Purification and characterization of the amylolytic enzymes of Saccharomycopsis fibuligera |
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| Affiliation: | 1. Technische Universität Dresden, Institute of Process Engineering and Environmental Technology, 01062 Dresden, Germany;2. Åbo Akademi University, Laboratory of Industrial Chemistry and Reaction Engineering, 20500 Turku, Finland;1. Department of Medicinal Chemistry, School of Pharmacy, Health Science Center, Xi′an Jiaotong University, 76 West Yanta Road, Xi′an, Shaanxi, 710061, PR China;2. Henan Xibaikang Health Industry Co., Ltd, Jiyuan, Henan, 459006, PR China;1. The Heart Research Institute, 7 Eliza St, Newtown, NSW 2042, Australia;2. Sydney Medical School, University of Sydney, Sydney, NSW 2006, Australia;3. Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Blegdamsvej 3, Copenhagen N 2200, Denmark;4. University of Technology Sydney, Centre for Forensic Science, Ultimo, NSW 2007, Australia;5. School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia;1. College of Pharmaceutical Science and Institute of Drug Development and Chemical Biology, Zhejiang University of Technology, Hangzhou 310014, China;2. Department of Pharmacy, The First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Zhengzhou 450000, China;3. Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai 201210, China;4. Hangzhou Minsheng Institutes for Pharma Research, Hangzhou 311121, China |
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| Abstract: | - 1.1. A complex of extracellular amylolytic enzymes produced by Saccharomycopsis fibuligera KZ, grown on fine fibre (waste product from corn starch production) and corn-steep liquor, has been studied.
- 2.2. α-Amylases and glucoamylases, as the main representatives of this complex, were separated by hydrophobic chromatography on Spheron 300 LC.
- 3.3. Individual isoenzymes of one type were separated on FPLC-Mono Q.
- 4.4. The relative molecular weight of α-amylases is 54,000, glucoamylases 62,000, maximal activity is reached by both enzymes between pH 5.0 and 6.2 at a temperature of 40–50°C.
- 5.5. Glucoamylases have a higher stability of the native structure than α-amylases, they retain 55% of their original activity, even after 10 min of incubation at 100°C.
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