Production and characterization of thermostable alpha-amylase from thermophilic Anoxybacillus flavithermus sp nov SO-19
| Autor: | Ozdemir, Sadin, Okumus, Veysi, Ulutas, Mehmet Sefa, Dundar, Abdurrahman, Akarsubasic, Alper Tunga, Dumontet, Stefano |
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| Přispěvatelé: | [Ozdemir, Sadin -- Okumus, Veysi -- Ulutas, Mehmet Sefa] Siirt Univ, Sci & Arts Fac, Dept Biol, TR-56100 Siirt, Turkey -- [Dundar, Abdurrahman] Mardin Artuklu Univ, Med Promot & Mkt Program, Vocat Higher Sch Hlth Serv, Mardin, Turkey -- [Akarsubasic, Alper Tunga] Istanbul Tech Univ, Dept Mol Biol & Genet, TR-34469 Istanbul, Turkey -- [Dumontet, Stefano] Parthenope Univ, Dept Environm Sci, Naples, Italy |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: | |
| Popis: | WOS: 000389311200025 This study was concerned with isolation and identification of thermophilic bacteria from hot spring in Afyonkarahisar (Gecek) and optimization of a-amylase production, partial purification of alpha-amylase, and characterization of extracellular enzyme from isolated thermophilic strain 19. To characterize and identify the thermophilic isolated bacteria, morphological analysis and biochemistry tests were studied. Besides, for classification 16S rRNA gene, G-C content and DNA-DNA hybridization analysis were performed. These results indicated that strain 19 is a novel species, Anoxybacillus flavithermus sp. nov. The effects of different fermentation conditions, such as incubation time, temperature, and pH, different carbon and nitrogen sources, and surfactants on a-amylase production were investigated. Various parameters such as temperature and temperature stability, pH and pH stability, detergents and surfactants, different starches, and metal ions on influence of enzyme characterization were assayed. About 93, 87, and 81% of the activities were retained after heating the partially purified enzyme solution at 50, 60, and 70 for 240 min, respectively. Enzyme was excessively inhibited by Hg2+ (6%). The enzyme was activated by Co2+ (212%) and Mg2+ (142%). Enzyme degradated 82% of starch content in apple juice at 70 degrees C in 30 min. The molecular weight of enzyme was estimated as 96 kDa. Scientific Research Projects Unit of Siirt University, Turkey [BAP-2011-SIUFED-F3] This study was supported by Scientific Research Projects Unit of Siirt University (project code: BAP-2011-SIUFED-F3), Turkey. |
| Databáze: | OpenAIRE |
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