Characterization and properties of an inulinase from a thermophilic bacteria |
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| Institution: | 1. Division of Clinical Neuroscience, Chiba University Center for Forensic Mental Health, Chiba, Chiba 260-8670, Japan;2. Key Laboratory of Medical Electrophysiology of Ministry of Education and Medical Electrophysiological Key Laboratory of Sichuan Province, Collaborative Innovation Center for Prevention and Treatment of Cardiovascular Disease, Institute of Cardiovascular Research, Southwest Medical University, Luzhou, 646000, Sichuan, China;3. Department of Entomology and Nematology and UC Davis Comprehensive Cancer Center, University of California, Davis, CA 95616, United States;1. Universidad Autónoma de San Luis Potosí, Facultad de Estudios Profesionales Zona Huasteca, Ciudad Valles, San Luis Potosí, Mexico;2. Tecnológico Nacional de México Campus Instituto Tecnológico de Ciudad Valles, Ciudad Valles, San Luis Potosí, Mexico |
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| Abstract: | The inulinase of the thermophilic bacterial strain LCB41 (Bacillus sp.) was produced in fermentor using a mineral medium containing inulin as carbon source. The enzyme content was as high as the known inulinase producers and most of the activity was found in the culture medium. The enzyme was stable at high temperature and active at neutral and slightly basic pH. Fructose is liberated as the sole reaction product of inulin hydrolysis, classifying the enzyme as an exoinulinase. Inulin and sucrose were both hydrolyzed at appreciable rates with an (I/S) ratio of 0·40 and (Vm/Km)1/(Vm/Km)S = 9·9. The enzyme was less inhibited than yeast invertase or Kluyveromyces fragilis inulinase at high sucrose concentrations. The inulinase of strain LCB41 is a good candidate for industrial hydrolysis of inulin or sucrose. |
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