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RISS 인기검색어
- 검색키워드
- 저자 : Shujing Ji, (검색결과 4 건)
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Qing Liu,Shujing Sun,Meizi Piao,Ji Young Yang 한국식품영양과학회 2013 Preventive Nutrition and Food Science Vol.18 No.4
Protease widely exists in the digestive tract of animals and humans, playing a very important role in protein digestion and absorption. In this study, a high protease-producing strain Planomicrobium sp. L-2 was isolated and identified from the digestive tract of Octopus variabilis. The strain was identified by physiological and biochemical experiments and 16S rDNA sequences analysis. A protease was obtained from the strain Planomicrobium sp. L-2 through ammonium sulfate precipitation, dialysis and enrichment, DEAE-Sephadex A50 anion-exchange chromatography, and Sephadex G-100 gel chromatography. The molecular weight and properties of the protease were characterized, including optimum temperature and pH, thermal stability, protease inhibitions and metal ions. According to our results, the protease from Planomicrobium sp. L-2 strain designated as F1-1 was obtained by three-step separation and purification from crude enzyme. The molecular weight of the protease was 61.4 kDa and its optimum temperature was 40℃. The protease F1-1 showed a broad pH profile for casein hydrolysis between 5.0∼11.0. No residual activity was observed after incubation for 40 min at 60℃ and 60 min at 50℃. F1-1 protease was inhibited by Mn<SUP>2+</SUP>, Hg<SUP>2+</SUP>, Pb<SUP>2+</SUP>, Zn<SUP>2+</SUP>, and Cu2+ ions, as well as PMSF, indicating that the protease F1-1 was a serine protease. Additionally, research basis provided by this study could be considered for industrial application of octopus intestinal proteases.
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Liu, Qing,Sun, Shujing,Piao, Meizi,Yang, Ji Young The Korean Society of Food Science and Nutrition 2013 Preventive Nutrition and Food Science Vol.18 No.4
Protease widely exists in the digestive tract of animals and humans, playing a very important role in protein digestion and absorption. In this study, a high protease-producing strain Planomicrobium sp. L-2 was isolated and identified from the digestive tract of Octopus variabilis. The strain was identified by physiological and biochemical experiments and 16S rDNA sequences analysis. A protease was obtained from the strain Planomicrobium sp. L-2 through ammonium sulfate precipitation, dialysis and enrichment, DEAE-Sephadex A50 anion-exchange chromatography, and Sephadex G-100 gel chromatography. The molecular weight and properties of the protease were characterized, including optimum temperature and pH, thermal stability, protease inhibitions and metal ions. According to our results, the protease from Planomicrobium sp. L-2 strain designated as F1-1 was obtained by three-step separation and purification from crude enzyme. The molecular weight of the protease was 61.4 kDa and its optimum temperature was $40^{\circ}C$. The protease F1-1 showed a broad pH profile for casein hydrolysis between 5.0~11.0. No residual activity was observed after incubation for 40 min at $60^{\circ}C$ and 60 min at $50^{\circ}C$. F1-1 protease was inhibited by $Mn^{2+}$, $Hg^{2+}$, $Pb^{2+}$, $Zn^{2+}$, and $Cu^{2+}$ ions, as well as PMSF, indicating that the protease F1-1 was a serine protease. Additionally, research basis provided by this study could be considered for industrial application of octopus intestinal proteases.
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Meng Sun,Penglei Cui,,Shujing Ji,,Ranxiao Tang,Qiuhua Wu,Chun Wang,Zhi Wang 대한화학회 2014 Bulletin of the Korean Chemical Society Vol.35 No.4
Octadecyl-modified graphene (graphene-C18) was fabricated and used as adsorbent in hollow fiber liquid phase microextraction (HF-LPME) for the first time. The extraction performance of graphene-C18 reinforced HF-LPME was evaluated using chlorophenols as model analytes. The factors affecting the extraction efficiency, such as extraction time, pH of the sample solution, agitation rate, the concentration of graphene-C18 and salt addition were optimized. After the graphene-C18 reinforced HF-LPME of the chlorophenols from honey sample, the analytes were separated and determined by high-performance liquid chromatography. The linearity was observed in the range of 5.0-200.0 ng g−1 for 2-chlorophenol and 3-chlorophenol, and 2.0-200.0 ng g−1 for 2,3-dichlorophenol and 3,4-dichlorophenol, respectively. The limits of detection (S/N = 3) of the method were lower than 1.5 ng g−1. The recoveries of the method were between 88% and 108%. The method is simple, sensitive and has been resoundingly applied to analysis of chlorophenols in honey samples.
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Sun, Meng,Cui, Penglei,Ji, Shujing,Tang, Ranxiao,Wu, Qiuhua,Wang, Chun,Wang, Zhi Korean Chemical Society 2014 Bulletin of the Korean Chemical Society Vol.35 No.4
Octadecyl-modified graphene (graphene-C18) was fabricated and used as adsorbent in hollow fiber liquid phase microextraction (HF-LPME) for the first time. The extraction performance of graphene-C18 reinforced HF-LPME was evaluated using chlorophenols as model analytes. The factors affecting the extraction efficiency, such as extraction time, pH of the sample solution, agitation rate, the concentration of graphene-C18 and salt addition were optimized. After the graphene-C18 reinforced HF-LPME of the chlorophenols from honey sample, the analytes were separated and determined by high-performance liquid chromatography. The linearity was observed in the range of 5.0-200.0 ng $g^{-1}$ for 2-chlorophenol and 3-chlorophenol, and 2.0-200.0 ng $g^{-1}$ for 2,3-dichlorophenol and 3,4-dichlorophenol, respectively. The limits of detection (S/N = 3) of the method were lower than 1.5 ng $g^{-1}$. The recoveries of the method were between 88% and 108%. The method is simple, sensitive and has been resoundingly applied to analysis of chlorophenols in honey samples.
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