Characterization of a thermophilic l-arabinose isomerase from Thermoanaerobacterium saccharolyticum NTOU1 |
| |
| Institution: | 1. Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan;2. Department of Chemical Engineering, National Taiwan University of Science and Technology, Taipei, Taiwan;3. Institute of Marine Biology, National Taiwan Ocean University, Keelung 20224, Taiwan;4. Institute of Bioscience and Biotechnology, National Taiwan Ocean University, Keelung 20224, Taiwan;5. Center of Excellence for Marine Bioenvironment and Biotechnology, National Taiwan Ocean University, Keelung 20224, Taiwan;1. Department of Biochemistry, P. D. Patel Institute of Applied Sciences, CHARUSAT, Changa, 388 421, Gujarat, India;2. Dr. K.C.Patel Research and Development Center, CHARUSAT, Changa, 388 421, Gujarat, India;1. State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing 211816, China;2. College of Food Science and Light Industry, Nanjing University of Technology, Nanjing 211816, China;3. School of Marine and Bioengineering, Yancheng Institute of Technology, Yancheng 224051, China;1. School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, Jiangsu, China;2. School of Medicine, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, Jiangsu, China;3. College of Biosciences and Biotechnology, Shenyang Agricultural University, 120 Dongling Road, Shenyang 110161, Liaoning, China;4. College of Science and Technology, Agricultural University of Hebei, 1 Bohai Road, Cangzhou 061100, Hebei, China;1. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, China;2. International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu, 214122, China;3. Synergetic Innovation Center of Food Safety and Quality Control of Jiangsu Province, Wuxi 214122, China;1. School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, Jiangsu, China;2. College of Biosciences and Biotechnology, Shenyang Agricultural University, 120 Dongling Road, Shenyang 110161, Liaoning, China;1. Cátedra de Bioquímica, Departamento de Biociencias, Facultad de Química, Universidad de la República, Avenida Gral. Flores 2124, CP 11800 Montevideo, Uruguay;2. Grupo de Ingeniería de Alimentos y Biotecnología, Instituto de Desarrollo Tecnológico para la Industria Química, Universidad Nacional del Litoral (UNL), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Colectora RN 168 Km 472 “Paraje El Pozo” S/N, S3000GLN Santa Fe, Argentina |
| |
| Abstract: | l-Arabinose isomerase (EC 5.3.1.4, l-AI) mainly catalyzes the reversible aldose–ketose isomerization between l-arabinose and l-ribulose. l-AIs can also catalyze other reactions, such as the conversion of d-galactose to d-tagatose. In this study, the araA gene encoding l-AI was PCR-cloned from Thermoanaerobacterium saccharolyticum NTOU1 and then expressed in Escherichia coli. The recombinant l-AI was purified from the cell-free extract using nickel nitrilotriacetic acid metal-affinity chromatography. The purified enzyme showed an optimal activity at 70 °C and pH 7–7.5. The enzyme was stable at pHs ranging from 6.5 to 9.5 and the activity was fully retained after 2 h incubation at 55–65 °C. The low concentrations of divalent metal ions, either 0.1 mM Mn2+ or 0.05 mM Co2+, could improve both catalytic activity and thermostability at higher temperatures. The recombinant T. saccharolyticum NTOU1 l-AI has the lowest demand for metal ions among all characterized thermophilic l-AIs. This thermophilic l-AI shows a potential to be used in industry to produce d-tagatose from d-galactose. |
| |
| Keywords: | Arabinose isomerase Bioconversion Recombinant DNA Enzyme activity Thermophiles |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
