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ndltd-OhioLink-oai-etd.ohiolink.edu-osu1313603839
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ndltd-OhioLink-oai-etd.ohiolink.edu-osu13136038392021-08-03T06:03:47Z Co-immobilization of thermostable Alpha-amylase and Glucoamylase for starch hydrolysis Dai, Zifei Starch is one of the most important carbon and renewable energy sources. Starch hydrolysis products, such as glucose, high fructose syrups or maltose are widely used in food industries. Also, the produced sugars can be fermented for bioethanol production. Starch hydrolysis involves large amount of enzymes consumption. The immobilization could recover enzymes and lower the production cost. A gel capsule system by dripping calcium chloride into a sodium alginate solution was developed for immobilization of recombinant glucoamylase (GA) by entrapment. Two types of starch hydrolysis enzymes, glucoamylase and alpha-amylase (AA), were co-immobilized inside and on the outside surface of calcium alginate gel capsules. A His6-tagged thermostable recombinant GA from Sulfolobus Solfataricus P2 was expressed, purified and characterized. The recombinant thermostable GA had an optimum pH and temperature range of 5-5.5 and 90-95°C respectively. The effects of cations and chemicals on the recombinant GA activity were also studied. Thermal stability and inactivation energy of the recombinant thermostable GA were determined with a half-time of 5.3 minutes at 95°C and 218 kJ/mol. GA from fungus (Aspergillus niger ) and AA from bacterial (Bacillus licheniformis) with low application temperature (50-65°C) were immobilized on the gel capsules by entrapment and adsorption. Then the optimum pH, temperature, reaction kinetics and reusability of the co-immobilized enzymes system were tested. The recombinant thermostable GA and a commercially available thermostable AA (Liquozyme X) were immobilized on the developed gel capsule. A co-immobilization method was developed by entrapping GA inside and covalently bounding AA on the surface of capsules. The reaction kinetics, thermostability and reusability of the thermostable co-immobilized AA and GA system were tested both in a batch reactor and with a continuous stirred tank reactor. 2011-09-26 English text The Ohio State University / OhioLINK http://rave.ohiolink.edu/etdc/view?acc_num=osu1313603839 http://rave.ohiolink.edu/etdc/view?acc_num=osu1313603839 unrestricted This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws.
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NDLTD
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| language |
English
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NDLTD
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| author |
Dai, Zifei
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| spellingShingle |
Dai, Zifei
Co-immobilization of thermostable Alpha-amylase and Glucoamylase for starch hydrolysis
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| author_facet |
Dai, Zifei
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| author_sort |
Dai, Zifei
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| title |
Co-immobilization of thermostable Alpha-amylase and Glucoamylase for starch hydrolysis
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| title_short |
Co-immobilization of thermostable Alpha-amylase and Glucoamylase for starch hydrolysis
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| title_full |
Co-immobilization of thermostable Alpha-amylase and Glucoamylase for starch hydrolysis
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| title_fullStr |
Co-immobilization of thermostable Alpha-amylase and Glucoamylase for starch hydrolysis
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| title_full_unstemmed |
Co-immobilization of thermostable Alpha-amylase and Glucoamylase for starch hydrolysis
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| title_sort |
co-immobilization of thermostable alpha-amylase and glucoamylase for starch hydrolysis
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| publisher |
The Ohio State University / OhioLINK
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| publishDate |
2011
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| url |
http://rave.ohiolink.edu/etdc/view?acc_num=osu1313603839
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| work_keys_str_mv |
AT daizifei coimmobilizationofthermostablealphaamylaseandglucoamylaseforstarchhydrolysis
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| _version_ |
1719430203128676352
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