interestingly, at a low concentration, the U-AuNC solution was found to be a dual-emissive system with the blue emission of the dityrosine (diTyr) residues of urease and the red emission of the embedded AuNCs. Further experiments demonstrated that p-nitrophenol (PNP) can selectively suppress the 410 nm emission of the diTyr residues of U-AuNCs without affecting the red emission of the U-AuNCs. The fluorescence quenching mechanism between U-AuNCs and PNP was systematically studied, and the leading role of the inner filter effect (IFE) was identified. Additionally, based on the sulfatase-catalyzed hydrolysis of p-nitrophenyl sulfate (PNPS) to release PNP, a self-referenced ratiometric detection method for sulfatase, which plays a crucial role in sulfur cycling, degradation of sulfated glycosaminoglycans and glycolipids, and extracellular remodeling of sulfated glycosaminoglycans, was developed by using dual-emissive U-AuNCs as the signal readout, in which the diTyr residues served as the probe and the AuNCs functioned as the internal reference. This IFE-based ratiometric sensing strategy showed a good linear relationship over the range of 0.01–1 U/mL (R2 = 0.997). The detection limit for sulfatase activity was 0.01 U/mL. The developed protocol was successfully used to detect sulfatase activity in human serum samples. The simplicity, rapidity, low cost, high credibility, good reproducibility, and excellent selectivity of the detection platform serve as an inspiration for further applications of fluorescent AuNCs in chemo/biosensing.
研究领域:
生物化学
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医学检测
·
纳米材料科学
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产品关联
DOI
PubMed
高影响因子
ACS Omega
·
2021
·
IF 3.512
Shu-shu Zhong,Jun Zhang,Ze-hua Liu,Zhi Dang,Yu Liu
Arylsulfatase and β-glucuronidase are two important enzymes in humans, which play an important role in the dynamic equilibrium of steroidal estrogens. This work probably for the first time reported that hydrogen peroxide (H2O2), hypochlorite, and peracetic acid (PAA) could effectively inhibit the activities of arylsulfatase and/or β-glucuronidase. The 50% of inhibitions (IC50) of H2O2, hypochlorite, and PAA on arylsulfatase were found to be 142.90 ± 9.00, 91.83 ± 10.01, and 43.46 ± 2.92 μM, respectively. The corresponding IC50 values of hypochlorite and PAA on β-glucuronidase were 704.90 ± 41.40 and 23.26 ± 0.82 μM, whereas H2O2 showed no inhibition on β-glucuronidase. The inhibitions of arylsulfatase and/or β-glucuronidase by these three chemicals were pH-dependent. It was further revealed that the inhibitions of hypochlorite on both arylsulfatase and β-glucuronidase were irreversible. On the contrary, the inhibitions by H2O2 and PAA were reversible. In addition, the inhibition by H2O2 was competitive and that by PAA was noncompetitive. In general, H2O2 and hypochlorite can be endogenously produced in humans, which suggested that the two compounds are potential endocrine disruption compounds (EDCs) as they can cause endocrine disruption via the inhibition of arylsulfatase and β-glucuronidase. This work further indicated that any agent that can induce the production of H2O2 or hypochlorite in humans is a potential EDC, which explains why some EDCs with very weak or no estrogenic potency can cause endocrine disruption, which is confirmed in epidemiological studies.
研究领域:
生物化学
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医学
·
环境健康科学
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DOI
PubMed
高影响因子
ENZYME AND MICROBIAL TECHNOLOGY
·
2021
·
IF 3.493
Xinqi Xu,Xiangzhen Deng,Juan Lin,Jie Yang
Arylsulfatase is useful in industrial agar processing by removing sulfate groups. A full-length arylsulfatase gene, designated ArySMA1, was obtained from marine bacteria Serratia sp. SM1. The ArySMA1 gene encoded a novel serine-type arylsulfatase and the enzymatic properties were characterized. The enzyme presented notable capacity of removing sulfate groups from natural algae substrates. Kinetic study suggested that the microscopic thermal inactivation rate of ArySMA1 in free form was smaller than that of the enzyme-substrate complex. The presence of substrate could unexpectedly accelerate ArySMA1 to deactivate at high temperature. Such phenomenon was opposite to many findings that substrate could stabilize enzymes against heat. Molecular dynamics simulation and ANS fluorescent assay indicated the substrate led the hydrophobic regions of the active site more flexible and the sulfate group of the substrate could retard the processivity of ArySMA1 catalysis. This study provides guidance for agar desulfation and down-stream processing industry.
研究领域:
酶学
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海洋生物技术
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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
SCIENCE OF THE TOTAL ENVIRONMENT
·
2024
·
IF 8.2
Jun Zhang,Ze-hua Liu,Jia-le Wu,Yu-ting Ding,Qing-guang Ma,Waseem Hayat,Yun Liu,Peng-jie Wang,Zhi Dang,Bruce Rittmann
Natural estrogen conjugates play important roles in municipal wastewater treatment plant (WWTP), but their deconjugation potentials are poorly understood. This work is the first to investigate the relationships between the enzyme activities of arylsulfatase/β-glucuronidase and deconjugation potentials of natural estrogen conjugates. This work led to three important findings. First, the enzyme activity of β-glucuronidase in sewage is far higher than that of arylsulfatase, while their corresponding activities in activated sludge were similar. Second, a model based on β-glucuronidase could successfully predict the deconjugation potentials of natural estrogen glucuronide conjugates in sewage. Third, the enzyme activity of arylsulfatase in sewage was too low to lead to evident deconjugation of sulfate conjugates, which means that the deconjugation rate of estrogen sulfates can be regarded as zero. By comparing their theoretical removal based on enzyme activity and on-site investigation, it is reasonable to conclude that reverse deconjugation of estrogen conjugates (i.e., conjugation of natural estrogens to form conjugated estrogens) likely exist in WWTP, which explains well why natural estrogen conjugates cannot be effectively removed in WWTP. Meanwhile, this work provides new insights how to improve the removal performance of WWTP on natural estrogen conjugates. Synopsis This work is the first to show how arylsulfatase/β-glucuronidase could affect deconjugation of natural estrogen conjugates and possible way to enhance their removal in wastewater treatment plant.
研究领域:
环境科学
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水处理
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生物技术
·
酶学
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DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）