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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27156

Title: Characterization of the thermophilic isoamylase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
Authors: Tsuei-Yun Fang;Wen-Chi Tseng;Ching-Ju Yu;Tong-Yuan Shih
Contributors: NTOU:Department of Food Science
Keywords: Thermophilic;Isoamylase;Trehalose;Starch;Sulfolobus solfataricus;E. coli
Date: 2005-06-01
Issue Date: 2011-10-21T02:23:46Z
Publisher: Journal of Molecular Catalysis B: Enzymatic
Abstract: Abstract:Isoamylase catalyzes the hydrolysis of α-1,6-glucosidic linkages of starch and related polysaccharides. In this study, the treX gene (GenBank accession no. AE006815 REGION: 9279 … 11435) encoding the thermophilic isoamylase was PCR-cloned from the genomic DNA of Sulfolobus solfataricus ATCC 35092 to an expression vector with a T7lac promoter. Both wild-type and His-tagged isoamylases were expressed in Escherichia coli. The wild-type isoamylase was purified sequentially using heat treatment, nucleic acid precipitation, ion-exchange chromatography, and gel filtration chromatography while the His-tagged isoamylase was purified from the cell-free extract directly by metal chelating chromatography. Both enzymes were active only under their homo-trimer forms. In the absence of NaCl, both enzymes became inactive monomers. In addition, both enzymes were more stable when being stored at room temperature than at 4 °C. They had an apparent optimal pH of 5 and an optimal temperature at 75 °C. The enzyme activities remained unchanged after a 2 h incubation at 80 and 75 °C for the wild-type and His-tagged enzymes, respectively. These thermophilic isoamylases showed a potential to be used in industry to degrade the branching points of starch at a high temperature.
Relation: 33(3-6), pp.99–107
URI: http://ntour.ntou.edu.tw/handle/987654321/27156
Appears in Collections:[食品科學系] 期刊論文

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