Highly Efficient Synthesis of Fructooligosaccharides by Extracellular Fructooligosaccharide-Producing Enzymes and Immobilized Cells of Aspergillus aculeatus M105 and Purification and Biochemical Characterization of a Fructosyltransferase from the Fungus
| العنوان: | Highly Efficient Synthesis of Fructooligosaccharides by Extracellular Fructooligosaccharide-Producing Enzymes and Immobilized Cells of Aspergillus aculeatus M105 and Purification and Biochemical Characterization of a Fructosyltransferase from the Fungus |
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| المؤلفون: | Mei-Ping Huang, Jia-Xun Feng, De-Jiao Mo, Min Wu, Qiang-Sheng Xu |
| المصدر: | Journal of Agricultural and Food Chemistry. 64:6425-6432 |
| بيانات النشر: | American Chemical Society (ACS), 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0106 biological sciences, 0301 basic medicine, Oligosaccharides, 01 natural sciences, Mass Spectrometry, Fungal Proteins, 03 medical and health sciences, Hydrolysis, 010608 biotechnology, Extracellular, Enzyme kinetics, Cloning, Molecular, Chromatography, High Pressure Liquid, chemistry.chemical_classification, biology, Fructooligosaccharide, Aspergillus aculeatus, Aspergillus niger, Temperature, General Chemistry, Cells, Immobilized, Hydrogen-Ion Concentration, biology.organism_classification, Enzyme assay, Kinetics, Aspergillus, 030104 developmental biology, Enzyme, Hexosyltransferases, Biochemistry, chemistry, biology.protein, General Agricultural and Biological Sciences |
| الوصف: | In this work, Aspergillus aculeatus M105 was obtained to produce high extracellular fructooligosaccharide-producing enzyme activity. The maximum yields of fructooligosaccharides produced by its extracellular enzymes and immobilized cells were 67.54 and 65.47% (w/w), respectively. A fructosyltransferase (FTase), AaFT32A, was purified from M105. The optimal pH and temperature of AaFT32A were pH 5.0-6.0 and 65 °C, respectively. The Km, Vmax, and kcat values for the transfructosylating activity of AaFT32A were 2267 mM, 1347 μmol/min/mg protein, and 1550.2 s(-1), respectively, and those values for the hydrolytic activity of AaFT32A were 6.10 mM, 32.44 μmol/min/mg protein, and 37.3 s(-1), respectively. The sequence of AaFT32A deduced from the cloned gene shared 99.4% identity with a FTase from Aspergillus japonicus CB05 and a fructofuranosidase from Aspergillus niger and 96.5% identity with a FTase (Aspacl_37092) from A. aculeatus ATCC 16872. The fungal strain and its FTase may have potential applications in the prebiotics industry. |
| تدمد: | 1520-5118 0021-8561 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::026b80654805bfaa8345f59d6248eb6bTest https://doi.org/10.1021/acs.jafc.6b02115Test |
| رقم الانضمام: | edsair.doi.dedup.....026b80654805bfaa8345f59d6248eb6b |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15205118 00218561 |
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