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1. A review: Inhibitors and activators for paraoxonase 1 | |||
Li Yan,Tang Meiling,Chen Gang,Mu Xiaojing,Huang Haiming | |||
Biology 23 April 2020 | |||
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Abstract:Paraoxonase 1 (PON1) is a calcium-dependent hydrolase with many physiological functions. The decrease of PON1 activity is related to many diseases. The research about PON1 is a hot topic, and its activators and inhibitors are expected to help in our diets and in choose of drugs. The papers about PON1 activators and inhibitors were collected and classified. The PON1 activators and inhibitors are grouped into four categories: in-vivo activators, in-vitro activators, in-vivo inhibitors and in-vitro inhibitors. For each activator or inhibitor, the activating effect or inhibiting effect along with the methods used was reviewed. Up to now, we found from literatures that there were 16 samples demonstrating activating effects on PON1 in-vivo and 5 compounds showed in-vitro activation. Of the 16 in-vivo activators there were 4 plant extracts and 12 pure components. Seven in-vivo inhibitors and 71 in-vitro inhibitors have been reported in publications. Additionally, smoking, drinking and treatment with exogenous gonadotropins induced decrease of PON1 activity. The summary of the activators and inhibitors are beneficial to reveal the structure-activity relationship, and also it provides convenience to look up the activating or inhibiting effects of the compounds on PON1 at a glance. | |||
TO cite this article:Li Yan,Tang Meiling,Chen Gang, et al. A review: Inhibitors and activators for paraoxonase 1[OL].[23 April 2020] http://en.paper.edu.cn/en_releasepaper/content/4751765 |
2. Overexpression, characterization, and dye-decolorizing ability of a thermostable, pH-stable, and organic solvent-tolerant laccase from Bacillus pumilus W3 | |||
GUAN Zhengbing,SONG Chenmeng,ZHANG Ning,LIAO Xiangru | |||
Biology 24 October 2013 | |||
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Abstract:Fungal laccases are typically unstable at high temperatures and alkaline conditions, thereby limiting their practical application. In this study, the novel laccase-producing Bacillus pumilus strain W3 was isolated from raw gallnut honey samples. The CotA-laccase gene was cloned from W3 and efficiently expressed by recombinant Escherichia coli in its biologically active form. The purified recombinant laccase had an extensive pH range for substrate catalysis. The enzyme was highly stable in alkaline pH and high temperatures, with considerable tolerance to NaCl and organic solvents. Laccase activity remained constant after 10 d of incubation at pH 9.0, whereas approximately 45% of the initial activity was detected after 10 h incubation at 80 C. Two azo dyes and two anthraquinonic dyes could be efficiently decolorized by purified laccase in the presence of a mediator under alkaline condition. More than 90% decolorization was observed at pH 9.0 after incubation for 5 h. These unusual properties indicated a high potential of the novel CotA-laccase for industrial application on decolorisation of textile dyeing effluent. | |||
TO cite this article:GUAN Zhengbing,SONG Chenmeng,ZHANG Ning, et al. Overexpression, characterization, and dye-decolorizing ability of a thermostable, pH-stable, and organic solvent-tolerant laccase from Bacillus pumilus W3[OL].[24 October 2013] http://en.paper.edu.cn/en_releasepaper/content/4565795 |
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